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Conserved domains on  [gi|657347733|ref|WP_029404560|]
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GTP 3',8-cyclase MoaA [Stutzerimonas stutzeri]

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 ...
1-331 0e+00

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: 503.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733   1 MPdSKLVDPFGRRITYLRLSVTDRCDFRCTYCMSED-MVFAPRAQILTLEELYAVADAFISLGVKRIRVTGGEPLVRKGL 79
Cdd:COG2896    1 MT-SPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEgYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  80 PSLLSRLGAREELEDLAITTNGSQLPTLAPVLREAGVKRLNISLDSLKRERFAELTRRDMLGQVVAGIDAARSAGFDRIK 159
Cdd:COG2896   80 PELIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733 160 LNSVIQKGRNDDEVLDLVNFAVERGLDISFIEEMPLGNVSSHEREiTFCSSDEVRERIEVGHQLIRSSHTTGGPSRYWQV 239
Cdd:COG2896  160 INAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRD-QVVSAAEILERLEARFPLEPLPARGGGPARYYRV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733 240 AGSDTQVGFISPHSNNFCGSCNRVRVTAEGKLVLCLGHEGALDLKTLMRRYPGDrERLRQALVDALQLKPEKHEFRTDEQ 319
Cdd:COG2896  239 PGGGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASD-EELAEAIREAIARKPEGHGFDEGDF 317
                        330
                 ....*....|..
gi 657347733 320 VQVVRFMSMTGG 331
Cdd:COG2896  318 PQPKRSMSAIGG 329
 
Name Accession Description Interval E-value
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
1-331 0e+00

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: 503.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733   1 MPdSKLVDPFGRRITYLRLSVTDRCDFRCTYCMSED-MVFAPRAQILTLEELYAVADAFISLGVKRIRVTGGEPLVRKGL 79
Cdd:COG2896    1 MT-SPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEgYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  80 PSLLSRLGAREELEDLAITTNGSQLPTLAPVLREAGVKRLNISLDSLKRERFAELTRRDMLGQVVAGIDAARSAGFDRIK 159
Cdd:COG2896   80 PELIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733 160 LNSVIQKGRNDDEVLDLVNFAVERGLDISFIEEMPLGNVSSHEREiTFCSSDEVRERIEVGHQLIRSSHTTGGPSRYWQV 239
Cdd:COG2896  160 INAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRD-QVVSAAEILERLEARFPLEPLPARGGGPARYYRV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733 240 AGSDTQVGFISPHSNNFCGSCNRVRVTAEGKLVLCLGHEGALDLKTLMRRYPGDrERLRQALVDALQLKPEKHEFRTDEQ 319
Cdd:COG2896  239 PGGGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASD-EELAEAIREAIARKPEGHGFDEGDF 317
                        330
                 ....*....|..
gi 657347733 320 VQVVRFMSMTGG 331
Cdd:COG2896  318 PQPKRSMSAIGG 329
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-331 1.62e-156

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 441.12  E-value: 1.62e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733   1 MPDSKLVDPFGRRITYLRLSVTDRCDFRCTYCMSED-MVFAPRAQILTLEELYAVADAFISLGVKRIRVTGGEPLVRKGL 79
Cdd:PRK00164   3 PMTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGyLPFLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  80 PSLLSRLGAREELEDLAITTNGSQLPTLAPVLREAGVKRLNISLDSLKRERFAELTRRDMLGQVVAGIDAARSAGFDRIK 159
Cdd:PRK00164  83 EDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTPVK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733 160 LNSVIQKGRNDDEVLDLVNFAVERGLDISFIEEMPLGNvSSHEREITFCSSDEVRERIEVGHQLIRSSHTTGGPSRYWQV 239
Cdd:PRK00164 163 VNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGE-GNEWFRKHHLSGAEIRARLAERGWTLQPRARSGGPAQYFRH 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733 240 AGSDTQVGFISPHSNNFCGSCNRVRVTAEGKLVLCLGHEGALDLKTLMRRyPGDRERLRQALVDALQLKPEKHEFRtDEQ 319
Cdd:PRK00164 242 PDYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRS-GADDEELAAAIREALQNKPEGHGLH-DGN 319
                        330
                 ....*....|..
gi 657347733 320 VQVVRFMSMTGG 331
Cdd:PRK00164 320 TGPTRHMSYIGG 331
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
6-331 3.89e-142

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: 405.07  E-value: 3.89e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733    6 LVDPFGRRITYLRLSVTDRCDFRCTYCMSEDMV--FAPRAQILTLEELYAVADAFISLGVKRIRVTGGEPLVRKGLPSLL 83
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGldFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733   84 SRLGAREELEDLAITTNGSQLPTLAPVLREAGVKRLNISLDSLKRERFAELTRRDM-LGQVVAGIDAARSAGFDRIKLNS 162
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGrLEQVLAGIDAALAAGLEPVKLNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  163 VIQKGRNDDEVLDLVNFAVERGLDISFIEEMPLGNVSSHEREiTFCSSDEVRERIEVGHQLIR--SSHTTGGPSRYWQVA 240
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGWREK-KFVSADEILERLEQAFGPLEpvPSPRGNGPAPAYRWR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  241 GSDTQ--VGFISPHSNNFCGSCNRVRVTAEGKLVLCLGHEGALDLKTLMRRyPGDRERLRQALVDALQLKPEKH---EFR 315
Cdd:TIGR02666 240 LPGGKgrIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRG-GASDALLEAIIQAILQKKPEGHsflRFT 318
                         330
                  ....*....|....*.
gi 657347733  316 TDEQVQVVRFMSMTGG 331
Cdd:TIGR02666 319 SPANKRRKRAMSQIGG 334
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
185-312 3.96e-49

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: 160.46  E-value: 3.96e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  185 LDISFIEEMPLGNVSSHEREiTFCSSDEVRERIEVGHQLIRSSHTTGGPSRYWQVAGSDTQVGFISPHSNNFCGSCNRVR 264
Cdd:pfam06463   1 IDLRFIELMPVGEGNGWRRK-KFVSLDEILERIEARFPLLPARKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLR 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 657347733  265 VTAEGKLVLCLGHEGALDLKTLMRRyPGDRERLRQALVDALQLKPEKH 312
Cdd:pfam06463  80 LTADGKLKTCLFAEDGIDLRDALRS-GDDDEELREAIREALARKPPRH 126
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
252-321 1.05e-23

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: 92.22  E-value: 1.05e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733 252 HSNNFCGSCNRVRVTAEGKLVLCLGHEGALDLKTLMRRYPGDrERLRQALVDALQLKPEKHEFRTDEQVQ 321
Cdd:cd21117    1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGASD-EELREAIRAAVQRKPERHSLERGDSGT 69
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
15-190 3.25e-14

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: 70.51  E-value: 3.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733    15 TYLRLSVTDRCDFRCTYC----MSEDMVFAPRAQILTLEELYAVADAFISLgVKRIRVTGGEPLV--RKGLPSLLSRLGA 88
Cdd:smart00729   1 PLALYIITRGCPRRCTFCsfpsLRGKLRSRYLEALVREIELLAEKGEKEGL-VGTVFIGGGTPTLlsPEQLEELLEAIRE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733    89 REELED---LAITTNGSQL-PTLAPVLREAGVKRLNISLDSLKRERFAELTRRDMLGQVVAGIDAARSAGFDRIKLNSVI 164
Cdd:smart00729  80 ILGLAKdveITIETRPDTLtEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAGPIKVSTDLIV 159
                          170       180
                   ....*....|....*....|....*..
gi 657347733   165 -QKGRNDDEVLDLVNFAVERGLDISFI 190
Cdd:smart00729 160 gLPGETEEDFEETLKLLKELGPDRVSI 186
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
17-105 2.02e-04

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: 42.64  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  17 LRLSVTdrCDFRCTYCMS-------EDMVFAPRAQILTLEEL-YAVADAFISL------GVKRIRVTGGEPLVRKGLPSL 82
Cdd:NF033640 114 LRFGNL--CNLKCRMCGPhsssswaKEAKKLGGPKLGDKKKIsWFEDEEFWKWleellpSLKEIYFAGGEPLLIKEHYKL 191
                         90       100
                 ....*....|....*....|....*.
gi 657347733  83 LSRL---GAREELEdLAITTNGSQLP 105
Cdd:NF033640 192 LEKLvekGRAKNIE-LRYNTNLTVLP 216
 
Name Accession Description Interval E-value
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
1-331 0e+00

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: 503.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733   1 MPdSKLVDPFGRRITYLRLSVTDRCDFRCTYCMSED-MVFAPRAQILTLEELYAVADAFISLGVKRIRVTGGEPLVRKGL 79
Cdd:COG2896    1 MT-SPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEgYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  80 PSLLSRLGAREELEDLAITTNGSQLPTLAPVLREAGVKRLNISLDSLKRERFAELTRRDMLGQVVAGIDAARSAGFDRIK 159
Cdd:COG2896   80 PELIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733 160 LNSVIQKGRNDDEVLDLVNFAVERGLDISFIEEMPLGNVSSHEREiTFCSSDEVRERIEVGHQLIRSSHTTGGPSRYWQV 239
Cdd:COG2896  160 INAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRD-QVVSAAEILERLEARFPLEPLPARGGGPARYYRV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733 240 AGSDTQVGFISPHSNNFCGSCNRVRVTAEGKLVLCLGHEGALDLKTLMRRYPGDrERLRQALVDALQLKPEKHEFRTDEQ 319
Cdd:COG2896  239 PGGGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASD-EELAEAIREAIARKPEGHGFDEGDF 317
                        330
                 ....*....|..
gi 657347733 320 VQVVRFMSMTGG 331
Cdd:COG2896  318 PQPKRSMSAIGG 329
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-331 1.62e-156

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 441.12  E-value: 1.62e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733   1 MPDSKLVDPFGRRITYLRLSVTDRCDFRCTYCMSED-MVFAPRAQILTLEELYAVADAFISLGVKRIRVTGGEPLVRKGL 79
Cdd:PRK00164   3 PMTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGyLPFLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  80 PSLLSRLGAREELEDLAITTNGSQLPTLAPVLREAGVKRLNISLDSLKRERFAELTRRDMLGQVVAGIDAARSAGFDRIK 159
Cdd:PRK00164  83 EDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTPVK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733 160 LNSVIQKGRNDDEVLDLVNFAVERGLDISFIEEMPLGNvSSHEREITFCSSDEVRERIEVGHQLIRSSHTTGGPSRYWQV 239
Cdd:PRK00164 163 VNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGE-GNEWFRKHHLSGAEIRARLAERGWTLQPRARSGGPAQYFRH 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733 240 AGSDTQVGFISPHSNNFCGSCNRVRVTAEGKLVLCLGHEGALDLKTLMRRyPGDRERLRQALVDALQLKPEKHEFRtDEQ 319
Cdd:PRK00164 242 PDYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRS-GADDEELAAAIREALQNKPEGHGLH-DGN 319
                        330
                 ....*....|..
gi 657347733 320 VQVVRFMSMTGG 331
Cdd:PRK00164 320 TGPTRHMSYIGG 331
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
6-331 3.89e-142

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: 405.07  E-value: 3.89e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733    6 LVDPFGRRITYLRLSVTDRCDFRCTYCMSEDMV--FAPRAQILTLEELYAVADAFISLGVKRIRVTGGEPLVRKGLPSLL 83
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGldFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733   84 SRLGAREELEDLAITTNGSQLPTLAPVLREAGVKRLNISLDSLKRERFAELTRRDM-LGQVVAGIDAARSAGFDRIKLNS 162
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGrLEQVLAGIDAALAAGLEPVKLNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  163 VIQKGRNDDEVLDLVNFAVERGLDISFIEEMPLGNVSSHEREiTFCSSDEVRERIEVGHQLIR--SSHTTGGPSRYWQVA 240
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGWREK-KFVSADEILERLEQAFGPLEpvPSPRGNGPAPAYRWR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  241 GSDTQ--VGFISPHSNNFCGSCNRVRVTAEGKLVLCLGHEGALDLKTLMRRyPGDRERLRQALVDALQLKPEKH---EFR 315
Cdd:TIGR02666 240 LPGGKgrIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRG-GASDALLEAIIQAILQKKPEGHsflRFT 318
                         330
                  ....*....|....*.
gi 657347733  316 TDEQVQVVRFMSMTGG 331
Cdd:TIGR02666 319 SPANKRRKRAMSQIGG 334
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
6-331 6.86e-85

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 260.84  E-value: 6.86e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733   6 LVDPFGRRITYLRLSVTDRCDFRCTYCMSEDMV-FAPRAQILTLEELYAVADAFISLGVKRIRVTGGEPLVRKGLPSLLS 84
Cdd:PLN02951  49 LVDSFGRRHNYLRISLTERCNLRCQYCMPEEGVeLTPKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDICL 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  85 RLGAREELEDLAITTNGSQLPTLAPVLREAGVKRLNISLDSLKRERFAELTRRDMLGQVVAGIDAARSAGFDRIKLNSVI 164
Cdd:PLN02951 129 QLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTRRKGHDRVLESIDTAIELGYNPVKVNCVV 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733 165 QKGRNDDEVLDLVNFAVERGLDISFIEEMPL-GNVSSHEREITFCssdEVRERIEVGH-QLIRSSHTTGGPSRYWQVAGS 242
Cdd:PLN02951 209 MRGFNDDEICDFVELTRDKPINVRFIEFMPFdGNVWNVKKLVPYA---EMMDRIEQRFpSLKRLQDHPTDTAKNFRIDGH 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733 243 DTQVGFISPHSNNFCGSCNRVRVTAEGKLVLCLGHEGALDLKTLMRRYPGDRErLRQALVDALQLKPEKHEFRTDEQVQV 322
Cdd:PLN02951 286 CGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSLRDALRSGADDDE-LREIIGAAVKRKKAAHAGMFDLAKTA 364

                 ....*....
gi 657347733 323 VRFMSMTGG 331
Cdd:PLN02951 365 NRPMIHIGG 373
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
185-312 3.96e-49

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: 160.46  E-value: 3.96e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  185 LDISFIEEMPLGNVSSHEREiTFCSSDEVRERIEVGHQLIRSSHTTGGPSRYWQVAGSDTQVGFISPHSNNFCGSCNRVR 264
Cdd:pfam06463   1 IDLRFIELMPVGEGNGWRRK-KFVSLDEILERIEARFPLLPARKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLR 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 657347733  265 VTAEGKLVLCLGHEGALDLKTLMRRyPGDRERLRQALVDALQLKPEKH 312
Cdd:pfam06463  80 LTADGKLKTCLFAEDGIDLRDALRS-GDDDEELREAIREALARKPPRH 126
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
21-176 5.79e-29

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: 109.15  E-value: 5.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733   21 VTDRCDFRCTYCMSEDMVFAPRAQILTLEELYAVADAFISLGVKRIRVTGGEPLVRKGLPSLLSRLGAREELED--LAIT 98
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAEGirITLE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657347733   99 TNGSQL-PTLAPVLREAGVKRLNISLDSLKRERFAELTRRDMLGQVVAGIDAARSAGFDRIKLNSVIQKGRNDDEVLDL 176
Cdd:pfam04055  81 TNGTLLdEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETDEDLEET 159
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
16-163 4.16e-25

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: 98.82  E-value: 4.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  16 YLRLSVTDRCDFRCTYCMSEDMvfAPRAQILTLEELYAVADAFISLGVKRIRVTGGEPLVRKGLPSLLSRlgAREELEDL 95
Cdd:COG0535    1 RLQIELTNRCNLRCKHCYADAG--PKRPGELSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEY--AKELGIRV 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  96 AITTNGSQL-PTLAPVLREAGVKRLNISLDSLKRERFAELTRRD-MLGQVVAGIDAARSAGFdRIKLNSV 163
Cdd:COG0535   77 NLSTNGTLLtEELAERLAEAGLDHVTISLDGVDPETHDKIRGVPgAFDKVLEAIKLLKEAGI-PVGINTV 145
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
252-321 1.05e-23

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: 92.22  E-value: 1.05e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733 252 HSNNFCGSCNRVRVTAEGKLVLCLGHEGALDLKTLMRRYPGDrERLRQALVDALQLKPEKHEFRTDEQVQ 321
Cdd:cd21117    1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGASD-EELREAIRAAVQRKPERHSLERGDSGT 69
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
19-217 1.61e-17

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: 79.68  E-value: 1.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  19 LSVTDRCDFRCTYCMSEDMVFAPRAQILTLEELYAVADAFISLGVKRIRVTGGEPLVRKGLPSLLSRLGAREELEDLAIT 98
Cdd:cd01335    1 LELTRGCNLNCGFCSNPASKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGFEISIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  99 TNGSQL-PTLAPVLREAGVKRLNISLDSlKRERFAELTRRDM--LGQVVAGIDAARSAGFdRIKLNSVIQKGRNDDEVLD 175
Cdd:cd01335   81 TNGTLLtEELLKELKELGLDGVGVSLDS-GDEEVADKIRGSGesFKERLEALKELREAGL-GLSTTLLVGLGDEDEEDDL 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 657347733 176 lvnFAVERGLDISFIEEMPLGNVSSHEREITFCSSDEVRERI 217
Cdd:cd01335  159 ---EELELLAEFRSPDRVSLFRLLPEEGTPLELAAPVVPAEK 197
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
15-190 3.25e-14

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: 70.51  E-value: 3.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733    15 TYLRLSVTDRCDFRCTYC----MSEDMVFAPRAQILTLEELYAVADAFISLgVKRIRVTGGEPLV--RKGLPSLLSRLGA 88
Cdd:smart00729   1 PLALYIITRGCPRRCTFCsfpsLRGKLRSRYLEALVREIELLAEKGEKEGL-VGTVFIGGGTPTLlsPEQLEELLEAIRE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733    89 REELED---LAITTNGSQL-PTLAPVLREAGVKRLNISLDSLKRERFAELTRRDMLGQVVAGIDAARSAGFDRIKLNSVI 164
Cdd:smart00729  80 ILGLAKdveITIETRPDTLtEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAGPIKVSTDLIV 159
                          170       180
                   ....*....|....*....|....*..
gi 657347733   165 -QKGRNDDEVLDLVNFAVERGLDISFI 190
Cdd:smart00729 160 gLPGETEEDFEETLKLLKELGPDRVSI 186
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
19-206 8.33e-14

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 71.17  E-value: 8.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  19 LSVTDRCDFRCTYCMSEDMVFAPRaQILTLEELYAVADAFI--SLGVKRIRVT--GGEPL-----VRKGLPSLLSRLGAR 89
Cdd:COG0641    5 LKPTSRCNLRCSYCYYSEGDEGSR-RRMSEETAEKAIDFLIesSGPGKELTITffGGEPLlnfdfIKEIVEYARKYAKKG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  90 EELEdLAITTNGSQL-PTLAPVLREAGVkRLNISLDSlkRERFAELTRRDMLGQ-----VVAGIDAARSAGFDrIKLNSV 163
Cdd:COG0641   84 KKIR-FSIQTNGTLLdDEWIDFLKENGF-SVGISLDG--PKEIHDRNRVTKNGKgsfdrVMRNIKLLKEHGVE-VNIRCT 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 657347733 164 IQKgRNDDEVLDLVNFAVERGLD-ISFIeemPLGNVSSHEREIT 206
Cdd:COG0641  159 VTR-ENLDDPEELYDFLKELGFRsIQFN---PVVEEGEADYSLT 198
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
11-138 5.67e-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: 52.45  E-value: 5.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  11 GRRITYLRLSvtdRCDFRCTYCMSEDMVFAPRAQILTLEELYAVADAFislGVKRIRVTGGEPLVRKGLPSLLSRLGARE 90
Cdd:COG0602   19 GRPAVFVRLA---GCNLRCSWCDTKYAWDGEGGKRMSAEEILEEVAAL---GARHVVITGGEPLLQDDLAELLEALKDAG 92
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 657347733  91 ---ELEdlaitTNGSqLPtlapvlREAGVKRLNISL---DSLKRERFAE----LTRRD 138
Cdd:COG0602   93 yevALE-----TNGT-LP------IPAGIDWVTVSPklpSSGEEEDNREnlevLRRAD 138
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
71-185 1.18e-05

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


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 46.44  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  71 GEPLVRKGLPSLLSRLGAREELEDLAITTNGSQLP-TLAPVLREAGVKRLNISLDSLKRERFAELTRRDMLG-----QVV 144
Cdd:COG2100   98 GEPLLYPYIVELVKGLKEIKGVKVVSMQTNGTLLSeKLIDELEEAGLDRINLSIDTLDPEKAKKLAGTKWYDvekvlELA 177
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 657347733 145 AGIdaARSAGFDrIKLNSVIQKGRNDDEVLDLVNFAVERGL 185
Cdd:COG2100  178 EYI--ARETKID-LLIAPVWLPGINDEDIPKIIEWALEIGA 215
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
24-172 1.31e-04

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: 42.87  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  24 RCDFRCTYC---MSEDMV-----FAPRAQILT-LEELYAVadafISLGVKRIRV---TG-GEPLVRKGLPSLLSRLGARE 90
Cdd:COG0731   33 TCNFDCVYCqrgRTTDLTrerreFDDPEEILEeLIEFLRK----LPEEAREPDHitfSGsGEPTLYPNLGELIEEIKKLR 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  91 ELeDLAITTNGSQLpTLAPVLRE-AGVKRLNISLDSLKRERFAELTR---RDMLGQVVAGIDAARSAGFDRIklnsVIQ- 165
Cdd:COG0731  109 GI-KTALLTNGSLL-HRPEVREElLKADQVYPSLDAADEETFRKINRphpGLSWERIIEGLELFRKLYKGRT----VIEt 182
                        170
                 ....*....|
gi 657347733 166 ---KGRNDDE 172
Cdd:COG0731  183 mlvKGINDSE 192
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
17-105 2.02e-04

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: 42.64  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  17 LRLSVTdrCDFRCTYCMS-------EDMVFAPRAQILTLEEL-YAVADAFISL------GVKRIRVTGGEPLVRKGLPSL 82
Cdd:NF033640 114 LRFGNL--CNLKCRMCGPhsssswaKEAKKLGGPKLGDKKKIsWFEDEEFWKWleellpSLKEIYFAGGEPLLIKEHYKL 191
                         90       100
                 ....*....|....*....|....*.
gi 657347733  83 LSRL---GAREELEdLAITTNGSQLP 105
Cdd:NF033640 192 LEKLvekGRAKNIE-LRYNTNLTVLP 216
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
21-180 5.07e-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: 41.36  E-value: 5.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733   21 VTDRCDFRCTYCMsedmvFAPRAQ-------ILTLEELYAVADAFISLGVKRIRVTGGEPLVRKGLPSLLSRLgaREELE 93
Cdd:TIGR04251  10 LTEGCNLKCRHCW-----IDPKYQgegeqhpSLDPSLFRSIIRQAIPLGLTSVKLTGGEPLLHPAIGEILECI--GENNL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733   94 DLAITTNGSQL-PTLAPVLREAGVKRLNISLDSLKRERFAELTR-RDMLGQVVAGIDAARSAGFDRIKLNSVIQkgRNDD 171
Cdd:TIGR04251  83 QLSVETNGLLCtPQTARDLASCETPFVSVSLDGVDAATHDWMRGvKGAFDKAVRGIHNLVEAGIHPQIIMTVTR--RNVG 160

                  ....*....
gi 657347733  172 EVLDLVNFA 180
Cdd:TIGR04251 161 QMEQIVRLA 169
COG2108 COG2108
Uncharacterized radical SAM domain-containing protein [Function unknown];
21-76 7.48e-04

Uncharacterized radical SAM domain-containing protein [Function unknown];


Pssm-ID: 441711 [Multi-domain]  Cd Length: 361  Bit Score: 40.72  E-value: 7.48e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657347733  21 VTDRCDFRCTYC-MSE-----DMVFAPRAQILTLEELYAVADAFISLGVKrirVTGGEPLVR 76
Cdd:COG2108   33 ITGLCNRNCFYCpLSEerkgkDVIYANERPVESDEDVIEEARRMGALGAG---ITGGEPLLV 91
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
17-184 7.18e-03

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 37.47  E-value: 7.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  17 LRLSV-TDRCDFRCTYCMSEDMVFAPR---AQILTLEELYAVADAFISL--GVKRIRVTGGEPLV-RKGLPSLLSRlgAR 89
Cdd:COG1180   22 IRLSVfTQGCNLRCPYCHNPEISQGRPdaaGRELSPEELVEEALKDRGFldSCGGVTFSGGEPTLqPEFLLDLAKL--AK 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  90 EelEDLAIT--TNGSqlptlapvLREAGVKRL-------NISLDSLKRERFAELTRRDmLGQVVAGIDAARSAGFD---R 157
Cdd:COG1180  100 E--LGLHTAldTNGY--------IPEEALEELlpyldavNIDLKAFDDEFYRKLTGVS-LEPVLENLELLAESGVHveiR 168
                        170       180
                 ....*....|....*....|....*....
gi 657347733 158 IklnsVIQKGRNDD--EVLDLVNFAVERG 184
Cdd:COG1180  169 T----LVIPGLNDSeeELEAIARFIAELG 193
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
1-190 7.60e-03

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


Pssm-ID: 440655 [Multi-domain]  Cd Length: 394  Bit Score: 37.62  E-value: 7.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733   1 MPDSKLVDpfgRRITYLRLSV-TDR-CDFRCTYCMSeDMVFAPRAQILTLEELYAVADAFIS-LGVKRIRvtggeplvrk 77
Cdd:COG1032  161 FPAYDLLD---LEAYHRRASIeTSRgCPFGCSFCSI-SALYGRKVRYRSPESVVEEIEELVKrYGIREIF---------- 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657347733  78 glpsllsrlgareeLEDLAITTNGSQLPTLAPVLREAGVK---RLNISLDSLKRERFAELtRRDMLGQVVAGIDAARSAG 154
Cdd:COG1032  227 --------------FVDDNFNVDKKRLKELLEELIERGLNvsfPSEVRVDLLDEELLELL-KKAGCRGLFIGIESGSQRV 291
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 657347733 155 FDRIKlnsviqKGRNDDEVLDLVNFAVERGLDI--SFI 190
Cdd:COG1032  292 LKAMN------KGITVEDILEAVRLLKKAGIRVklYFI 323
 
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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