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Conserved domains on  [gi|543966836|gb|ERJ73269|]
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putative gliding motility-associated lipoprotein GldK [Porphyromonas sp. oral taxon 278 str. W7784]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GldK super family cl42490
gliding motility-associated lipoprotein GldK; Members of this protein family are exclusive to ...
1-419 9.32e-97

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.


The actual alignment was detected with superfamily member TIGR03525:

Pssm-ID: 478238  Cd Length: 450  Bit Score: 297.16  E-value: 9.32e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836    1 MVHIPRGHIILGSELRDSLWGTPAVSRGISVEAFWMDRTEVTNAQYRQFVYYVRDSIIRERLA----------------- 63
Cdd:TIGR03525  41 MVLVPGGSFIMGKSDEDIAGVMNAPTKTVTVRSFYMDETEITNSEYRQFVEWVRDSIVRTKLAeladlagigpgdgggsi 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836   64 -DPAYGGDESYKITE-DKY-----------GEPVAPHLDWSRPIPSEKRASEEELRA--IQSVYYTN--PVTGERKLDPT 126
Cdd:TIGR03525 121 qDYAFKDAESDNATPyQKYmydnyyslgetDDYAGRKLNKKTELIWDTSEYPDEYYVevMDSLYLPEdeSYNGLRTFDVT 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  127 QLYYRYERYDHRAAAlwrnqlrSAQGnplwekerpeniqiskdtayidrsgqiiretitrpltSEYDFLNTYIVPVLPDE 206
Cdd:TIGR03525 201 KLKYRYSWMDIDAAA-------RSKG-------------------------------------SRKDFIKTEEVQVYPDT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  207 TVWVNDFPNSTNATYTAKYFNHPGYDDYPVVGVTWEQAQAYCAWRTAFYKKDLRLPEGQVVEEFRLPTEAEWEYAARMGN 286
Cdd:TIGR03525 237 TVWIKDFNYSYNEPMHNDYFWHQAYDDYPVVGVTWKQARAFCNWRTKYKNDFRKKKGPANVNTFRLPTEAEWEYAARGGL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  287 SKIVYPWGTEEVRSCDGCFLGNFKPGDGDYTADRHLITARVSSYPPNDFGLFDMAGNVAEWTSTAWISSGLRLISDVNPE 366
Cdd:TIGR03525 317 EGATYPWGGPYTKNDRGCFMANFKPVRGDYAADEALYTVEAKSYEPNDYGLYNMAGNVSEWTNSSYDPSSYEYMSTMNPN 396
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 543966836  367 LSYPADfkdsrdrTLKVVKGGSWKDIARNVQANNRSQAAQNAAHSYIGFRCVR 419
Cdd:TIGR03525 397 VNDSEN-------TRKVVRGGSWKDVAYFLQVSTRDYEYADSARSYIGFRTVQ 442
 
Name Accession Description Interval E-value
GldK TIGR03525
gliding motility-associated lipoprotein GldK; Members of this protein family are exclusive to ...
1-419 9.32e-97

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: 297.16  E-value: 9.32e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836    1 MVHIPRGHIILGSELRDSLWGTPAVSRGISVEAFWMDRTEVTNAQYRQFVYYVRDSIIRERLA----------------- 63
Cdd:TIGR03525  41 MVLVPGGSFIMGKSDEDIAGVMNAPTKTVTVRSFYMDETEITNSEYRQFVEWVRDSIVRTKLAeladlagigpgdgggsi 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836   64 -DPAYGGDESYKITE-DKY-----------GEPVAPHLDWSRPIPSEKRASEEELRA--IQSVYYTN--PVTGERKLDPT 126
Cdd:TIGR03525 121 qDYAFKDAESDNATPyQKYmydnyyslgetDDYAGRKLNKKTELIWDTSEYPDEYYVevMDSLYLPEdeSYNGLRTFDVT 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  127 QLYYRYERYDHRAAAlwrnqlrSAQGnplwekerpeniqiskdtayidrsgqiiretitrpltSEYDFLNTYIVPVLPDE 206
Cdd:TIGR03525 201 KLKYRYSWMDIDAAA-------RSKG-------------------------------------SRKDFIKTEEVQVYPDT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  207 TVWVNDFPNSTNATYTAKYFNHPGYDDYPVVGVTWEQAQAYCAWRTAFYKKDLRLPEGQVVEEFRLPTEAEWEYAARMGN 286
Cdd:TIGR03525 237 TVWIKDFNYSYNEPMHNDYFWHQAYDDYPVVGVTWKQARAFCNWRTKYKNDFRKKKGPANVNTFRLPTEAEWEYAARGGL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  287 SKIVYPWGTEEVRSCDGCFLGNFKPGDGDYTADRHLITARVSSYPPNDFGLFDMAGNVAEWTSTAWISSGLRLISDVNPE 366
Cdd:TIGR03525 317 EGATYPWGGPYTKNDRGCFMANFKPVRGDYAADEALYTVEAKSYEPNDYGLYNMAGNVSEWTNSSYDPSSYEYMSTMNPN 396
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 543966836  367 LSYPADfkdsrdrTLKVVKGGSWKDIARNVQANNRSQAAQNAAHSYIGFRCVR 419
Cdd:TIGR03525 397 VNDSEN-------TRKVVRGGSWKDVAYFLQVSTRDYEYADSARSYIGFRTVQ 442
YfmG COG1262
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain ...
225-421 1.39e-48

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: 165.56  E-value: 1.39e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836 225 YFNHPGYDDYPVVGVTWEQAQAYCAWRTAfykkdlrlpegQVVEEFRLPTEAEWEYAARMGNSKIvYPWGTEEVRScdgc 304
Cdd:COG1262   74 LYSDFGGPDHPVVHVSWYDAQAYCRWLGK-----------KTGKGYRLPTEAEWEYAARGGDGRP-YPWGDDLPPE---- 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836 305 fLGNFKPGDGdytadrHLITARVSSYPPNDFGLFDMAGNVAEWTSTAWissglrlisDVNPELSYPADFKDSRDRTLKVV 384
Cdd:COG1262  138 -LANYAGNDG------RGSTAPVGSFPPNPFGLYDMAGNVWEWTADWY---------DPPYPGAPADGPVGPENGGQRVL 201
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 543966836 385 KGGSWKDIARNVQANNRSQAAQNAAHSYIGFRCVRSA 421
Cdd:COG1262  202 RGGSWATPPDHLRSAYRNFFPPDARWQFVGFRLARDL 238
FGE-sulfatase pfam03781
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
202-419 6.43e-35

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: 129.93  E-value: 6.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  202 VLPDETVWVNDFPNSTNATYTAKYFNHPGYDDYPVVGVTWEQAQAYCAWRTAfykkdlrlpegQVVEEFRLPTEAEWEYA 281
Cdd:pfam03781  59 TTEVYPQWWAEVEGANWRHPSGGLSDIDDGADHPVTGVSWYDAVAYARWLGK-----------RTGNGYRLPTEAEWEYA 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  282 ARMGNSKIVYPWGTEEV---RSCDGCFLGNFKPGDGDYtadrHLITARVSSYPPNDFGLFDMAGNVAEWTSTAWISSGLR 358
Cdd:pfam03781 128 ARGGSKGRRYPWGDELYpagNIWQGADFPNEHAGADSF----NGRTSPVGSFPPNALGLYDMAGNVWEWTSDWYKPHYSF 203
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543966836  359 lisDVNPELSYPADFKDSRdrtlkVVKGGSWKDIARNVQ---ANNRSQAAQNAAHSYIGFRCVR 419
Cdd:pfam03781 204 ---APYDELSRDNFGGGYR-----VVRGGSWACSVYPSRlrpAFRGNCQTPGTRADDVGFRLVR 259
 
Name Accession Description Interval E-value
GldK TIGR03525
gliding motility-associated lipoprotein GldK; Members of this protein family are exclusive to ...
1-419 9.32e-97

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: 297.16  E-value: 9.32e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836    1 MVHIPRGHIILGSELRDSLWGTPAVSRGISVEAFWMDRTEVTNAQYRQFVYYVRDSIIRERLA----------------- 63
Cdd:TIGR03525  41 MVLVPGGSFIMGKSDEDIAGVMNAPTKTVTVRSFYMDETEITNSEYRQFVEWVRDSIVRTKLAeladlagigpgdgggsi 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836   64 -DPAYGGDESYKITE-DKY-----------GEPVAPHLDWSRPIPSEKRASEEELRA--IQSVYYTN--PVTGERKLDPT 126
Cdd:TIGR03525 121 qDYAFKDAESDNATPyQKYmydnyyslgetDDYAGRKLNKKTELIWDTSEYPDEYYVevMDSLYLPEdeSYNGLRTFDVT 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  127 QLYYRYERYDHRAAAlwrnqlrSAQGnplwekerpeniqiskdtayidrsgqiiretitrpltSEYDFLNTYIVPVLPDE 206
Cdd:TIGR03525 201 KLKYRYSWMDIDAAA-------RSKG-------------------------------------SRKDFIKTEEVQVYPDT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  207 TVWVNDFPNSTNATYTAKYFNHPGYDDYPVVGVTWEQAQAYCAWRTAFYKKDLRLPEGQVVEEFRLPTEAEWEYAARMGN 286
Cdd:TIGR03525 237 TVWIKDFNYSYNEPMHNDYFWHQAYDDYPVVGVTWKQARAFCNWRTKYKNDFRKKKGPANVNTFRLPTEAEWEYAARGGL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  287 SKIVYPWGTEEVRSCDGCFLGNFKPGDGDYTADRHLITARVSSYPPNDFGLFDMAGNVAEWTSTAWISSGLRLISDVNPE 366
Cdd:TIGR03525 317 EGATYPWGGPYTKNDRGCFMANFKPVRGDYAADEALYTVEAKSYEPNDYGLYNMAGNVSEWTNSSYDPSSYEYMSTMNPN 396
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 543966836  367 LSYPADfkdsrdrTLKVVKGGSWKDIARNVQANNRSQAAQNAAHSYIGFRCVR 419
Cdd:TIGR03525 397 VNDSEN-------TRKVVRGGSWKDVAYFLQVSTRDYEYADSARSYIGFRTVQ 442
GldK_short TIGR03529
gliding motility-associated lipoprotein GldK; Members of this protein family are exclusive to ...
187-418 6.25e-66

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: 214.40  E-value: 6.25e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  187 PLTSEYDFLNTYivpvlPDETVWVNDFPNSTNATYTAKYFNHPGYDDYPVVGVTWEQAQAYCAWRTaFYKKDLRLPEGQV 266
Cdd:TIGR03529 116 PLPPEYDMEELY-----PDTTVWSTSFSHHMGDPLMEYYFDHPAFDNYPVVGVDWNAAKQFCEWRT-YHMNAYRNEESQY 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  267 -VEEFRLPTEAEWEYAARMGNSKIVYPWGTEEVRSCDGCFLGNFKPGDGDYTADRHLITARVSSYPPNDFGLFDMAGNVA 345
Cdd:TIGR03529 190 dMPRFRLPSEAEWEYAARGGRDMAKYPWGGPYLRNKRGCMLANFKPGRGNYYDDGFPYTAPVAVYFPNDFGLYDMAGNVA 269
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543966836  346 EWTSTAWISSGLRLISDVNPELSYPADFKdsrdrtlKVVKGGSWKDIARNVQANNRSQAAQNAAHSYIGFRCV 418
Cdd:TIGR03529 270 EWVLDAYAATSVPIVWDLNPVYEDPNEVR-------KIIRGGSWKDIAYYLETGTRTFEYEDVSQAHIGFRTV 335
GldJ_short TIGR03530
gliding motility-associated lipoprotein GldJ; Members of this protein family are exclusive to ...
198-417 1.29e-49

gliding motility-associated lipoprotein GldJ; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldJ is a lipoprotein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae. Knockouts of GldJ abolish the gliding phenotype. GldJ is homologous to GldK. This model represents the GldJ homolog in Cytophaga hutchinsonii and several other species which is of shorter architecture than that found in Flavobacterium johnsoniae and is represented by a separate model (TIGR03524). 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: 132569  Cd Length: 402  Bit Score: 173.29  E-value: 1.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  198 YIVPVLPDETVWVNDFpnSTNATYTAKYFNHPGYDDYPVVGVTWEQAQAYCAWRT---------------AFYKKDLRLP 262
Cdd:TIGR03530 126 FIEKAEPDEDVWAGEL--AFNDLYQDHYFRFPGFNFFPVAGVNWIQANAYCIWRTevvnellaeeagidsPEGGGQIPIE 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  263 EGQVVEEFRLPTEAEWEYAAR--MGNS--------KIVYPWGTEEVRSC---------DGCFLGNFKPGDGDYTA----- 318
Cdd:TIGR03530 204 RGVALADFRLPNEAEWEYAAKalIGNQwldenqehGRIYPWDGHALRNPynvkrkgkqMGDFLANFKRGRGDYAGiagnk 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  319 --DRHLITARVSSYPPNDFGLFDMAGNVAEWTSTAWISSGLRLISDVNP---------ELSY-PADFKDSRDRTLKVVKG 386
Cdd:TIGR03530 284 lnDGAIIPTNIYDFAPNDFGLYCMAGNMNEWVYDVYRPLSFQDFDDLNPlrkdgffdeEEGYdKAGFQSLLDDEFRVYKG 363
                         250       260       270
                  ....*....|....*....|....*....|.
gi 543966836  387 GSWKDIARNVQANNRSQAAQNAAHSYIGFRC 417
Cdd:TIGR03530 364 GSWKDVAYWLSPGTRRFLAEDSATAAIGFRC 394
YfmG COG1262
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain ...
225-421 1.39e-48

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: 165.56  E-value: 1.39e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836 225 YFNHPGYDDYPVVGVTWEQAQAYCAWRTAfykkdlrlpegQVVEEFRLPTEAEWEYAARMGNSKIvYPWGTEEVRScdgc 304
Cdd:COG1262   74 LYSDFGGPDHPVVHVSWYDAQAYCRWLGK-----------KTGKGYRLPTEAEWEYAARGGDGRP-YPWGDDLPPE---- 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836 305 fLGNFKPGDGdytadrHLITARVSSYPPNDFGLFDMAGNVAEWTSTAWissglrlisDVNPELSYPADFKDSRDRTLKVV 384
Cdd:COG1262  138 -LANYAGNDG------RGSTAPVGSFPPNPFGLYDMAGNVWEWTADWY---------DPPYPGAPADGPVGPENGGQRVL 201
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 543966836 385 KGGSWKDIARNVQANNRSQAAQNAAHSYIGFRCVRSA 421
Cdd:COG1262  202 RGGSWATPPDHLRSAYRNFFPPDARWQFVGFRLARDL 238
FGE-sulfatase pfam03781
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
202-419 6.43e-35

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: 129.93  E-value: 6.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  202 VLPDETVWVNDFPNSTNATYTAKYFNHPGYDDYPVVGVTWEQAQAYCAWRTAfykkdlrlpegQVVEEFRLPTEAEWEYA 281
Cdd:pfam03781  59 TTEVYPQWWAEVEGANWRHPSGGLSDIDDGADHPVTGVSWYDAVAYARWLGK-----------RTGNGYRLPTEAEWEYA 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  282 ARMGNSKIVYPWGTEEV---RSCDGCFLGNFKPGDGDYtadrHLITARVSSYPPNDFGLFDMAGNVAEWTSTAWISSGLR 358
Cdd:pfam03781 128 ARGGSKGRRYPWGDELYpagNIWQGADFPNEHAGADSF----NGRTSPVGSFPPNALGLYDMAGNVWEWTSDWYKPHYSF 203
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543966836  359 lisDVNPELSYPADFKDSRdrtlkVVKGGSWKDIARNVQ---ANNRSQAAQNAAHSYIGFRCVR 419
Cdd:pfam03781 204 ---APYDELSRDNFGGGYR-----VVRGGSWACSVYPSRlrpAFRGNCQTPGTRADDVGFRLVR 259
GldJ TIGR03524
gliding motility-associated lipoprotein GldJ; Members of this protein family are exclusive to ...
190-422 1.20e-26

gliding motility-associated lipoprotein GldJ; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldJ is a lipoprotein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae. Knockouts of GldJ abolish the gliding phenotype. GldJ is homologous to GldK. There is a GldJ 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: 132563  Cd Length: 559  Bit Score: 111.97  E-value: 1.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  190 SEYDFLNTYiVPVLPDETVWVNDFPNstNATYTAKYFNHPGYDDYPVVGVTWEQAQAYCAWRT----------------- 252
Cdd:TIGR03524 120 SEANYKNIY-SGALPDTLVWRNRLGN--NETMTENYLRHPAYADYPVVGVSWIQAVEFSKWRTnrvnekvledkgnikkg 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  253 --------AFYKKDLRL------------------------------------------PEGQVVEEFRLPTEAEWEYAA 282
Cdd:TIGR03524 197 akidvtasSFFDTDVYLvdpsktyggdttvykrgigrtrrkkgearpavpeekdayqqrKDGIITQRYRLPTEAEWEYAA 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  283 R-----------MGNSKivYPWGTEEVRSCD----GCFLGNFKPGDGDY------TADRHLITARVSSYPPNDFGLFDMA 341
Cdd:TIGR03524 277 KanvgnreynnyRGRKK--YPWNGKYTRSKNrrnrGDQLANFKQGKGDYggiagwSDDGADITNEIKSYPPNDFGLYDMA 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  342 GNVAEWTSTAW------------------------------------------ISSGLRLISDVNPELSY-PAD------ 372
Cdd:TIGR03524 355 GNVAEWVADVYrpiidneandfnyyrgnlytknmidsdgnvvfagtqeieydtLPNGKVVARYLPGEIAQvPVDknetyl 434
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  373 ---------------------------------------------------------FKDSRDRT------LKVVKGGSW 389
Cdd:TIGR03524 435 rtnfsksdnanirdgdkqssryyefgddedeiarrpsmynspkspieidpvggmivlYDDDKKRTtliddrVRVYKGGSW 514
                         410       420       430
                  ....*....|....*....|....*....|...
gi 543966836  390 KDIARNVQANNRSQAAQNAAHSYIGFRCVRSAV 422
Cdd:TIGR03524 515 RDREYWLDPAQRRYLPQYMATDYIGFRCAMSRV 547
egtB_TIGR03440 TIGR03440
ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of ...
232-389 3.08e-11

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: 64.66  E-value: 3.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543966836  232 DDYPVVGVTWEQAQAYCAWRTAfykkdlrlpegqvveefRLPTEAEWEYAARMgnskivypwgteevrscdgcflgnfkp 311
Cdd:TIGR03440 269 PDAPVCHVSYYEADAYARWAGA-----------------RLPTEAEWEKAARW--------------------------- 304
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543966836  312 GDGDYTADRHLITARVSSYPPNDFGLFDMAGNVAEWTSTAWIS-SGLRLISDVNPElsYPADFKDsrdrTLKVVKGGSW 389
Cdd:TIGR03440 305 GDAPPNFAEANLGAPVGAYPAGAQGLGQLFGDVWEWTASPYEPyPGFRPPPGAYGE--YNGKFMD----GQMVLRGGSC 377
 
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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