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Conserved domains on  [gi|2794653958|ref|WP_372487318|]
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GTP 3',8-cyclase MoaA [Dermabacter vaginalis]

Protein Classification

GTP 3',8-cyclase MoaA( domain architecture ID 11458418)

GTP 3',8-cyclase MoaA catalyzes, together with MoaC, the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
28-409 2.16e-170

GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and metabolism]; GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) is part of the Pathway/BioSystem: Molybdopterin biosynthesis


:

Pssm-ID: 442141 [Multi-domain]  Cd Length: 329  Bit Score: 479.56  E-value: 2.16e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  28 TGALLDTYGRTATDLRVSLTDFCNLRCTYCMPEAGLQFLKKPQLMSVDEIARFVRIGVEnLGIREVRFTGGEPLTRADLP 107
Cdd:COG2896     2 TSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQFLPKEELLSFEEIERLVRAFVE-LGVRKIRLTGGEPLLRKDLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 108 DIIESVAGLSPRPDISLTTNAIGLEKRAETLVAAGLDRLNISLDSAHSETFEAMTRRPFLHRVLQGIDAARDAGLSPIKI 187
Cdd:COG2896    81 ELIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 188 NAVLQPGANEHEAAELLAWCLERGLELRFIEYMPLDGAGRWNRERMVTASDVWQLLSPYYVMHPVrEARGGAPAEKFDVw 267
Cdd:COG2896   161 NAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAAEILERLEARFPLEPL-PARGGGPARYYRV- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 268 prpgsasPGAPGTIagvlkergidpantdavrsilppapgkpfaeagerpheqalgtvGIIASVTRPFCADCTRTRLTAE 347
Cdd:COG2896   239 -------PGGGGRI--------------------------------------------GFISPVSHPFCGSCNRLRLTAD 267
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794653958 348 GRVRTCLFSHSETDLLGLMRQGASDEAIAERWRAAQWGKQAGHGMDRSDFVQPERPMSAIGG 409
Cdd:COG2896   268 GKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGHGFDEGDFPQPKRSMSAIGG 329
 
Name Accession Description Interval E-value
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
28-409 2.16e-170

GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and metabolism]; GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 442141 [Multi-domain]  Cd Length: 329  Bit Score: 479.56  E-value: 2.16e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  28 TGALLDTYGRTATDLRVSLTDFCNLRCTYCMPEAGLQFLKKPQLMSVDEIARFVRIGVEnLGIREVRFTGGEPLTRADLP 107
Cdd:COG2896     2 TSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQFLPKEELLSFEEIERLVRAFVE-LGVRKIRLTGGEPLLRKDLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 108 DIIESVAGLSPRPDISLTTNAIGLEKRAETLVAAGLDRLNISLDSAHSETFEAMTRRPFLHRVLQGIDAARDAGLSPIKI 187
Cdd:COG2896    81 ELIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 188 NAVLQPGANEHEAAELLAWCLERGLELRFIEYMPLDGAGRWNRERMVTASDVWQLLSPYYVMHPVrEARGGAPAEKFDVw 267
Cdd:COG2896   161 NAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAAEILERLEARFPLEPL-PARGGGPARYYRV- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 268 prpgsasPGAPGTIagvlkergidpantdavrsilppapgkpfaeagerpheqalgtvGIIASVTRPFCADCTRTRLTAE 347
Cdd:COG2896   239 -------PGGGGRI--------------------------------------------GFISPVSHPFCGSCNRLRLTAD 267
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794653958 348 GRVRTCLFSHSETDLLGLMRQGASDEAIAERWRAAQWGKQAGHGMDRSDFVQPERPMSAIGG 409
Cdd:COG2896   268 GKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGHGFDEGDFPQPKRSMSAIGG 329
moaA PRK00164
GTP 3',8-cyclase MoaA;
24-409 5.20e-163

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 460.76  E-value: 5.20e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  24 GRPATGALLDTYGRTATDLRVSLTDFCNLRCTYCMPEAGLQFLKKPQLMSVDEIARFVRIGVEnLGIREVRFTGGEPLTR 103
Cdd:PRK00164    1 PVPMTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPFLPKEELLSLEEIERLVRAFVA-LGVRKVRLTGGEPLLR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 104 ADLPDIIESVAGLSPRPDISLTTNAIGLEKRAETLVAAGLDRLNISLDSAHSETFEAMTRRPFLHRVLQGIDAARDAGLS 183
Cdd:PRK00164   80 KDLEDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 184 PIKINAVLQPGANEHEAAELLAWCLERGLELRFIEYMPLDGAGRWNRERMVTASDVWQLLSP-YYVMHPvrEARGGAPAE 262
Cdd:PRK00164  160 PVKVNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAEIRARLAErGWTLQP--RARSGGPAQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 263 KFdvwprpgsaspgapgtiagvlkergidpantdavrsilppapgkpfaeagerPHEQALGTVGIIASVTRPFCADCTRT 342
Cdd:PRK00164  238 YF----------------------------------------------------RHPDYGGEIGLIAPVTHDFCASCNRL 265
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2794653958 343 RLTAEGRVRTCLFSHSETDLLGLMRQGASDEAIAERWRAAQWGKQAGHGMDRSDfVQPERPMSAIGG 409
Cdd:PRK00164  266 RLTADGKLHLCLFAEDGVDLRDLLRSGADDEELAAAIREALQNKPEGHGLHDGN-TGPTRHMSYIGG 331
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
31-409 6.25e-130

molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes molybdenum cofactor biosynthesis protein A, or MoaA, as found in bacteria. It does not include the family of probable functional equivalent proteins from the archaea. MoaA works together with MoaC to synthesize precursor Z from guanine. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274250 [Multi-domain]  Cd Length: 334  Bit Score: 376.95  E-value: 6.25e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  31 LLDTYGRTATDLRVSLTDFCNLRCTYCMPE-AGLQFLKKPQLMSVDEIARFVRIGVEnLGIREVRFTGGEPLTRADLPDI 109
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEgGGLDFLPKEELLTFEEIERLVRAFVG-LGVRKVRLTGGEPLLRKDLVEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 110 IESVAGLSPRPDISLTTNAIGLEKRAETLVAAGLDRLNISLDSAHSETFEAMTRRPF-LHRVLQGIDAARDAGLSPIKIN 188
Cdd:TIGR02666  80 VARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGrLEQVLAGIDAALAAGLEPVKLN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 189 AVLQPGANEHEAAELLAWCLERGLELRFIEYMPLDGAGRWNRERMVTASDVWQLLSPYYV-MHPVREARGGAPAEkfdvw 267
Cdd:TIGR02666 160 TVVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGWREKKFVSADEILERLEQAFGpLEPVPSPRGNGPAP----- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 268 prpgSASPGAPGtiagvlkergidpantdavrsilppapgkpfaeagerpheqALGTVGIIASVTRPFCADCTRTRLTAE 347
Cdd:TIGR02666 235 ----AYRWRLPG-----------------------------------------GKGRIGFISPVSDPFCGTCNRLRLTAD 269
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2794653958 348 GRVRTCLFSHSETDLLGLMRQGASDEAIAERWRAAQWGKQAGHGMDRSD---FVQPERPMSAIGG 409
Cdd:TIGR02666 270 GKLRLCLFADDGVDLRPLLRGGASDALLEAIIQAILQKKPEGHSFLRFTspaNKRRKRAMSQIGG 334
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
212-390 1.12e-35

Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. Mutations in this region of Swiss:O14940 cause MOCOD (Molybdenum Co-Factor Deficiency) type A.


Pssm-ID: 428955 [Multi-domain]  Cd Length: 127  Bit Score: 127.33  E-value: 1.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 212 LELRFIEYMPLDGAGRWNRERMVTASDVWQLLSPYYVMHPVReARGGAPAEKFdvwprpgsaspgapgTIAGvlkergid 291
Cdd:pfam06463   1 IDLRFIELMPVGEGNGWRRKKFVSLDEILERIEARFPLLPAR-KRTGGPAKRY---------------RIPG-------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 292 pantdavrsilppapgkpfaeagerpheqALGTVGIIASVTRPFCADCTRTRLTAEGRVRTCLFSHSETDLLGLMRQGAS 371
Cdd:pfam06463  57 -----------------------------GGGRIGFIAPVSNPFCASCNRLRLTADGKLKTCLFAEDGIDLRDALRSGDD 107
                         170
                  ....*....|....*....
gi 2794653958 372 DEAIAERWRAAQWGKQAGH 390
Cdd:pfam06463 108 DEELREAIREALARKPPRH 126
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
331-400 6.58e-25

Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding Twitch domain is found at the C-terminus of GTP 3',8-cyclase (EC 4.1.99.22), which is also called molybdenum cofactor biosynthesis protein A (MoaA) in bacteria and archaea, molybdenum cofactor biosynthesis protein 1 (MOCS1) in most eukaryotes, and molybdenum cofactor biosynthesis enzyme CNX2 in plants. GTP 3',8-cyclase is a radical S-adenosylmethionine (SAM) enzyme that catalyzes the first step in molybdopterin biosynthesis, the cyclization of guanosine triphosphate to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate, which is then converted to molybdopterin in subsequent steps. Radical SAM enzymes are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster that is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical, which in turn abstracts a hydrogen from the appropriately positioned carbon atom of the substrate. GTP 3',8-cyclase contains an additional iron-sulfur cluster at the C-terminal Twitch domain that is involved in substrate binding. The Twitch domain may be related to another iron-sulfur cluster-binding domain found at the C-terminus of some radical SAM enzymes, the SPASM domain, named after the biochemically characterized members, AlbA, PqqE, anSMEs, and MftC, which are involved in Subtilosin A, Pyrroloquinoline quinone, Anaerobic Sulfatase, and Mycofactocin maturation, respectively.


Pssm-ID: 411052 [Multi-domain]  Cd Length: 70  Bit Score: 96.84  E-value: 6.58e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 331 VTRPFCADCTRTRLTAEGRVRTCLFSHSETDLLGLMRQGASDEAIAERWRAAQWGKQAGHGMDRSDFVQP 400
Cdd:cd21117     1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGASDEELREAIRAAVQRKPERHSLERGDSGTR 70
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
44-243 1.20e-19

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 86.69  E-value: 1.20e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958   44 VSLTDFCNLRCTYCMPEAGLQFLKKPQLMSV-DEIARFVRIGVENLGIREVRFTGGEP--LTRADLPDIIESVA---GLS 117
Cdd:smart00729   5 YIITRGCPRRCTFCSFPSLRGKLRSRYLEALvREIELLAEKGEKEGLVGTVFIGGGTPtlLSPEQLEELLEAIReilGLA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  118 PRPDISLTTNAIGL-EKRAETLVAAGLDRLNISLDSAHSETFEAMTRRPFLHRVLQGIDAARDAGlsPIKINAVL---QP 193
Cdd:smart00729  85 KDVEITIETRPDTLtEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAG--PIKVSTDLivgLP 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2794653958  194 GANEHEAAELLAWCLERGLE-LRFIEYMPLDG---AGRWNRERMVTASDVWQLL 243
Cdd:smart00729 163 GETEEDFEETLKLLKELGPDrVSIFPLSPRPGtplAKMYKRLKPPTKEERAELL 216
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
41-217 3.85e-05

twitch domain-containing radical SAM protein; Members of this family are unusual among radical SAM proteins in several ways. First, the N-terminal region consists of an iron-sulfur cluster-binding twitch domain (half of a SPASM domain), something usually found C-terminal to the radical SAM domain. Second, the radical SAM domains in many of the members of this family score poorly vs. the Pfam HMM, PF04055 (version 19), used to identify radical SAM. Lastly, the majority of members sequenced to date come from uncultured bacteria from marine or aquifer sources rather than from conventionally cultured bacterial isolates. The function is unknown.


Pssm-ID: 468123 [Multi-domain]  Cd Length: 396  Bit Score: 45.34  E-value: 3.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  41 DLRVSltDFCNLRCTYCMP--------------EAGLQFLKKPQLMSVDEIARFVRigvENL-GIREVRFTGGEPL---- 101
Cdd:NF033640  113 DLRFG--NLCNLKCRMCGPhsssswakeakklgGPKLGDKKKISWFEDEEFWKWLE---ELLpSLKEIYFAGGEPLlike 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 102 TRADLPDIIESvaGLSPRPDISLTTNAIGLEKRAETLvaagLD--------RLNISLDsAHSETFEAMtRRPF------- 166
Cdd:NF033640  188 HYKLLEKLVEK--GRAKNIELRYNTNLTVLPDKLKDL----LDlwkkfksvSISASID-GVGERNEYI-RYGSkwdeiek 259
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2794653958 167 -LHRVLQGIDAARdaglspIKINAVLQPgANEHEAAELLAWCLERGLELRFI 217
Cdd:NF033640  260 nLKKLKEECPNVE------LRINPTVSA-LNVLHLPELLDWLLELGLGPIDI 304
 
Name Accession Description Interval E-value
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
28-409 2.16e-170

GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and metabolism]; GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 442141 [Multi-domain]  Cd Length: 329  Bit Score: 479.56  E-value: 2.16e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  28 TGALLDTYGRTATDLRVSLTDFCNLRCTYCMPEAGLQFLKKPQLMSVDEIARFVRIGVEnLGIREVRFTGGEPLTRADLP 107
Cdd:COG2896     2 TSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQFLPKEELLSFEEIERLVRAFVE-LGVRKIRLTGGEPLLRKDLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 108 DIIESVAGLSPRPDISLTTNAIGLEKRAETLVAAGLDRLNISLDSAHSETFEAMTRRPFLHRVLQGIDAARDAGLSPIKI 187
Cdd:COG2896    81 ELIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 188 NAVLQPGANEHEAAELLAWCLERGLELRFIEYMPLDGAGRWNRERMVTASDVWQLLSPYYVMHPVrEARGGAPAEKFDVw 267
Cdd:COG2896   161 NAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAAEILERLEARFPLEPL-PARGGGPARYYRV- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 268 prpgsasPGAPGTIagvlkergidpantdavrsilppapgkpfaeagerpheqalgtvGIIASVTRPFCADCTRTRLTAE 347
Cdd:COG2896   239 -------PGGGGRI--------------------------------------------GFISPVSHPFCGSCNRLRLTAD 267
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794653958 348 GRVRTCLFSHSETDLLGLMRQGASDEAIAERWRAAQWGKQAGHGMDRSDFVQPERPMSAIGG 409
Cdd:COG2896   268 GKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGHGFDEGDFPQPKRSMSAIGG 329
moaA PRK00164
GTP 3',8-cyclase MoaA;
24-409 5.20e-163

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 460.76  E-value: 5.20e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  24 GRPATGALLDTYGRTATDLRVSLTDFCNLRCTYCMPEAGLQFLKKPQLMSVDEIARFVRIGVEnLGIREVRFTGGEPLTR 103
Cdd:PRK00164    1 PVPMTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPFLPKEELLSLEEIERLVRAFVA-LGVRKVRLTGGEPLLR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 104 ADLPDIIESVAGLSPRPDISLTTNAIGLEKRAETLVAAGLDRLNISLDSAHSETFEAMTRRPFLHRVLQGIDAARDAGLS 183
Cdd:PRK00164   80 KDLEDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 184 PIKINAVLQPGANEHEAAELLAWCLERGLELRFIEYMPLDGAGRWNRERMVTASDVWQLLSP-YYVMHPvrEARGGAPAE 262
Cdd:PRK00164  160 PVKVNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAEIRARLAErGWTLQP--RARSGGPAQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 263 KFdvwprpgsaspgapgtiagvlkergidpantdavrsilppapgkpfaeagerPHEQALGTVGIIASVTRPFCADCTRT 342
Cdd:PRK00164  238 YF----------------------------------------------------RHPDYGGEIGLIAPVTHDFCASCNRL 265
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2794653958 343 RLTAEGRVRTCLFSHSETDLLGLMRQGASDEAIAERWRAAQWGKQAGHGMDRSDfVQPERPMSAIGG 409
Cdd:PRK00164  266 RLTADGKLHLCLFAEDGVDLRDLLRSGADDEELAAAIREALQNKPEGHGLHDGN-TGPTRHMSYIGG 331
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
31-409 6.25e-130

molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes molybdenum cofactor biosynthesis protein A, or MoaA, as found in bacteria. It does not include the family of probable functional equivalent proteins from the archaea. MoaA works together with MoaC to synthesize precursor Z from guanine. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274250 [Multi-domain]  Cd Length: 334  Bit Score: 376.95  E-value: 6.25e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  31 LLDTYGRTATDLRVSLTDFCNLRCTYCMPE-AGLQFLKKPQLMSVDEIARFVRIGVEnLGIREVRFTGGEPLTRADLPDI 109
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEgGGLDFLPKEELLTFEEIERLVRAFVG-LGVRKVRLTGGEPLLRKDLVEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 110 IESVAGLSPRPDISLTTNAIGLEKRAETLVAAGLDRLNISLDSAHSETFEAMTRRPF-LHRVLQGIDAARDAGLSPIKIN 188
Cdd:TIGR02666  80 VARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGrLEQVLAGIDAALAAGLEPVKLN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 189 AVLQPGANEHEAAELLAWCLERGLELRFIEYMPLDGAGRWNRERMVTASDVWQLLSPYYV-MHPVREARGGAPAEkfdvw 267
Cdd:TIGR02666 160 TVVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGWREKKFVSADEILERLEQAFGpLEPVPSPRGNGPAP----- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 268 prpgSASPGAPGtiagvlkergidpantdavrsilppapgkpfaeagerpheqALGTVGIIASVTRPFCADCTRTRLTAE 347
Cdd:TIGR02666 235 ----AYRWRLPG-----------------------------------------GKGRIGFISPVSDPFCGTCNRLRLTAD 269
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2794653958 348 GRVRTCLFSHSETDLLGLMRQGASDEAIAERWRAAQWGKQAGHGMDRSD---FVQPERPMSAIGG 409
Cdd:TIGR02666 270 GKLRLCLFADDGVDLRPLLRGGASDALLEAIIQAILQKKPEGHSFLRFTspaNKRRKRAMSQIGG 334
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
17-409 1.47e-91

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 280.49  E-value: 1.47e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  17 EETPSTEGrPATGALLDTYGRTATDLRVSLTDFCNLRCTYCMPEAGLQFLKKPQLMSVDEIARFVRIGVENlGIREVRFT 96
Cdd:PLN02951   36 QVDPEASN-PVSDMLVDSFGRRHNYLRISLTERCNLRCQYCMPEEGVELTPKSHLLSQDEIVRLAGLFVAA-GVDKIRLT 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  97 GGEPLTRADLPDIIESVAGLSPRPDISLTTNAIGLEKRAETLVAAGLDRLNISLDSAHSETFEAMTRRPFLHRVLQGIDA 176
Cdd:PLN02951  114 GGEPTLRKDIEDICLQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTRRKGHDRVLESIDT 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 177 ARDAGLSPIKINAVLQPGANEHEAAELLAWCLERGLELRFIEYMPLDGAGrWNRERMVtasdvwqllsPYyvmhpvrear 256
Cdd:PLN02951  194 AIELGYNPVKVNCVVMRGFNDDEICDFVELTRDKPINVRFIEFMPFDGNV-WNVKKLV----------PY---------- 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 257 ggapAEKFDvwpRPGSASPGApgtiagvlkERGIDPANTDAvrsilppapgKPFAEAGERpheqalGTVGIIASVTRPFC 336
Cdd:PLN02951  253 ----AEMMD---RIEQRFPSL---------KRLQDHPTDTA----------KNFRIDGHC------GSVSFITSMTEHFC 300
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2794653958 337 ADCTRTRLTAEGRVRTCLFSHSETDLLGLMRQGASDEAIAERWRAAQWGKQAGH-GMDRSDfVQPERPMSAIGG 409
Cdd:PLN02951  301 AGCNRLRLLADGNLKVCLFGPSEVSLRDALRSGADDDELREIIGAAVKRKKAAHaGMFDLA-KTANRPMIHIGG 373
moaA_archaeal TIGR02668
probable molybdenum cofactor biosynthesis protein A, archaeal; This model describes an ...
31-378 2.08e-69

probable molybdenum cofactor biosynthesis protein A, archaeal; This model describes an archaeal family related, and predicted to be functionally equivalent, to molybdenum cofactor biosynthesis protein A (MoaA) of bacteria (see TIGR02666). [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274251 [Multi-domain]  Cd Length: 302  Bit Score: 221.41  E-value: 2.08e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  31 LLDTYGRTATDLRVSLTDFCNLRCTYCMPEaGLQFLKKPqLMSVDEIARFVRIGVEnLGIREVRFTGGEPLTRADLPDII 110
Cdd:TIGR02668   1 LYDRFGRPVTSLRISVTDRCNLSCFYCHME-GEDRSGGN-ELSPEEIERIVRVASE-FGVRKVKITGGEPLLRKDLIEII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 111 ESVAGLsPRPDISLTTNAIGLEKRAETLVAAGLDRLNISLDSAHSETFEAMTRRPFLHRVLQGIDAARDAGLSPIKINAV 190
Cdd:TIGR02668  78 RRIKDY-GIKDVSMTTNGILLEKLAKKLKEAGLDRVNVSLDTLDPEKYKKITGRGALDRVIEGIESAVDAGLTPVKLNMV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 191 LQPGANEHEAAELLAWCLERGLELRFIEYMPlDGAGRWNRERmvtasdvwqllspYYVmhPVRearggapaekfdvwprp 270
Cdd:TIGR02668 157 VLKGINDNEIPDMVEFAAEGGAILQLIELMP-PGEGEKEFKK-------------YHE--DID----------------- 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 271 gsaspgapgTIAGVLKERGIDPANT---DAVRSILPpapgkpfaeagerpheqALGTVGIIASVTRP-FCADCTRTRLTA 346
Cdd:TIGR02668 204 ---------PIEEELEKMADRVRTRrmhNRPKYFIP-----------------GGVEVEVVKPMDNPvFCAHCTRLRLTS 257
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2794653958 347 EGRVRTCLFSH-SETDLLGLMRQGASD-------EAIAER 378
Cdd:TIGR02668 258 DGKLKTCLLRDdNLVDILDALRNGEDDelreafrEAVARR 297
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
212-390 1.12e-35

Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. Mutations in this region of Swiss:O14940 cause MOCOD (Molybdenum Co-Factor Deficiency) type A.


Pssm-ID: 428955 [Multi-domain]  Cd Length: 127  Bit Score: 127.33  E-value: 1.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 212 LELRFIEYMPLDGAGRWNRERMVTASDVWQLLSPYYVMHPVReARGGAPAEKFdvwprpgsaspgapgTIAGvlkergid 291
Cdd:pfam06463   1 IDLRFIELMPVGEGNGWRRKKFVSLDEILERIEARFPLLPAR-KRTGGPAKRY---------------RIPG-------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 292 pantdavrsilppapgkpfaeagerpheqALGTVGIIASVTRPFCADCTRTRLTAEGRVRTCLFSHSETDLLGLMRQGAS 371
Cdd:pfam06463  57 -----------------------------GGGRIGFIAPVSNPFCASCNRLRLTADGKLKTCLFAEDGIDLRDALRSGDD 107
                         170
                  ....*....|....*....
gi 2794653958 372 DEAIAERWRAAQWGKQAGH 390
Cdd:pfam06463 108 DEELREAIREALARKPPRH 126
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
42-191 1.19e-34

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 125.79  E-value: 1.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  42 LRVSLTDFCNLRCTYCMPEAGLqflKKPQLMSVDEIARFVRIgVENLGIREVRFTGGEPLTRADLPDIIESVAGLSPRpd 121
Cdd:COG0535     2 LQIELTNRCNLRCKHCYADAGP---KRPGELSTEEAKRILDE-LAELGVKVVGLTGGEPLLRPDLFELVEYAKELGIR-- 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794653958 122 ISLTTNAIGL-EKRAETLVAAGLDRLNISLDSAHSETFEAMTRRP-FLHRVLQGIDAARDAGLsPIKINAVL 191
Cdd:COG0535    76 VNLSTNGTLLtEELAERLAEAGLDHVTISLDGVDPETHDKIRGVPgAFDKVLEAIKLLKEAGI-PVGINTVY 146
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
46-203 8.66e-32

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 118.40  E-value: 8.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  46 LTDFCNLRCTYCMPEAGlQFLKKPQLMSVDEIARFVRIGVEnLGIREVRFTGGEPLTRADLPDIIESVAGLSPRPD--IS 123
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSI-RARGKGRELSPEEILEEAKELKR-LGVEVVILGGGEPLLLPDLVELLERLLKLELAEGirIT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 124 LTTNAIGL-EKRAETLVAAGLDRLNISLDSAHSETFEAMTRRPFLHRVLQGIDAARDAGLSPIKINAVLQPGANEHEAAE 202
Cdd:pfam04055  79 LETNGTLLdEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETDEDLEE 158

                  .
gi 2794653958 203 L 203
Cdd:pfam04055 159 T 159
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
331-400 6.58e-25

Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding Twitch domain is found at the C-terminus of GTP 3',8-cyclase (EC 4.1.99.22), which is also called molybdenum cofactor biosynthesis protein A (MoaA) in bacteria and archaea, molybdenum cofactor biosynthesis protein 1 (MOCS1) in most eukaryotes, and molybdenum cofactor biosynthesis enzyme CNX2 in plants. GTP 3',8-cyclase is a radical S-adenosylmethionine (SAM) enzyme that catalyzes the first step in molybdopterin biosynthesis, the cyclization of guanosine triphosphate to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate, which is then converted to molybdopterin in subsequent steps. Radical SAM enzymes are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster that is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical, which in turn abstracts a hydrogen from the appropriately positioned carbon atom of the substrate. GTP 3',8-cyclase contains an additional iron-sulfur cluster at the C-terminal Twitch domain that is involved in substrate binding. The Twitch domain may be related to another iron-sulfur cluster-binding domain found at the C-terminus of some radical SAM enzymes, the SPASM domain, named after the biochemically characterized members, AlbA, PqqE, anSMEs, and MftC, which are involved in Subtilosin A, Pyrroloquinoline quinone, Anaerobic Sulfatase, and Mycofactocin maturation, respectively.


Pssm-ID: 411052 [Multi-domain]  Cd Length: 70  Bit Score: 96.84  E-value: 6.58e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 331 VTRPFCADCTRTRLTAEGRVRTCLFSHSETDLLGLMRQGASDEAIAERWRAAQWGKQAGHGMDRSDFVQP 400
Cdd:cd21117     1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGASDEELREAIRAAVQRKPERHSLERGDSGTR 70
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
44-243 1.04e-22

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 95.09  E-value: 1.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  44 VSLTDFCNLRCTYCMPEAGLQFLKKPQLmSVDEIARFVRIgVENLGIREVRFTGGEPLTRADLPDIIESVAGLSPRPDIS 123
Cdd:cd01335     1 LELTRGCNLNCGFCSNPASKGRGPESPP-EIEEILDIVLE-AKERGVEVVILTGGEPLLYPELAELLRRLKKELPGFEIS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 124 LTTNAIGL-EKRAETLVAAGLDRLNISLDSAHSETFEAMTRRPFLH-RVLQGIDAARDAGLsPIKINAVLQPGAN-EHEA 200
Cdd:cd01335    79 IETNGTLLtEELLKELKELGLDGVGVSLDSGDEEVADKIRGSGESFkERLEALKELREAGL-GLSTTLLVGLGDEdEEDD 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2794653958 201 AELLAWcLERGLELRFIEYMPLDGAGRWNRERMVTASDVWQLL 243
Cdd:cd01335   158 LEELEL-LAEFRSPDRVSLFRLLPEEGTPLELAAPVVPAEKLL 199
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
44-243 1.20e-19

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 86.69  E-value: 1.20e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958   44 VSLTDFCNLRCTYCMPEAGLQFLKKPQLMSV-DEIARFVRIGVENLGIREVRFTGGEP--LTRADLPDIIESVA---GLS 117
Cdd:smart00729   5 YIITRGCPRRCTFCSFPSLRGKLRSRYLEALvREIELLAEKGEKEGLVGTVFIGGGTPtlLSPEQLEELLEAIReilGLA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  118 PRPDISLTTNAIGL-EKRAETLVAAGLDRLNISLDSAHSETFEAMTRRPFLHRVLQGIDAARDAGlsPIKINAVL---QP 193
Cdd:smart00729  85 KDVEITIETRPDTLtEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAG--PIKVSTDLivgLP 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2794653958  194 GANEHEAAELLAWCLERGLE-LRFIEYMPLDG---AGRWNRERMVTASDVWQLL 243
Cdd:smart00729 163 GETEEDFEETLKLLKELGPDrVSIFPLSPRPGtplAKMYKRLKPPTKEERAELL 216
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
42-216 2.35e-14

Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function prediction only];


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 73.79  E-value: 2.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  42 LRVSLTDFCNLRCTYCMPEAG-------LQFLKKPQ--LMSVDEIARFVRIGVENLgIREVrftgGEPLTRADLPDIIES 112
Cdd:COG2100    38 LQVRPTTGCNLNCIFCSVDAGphsrtrqAEYIVDPEylVEWFEKVARFKGKGVEAH-IDGV----GEPLLYPYIVELVKG 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 113 VAGLSPRPDISLTTNAIGL-EKRAETLVAAGLDRLNISLDSAHSETFEAMTRRPF--LHRVLQGID-AARDAGLSpIKIN 188
Cdd:COG2100   113 LKEIKGVKVVSMQTNGTLLsEKLIDELEEAGLDRINLSIDTLDPEKAKKLAGTKWydVEKVLELAEyIARETKID-LLIA 191
                         170       180
                  ....*....|....*....|....*...
gi 2794653958 189 AVLQPGANEHEAAELLAWCLERGLELRF 216
Cdd:COG2100   192 PVWLPGINDEDIPKIIEWALEIGAGKKW 219
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
46-247 2.80e-14

Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 73.48  E-value: 2.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  46 LTDFCNLRCTYC-MPEAGLQflkKPQLMSVDEIARFVRIGVENLG-IREVRFT--GGEPLTRADL----PDIIESVAGLS 117
Cdd:COG0641     7 PTSRCNLRCSYCyYSEGDEG---SRRRMSEETAEKAIDFLIESSGpGKELTITffGGEPLLNFDFikeiVEYARKYAKKG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 118 PRPDISLTTNAIGL-EKRAETLVAAGLdRLNISLD---SAHSetfeamTRRPFL------HRVLQGIDAARDAGLsPIKI 187
Cdd:COG0641    84 KKIRFSIQTNGTLLdDEWIDFLKENGF-SVGISLDgpkEIHD------RNRVTKngkgsfDRVMRNIKLLKEHGV-EVNI 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 188 NAVLQPgANEHEAAELLAWCLERGleLRFIEYMPLDGAGRwnRERMVTASDVWQLLSPYY 247
Cdd:COG0641   156 RCTVTR-ENLDDPEELYDFLKELG--FRSIQFNPVVEEGE--ADYSLTPEDYGEFLIELF 210
NrdG2 TIGR02495
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
50-212 1.12e-09

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055). It is often gene clustered with the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487) and presumably fulfills the identical function as NrdG, which utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in NrdD. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274164 [Multi-domain]  Cd Length: 192  Bit Score: 57.37  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  50 CNLRCTYCMPEAgLQFLKKPQLMSVDEIARFVRIGVenLGIREVRFTGGEPLTRADLPDIIESVAGLSPRpdISLTTNAI 129
Cdd:TIGR02495  26 CNLKCPYCHNPL-LIPRRGSGEIEVEELLEFLRRRR--GLLDGVVITGGEPTLQAGLPDFLREVRELGFE--VKLDTNGS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 130 gLEKRAETLVAAGLdrLN-ISLD-SAHSETFEAMTRRPF---LHRVLQGIDAARDAGLsPIKINAVLQPGAN-EHEAAEL 203
Cdd:TIGR02495 101 -NPRRLEELLEEGL--VDyVAMDvKAPPEKYGELYGLEKngaAKNILKSLEILLESGI-PFELRTTVVRGFLtEEDLAEI 176

                  ....*....
gi 2794653958 204 LAWCLERGL 212
Cdd:TIGR02495 177 ATRIKENGT 185
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
50-217 7.42e-09

Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];


Pssm-ID: 440655 [Multi-domain]  Cd Length: 394  Bit Score: 57.26  E-value: 7.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  50 CNLRCTYCMpeAGLQFLKKPQLMSVDEIARFVRIGVENLGIREVRFTGgePLTRADLPDIIESVAGLSPRP-DISLTTNA 128
Cdd:COG1032   184 CPFGCSFCS--ISALYGRKVRYRSPESVVEEIEELVKRYGIREIFFVD--DNFNVDKKRLKELLEELIERGlNVSFPSEV 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 129 ---IGLEKRAETLVAAGLDRLNISLDSAHSETFEAMTRRPFLHRVLQGIDAARDAGlspIKINAVLQ---PGANEHEAAE 202
Cdd:COG1032   260 rvdLLDEELLELLKKAGCRGLFIGIESGSQRVLKAMNKGITVEDILEAVRLLKKAG---IRVKLYFIiglPGETEEDIEE 336
                         170
                  ....*....|....*
gi 2794653958 203 LLAWCLERGLELRFI 217
Cdd:COG1032   337 TIEFIKELGPDQAQV 351
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
50-211 1.89e-08

Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic radical activating enzyme NrdG/QueE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440367 [Multi-domain]  Cd Length: 205  Bit Score: 53.99  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  50 CNLRCTYC------MPEAGlqflkkpQLMSVDEIARFVrigvENLGIREVRFTGGEPLTRADLPDIIESV--AGLSprpd 121
Cdd:COG0602    30 CNLRCSWCdtkyawDGEGG-------KRMSAEEILEEV----AALGARHVVITGGEPLLQDDLAELLEALkdAGYE---- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 122 ISLTTNaiGlekraeTL-VAAGLDRLNISL-------DSAHSETFEAMTRRPFLHRVL---QGIDAARD-AGLSPIKINA 189
Cdd:COG0602    95 VALETN--G------TLpIPAGIDWVTVSPklpssgeEEDNRENLEVLRRADELKFVVadeTDLEEAEElLARLDFRCPV 166
                         170       180
                  ....*....|....*....|....*
gi 2794653958 190 VLQP--GANEHEAAELLA-WCLERG 211
Cdd:COG0602   167 YLQPvwGNKLEENTELLAeWCLAHP 191
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
49-206 4.11e-08

Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal structure and biogenesis]; Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440495 [Multi-domain]  Cd Length: 248  Bit Score: 53.66  E-value: 4.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  49 FCNLRCTYC------MPEAGLQFLKKPQLMsVDEIARFVR-IGVENLGIREVRFTG-GEPLTRADLPDIIESVAGLSPRP 120
Cdd:COG0731    33 TCNFDCVYCqrgrttDLTRERREFDDPEEI-LEELIEFLRkLPEEAREPDHITFSGsGEPTLYPNLGELIEEIKKLRGIK 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 121 dISLTTNA--IGLEKRAETLvaAGLDRLNISLDSAHSETFEAMTrRPFLH----RVLQGIDAARDAGLSPIKINAVLQPG 194
Cdd:COG0731   112 -TALLTNGslLHRPEVREEL--LKADQVYPSLDAADEETFRKIN-RPHPGlsweRIIEGLELFRKLYKGRTVIETMLVKG 187
                         170
                  ....*....|..
gi 2794653958 195 ANEHEaAELLAW 206
Cdd:COG0731   188 INDSE-EELEAY 198
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
50-239 4.20e-08

Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 53.65  E-value: 4.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  50 CNLRCTYCM-PE-AGLQFLKKPQLMSVDEIARFV--RIGVENLGIReVRFTGGEPLTRAD-LPDIIESV--AGLSprpdI 122
Cdd:COG1180    31 CNLRCPYCHnPEiSQGRPDAAGRELSPEELVEEAlkDRGFLDSCGG-VTFSGGEPTLQPEfLLDLAKLAkeLGLH----T 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 123 SLTTNAIGLEKRAETLvAAGLDRLNISLDSAHSETFEAMTRRPfLHRVLQGIDAARDAGLsPIKINAVLQPGAN--EHEA 200
Cdd:COG1180   106 ALDTNGYIPEEALEEL-LPYLDAVNIDLKAFDDEFYRKLTGVS-LEPVLENLELLAESGV-HVEIRTLVIPGLNdsEEEL 182
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2794653958 201 AELLAWCLERG----LEL-RFIEYMPLDGAGRWNRERMVTASDV 239
Cdd:COG1180   183 EAIARFIAELGdvipVHLlPFHPLYKLEDVPPPSPETLERAREI 226
BioB COG0502
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
49-184 2.53e-06

Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 440268 [Multi-domain]  Cd Length: 308  Bit Score: 48.89  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  49 FCNLRCTYcmpEAGLqflKKPQLMSVDEIARFVRIGVENlGIRevRF---TGGEPLTRADLPDIIESVAGLSPRPDISLT 125
Cdd:COG0502    56 YCGQSAHN---KTGI---ERYRLLSVEEILEAARAAKEA-GAR--RFclvASGRDPSDRDFEKVLEIVRAIKEELGLEVC 126
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2794653958 126 TNaIGL--EKRAETLVAAGLDRLNISLDSAhSETFEAM-TRRPFLHRvLQGIDAARDAGLSP 184
Cdd:COG0502   127 AS-LGElsEEQAKRLKEAGVDRYNHNLETS-PELYPKIcTTHTYEDR-LDTLKNAREAGLEV 185
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
50-184 2.15e-05

Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General function prediction only];


Pssm-ID: 444038  Cd Length: 261  Bit Score: 45.75  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  50 CNLRCTYC--------MPEAGlqflkkpQLMSVDEIA-RFVRIGVENlGIREVRFTGGEP-LTRADLPDIIESVaglspr 119
Cdd:COG5014    50 CNLRCGFCwswrfrdfPLTIG-------KFYSPEEVAeRLIEIARER-GYRQVRLSGGEPtIGFEHLLKVLELF------ 115
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2794653958 120 PDISLT----TNA--IGLEKR-AETLVAAGLDRLNISLDSAHSETFEAMT--RRPFLHRVLQGIDAARDAGLSP 184
Cdd:COG5014   116 SERGLTfileTNGilIGYDRElARELASFRNIVVRVSIKGCTPEEFSMLTgaDPEFFELQLRALKNLVDAGLEP 189
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
41-217 3.85e-05

twitch domain-containing radical SAM protein; Members of this family are unusual among radical SAM proteins in several ways. First, the N-terminal region consists of an iron-sulfur cluster-binding twitch domain (half of a SPASM domain), something usually found C-terminal to the radical SAM domain. Second, the radical SAM domains in many of the members of this family score poorly vs. the Pfam HMM, PF04055 (version 19), used to identify radical SAM. Lastly, the majority of members sequenced to date come from uncultured bacteria from marine or aquifer sources rather than from conventionally cultured bacterial isolates. The function is unknown.


Pssm-ID: 468123 [Multi-domain]  Cd Length: 396  Bit Score: 45.34  E-value: 3.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  41 DLRVSltDFCNLRCTYCMP--------------EAGLQFLKKPQLMSVDEIARFVRigvENL-GIREVRFTGGEPL---- 101
Cdd:NF033640  113 DLRFG--NLCNLKCRMCGPhsssswakeakklgGPKLGDKKKISWFEDEEFWKWLE---ELLpSLKEIYFAGGEPLlike 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 102 TRADLPDIIESvaGLSPRPDISLTTNAIGLEKRAETLvaagLD--------RLNISLDsAHSETFEAMtRRPF------- 166
Cdd:NF033640  188 HYKLLEKLVEK--GRAKNIELRYNTNLTVLPDKLKDL----LDlwkkfksvSISASID-GVGERNEYI-RYGSkwdeiek 259
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2794653958 167 -LHRVLQGIDAARdaglspIKINAVLQPgANEHEAAELLAWCLERGLELRFI 217
Cdd:NF033640  260 nLKKLKEECPNVE------LRINPTVSA-LNVLHLPELLDWLLELGLGPIDI 304
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
44-178 1.14e-04

SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in Syntrophobacter fumaroxidans MPOB, Chlorobium limicola DSM 245, Methanocella paludicola SANAE, and delta proteobacterium NaphS2 contains two PqqE-like radical SAM/SPASM domain proteins, a PqqD homolog, and a conserved hypothetical protein. These components suggest modification of a ribosomally produced peptide precursor, but the precursor has not been identified. Of the two PqqE homologs of the cassette, this family is the closer in sequence.


Pssm-ID: 211973 [Multi-domain]  Cd Length: 358  Bit Score: 44.08  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  44 VSLTDFCNLRCTYC--MPEAGlqflKKPQLMSVDEIARFVRiGVENLGIREVRFTGGEPLTRADLPDIIESVAGLSPRPD 121
Cdd:TIGR04250   7 IDITGRCNLRCRYCshFSSAA----ETPTDLETAEWLRFFR-ELNRCSVLRVVLSGGEPFMRSDFREIIDGIVKNRMRFS 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2794653958 122 IsLTTNAIGLEKRAETLVAAG-LDRLNISLDSAHSETFEAMTRRPFLHRVLQGIDAAR 178
Cdd:TIGR04250  82 I-LSNGTLITDAIASFLAATRrCDYVQVSIDGSTPGTHDRLRGTGSFLQAVEGIELLR 138
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
46-205 2.59e-04

SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in Syntrophobacter fumaroxidans MPOB, Chlorobium limicola DSM 245, Methanocella paludicola SANAE, and delta proteobacterium NaphS2 contains two PqqE-like radical SAM/SPASM domain proteins, a PqqD homolog, and a conserved hypothetical protein. These components suggest modification of a ribosomally produced peptide precursor, but the precursor has not been identified. Of the two PqqE homologs of the cassette, this family is the more distant in sequence.


Pssm-ID: 211974 [Multi-domain]  Cd Length: 353  Bit Score: 42.90  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  46 LTDFCNLRCTYCMPEAGLQFLK-KPQLMSVDEIARFVRIGVEnLGIREVRFTGGEPLTRADLPDIIESVA--GLSprpdI 122
Cdd:TIGR04251  10 LTEGCNLKCRHCWIDPKYQGEGeQHPSLDPSLFRSIIRQAIP-LGLTSVKLTGGEPLLHPAIGEILECIGenNLQ----L 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958 123 SLTTNAIGLEKR-AETLVAAGLDRLNISLDSAHSETFEAMTR-RPFLHRVLQGIDAARDAGLSPIKINAVLQPGANEHEA 200
Cdd:TIGR04251  85 SVETNGLLCTPQtARDLASCETPFVSVSLDGVDAATHDWMRGvKGAFDKAVRGIHNLVEAGIHPQIIMTVTRRNVGQMEQ 164

                  ....*
gi 2794653958 201 AELLA 205
Cdd:TIGR04251 165 IVRLA 169
sulfatase_rSAM TIGR03942
anaerobic sulfatase-maturating enzyme; Members of this protein family are radical SAM family ...
50-100 2.25e-03

anaerobic sulfatase-maturating enzyme; Members of this protein family are radical SAM family enzymes, maturases that prepare the oxygen-sensitive radical required in the active site of anaerobic sulfatases. This maturase role has led to many misleading legacy annotations suggesting that this enzyme maturase is instead a sulfatase regulatory protein. All members of the seed alignment are radical SAM enzymes encoded next to or near an anaerobic sulfatase. Note that a single genome may encode more than one sulfatase/maturase pair. [Protein fate, Protein modification and repair]


Pssm-ID: 188457 [Multi-domain]  Cd Length: 363  Bit Score: 39.90  E-value: 2.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2794653958  50 CNLRCTYCM-PEAGLQFLKKPQLMSVDEIARFVRIGVENLGIREVRFT--GGEP 100
Cdd:TIGR03942  11 CNLDCDYCFyLEKEDLYPKPKPKMSDETLETFIKQYIASQDGPEVNFAwqGGEP 64
cofG PRK06245
FO synthase subunit 1; Reviewed
34-99 4.29e-03

FO synthase subunit 1; Reviewed


Pssm-ID: 180485 [Multi-domain]  Cd Length: 336  Bit Score: 38.72  E-value: 4.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2794653958  34 TYGRTATdlrVSLTDFCNLRCTYCmpeaglQFLK---KPQLMSVDEIARFVRIGvENLGIREVRFTGGE 99
Cdd:PRK06245    9 TYSRNVF---IPLTYECRNRCGYC------TFRRdpgQPSLLSPEEVKEILRRG-ADAGCTEALFTFGE 67
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
42-126 9.77e-03

4Fe-4S single cluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 433138 [Multi-domain]  Cd Length: 137  Bit Score: 36.38  E-value: 9.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2794653958  42 LRVSLtdF---CNLRCTYCMPEAGlQFLKKPQLMSVDEIARFVRIgVENLGIREVRFTGGEPLTRAD-LPDIIESVAGLS 117
Cdd:pfam13353   6 VRCSL--FvsgCNHHCKGCFNPET-WDFKYGKPFTEELEDEIIED-LAKPYIQGLTLSGGEPLLNAEaLLELVKRVREEC 81

                  ....*....
gi 2794653958 118 PRPDISLTT 126
Cdd:pfam13353  82 PEKDIWLWT 90
 
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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