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Conserved domains on  [gi|2320288086|ref|WP_263660453|]
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MULTISPECIES: GTP 3',8-cyclase MoaA [unclassified Campylobacter]

Protein Classification

GTP 3',8-cyclase MoaA( domain architecture ID 11478261)

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

EC:  4.1.99.22
Gene Symbol:  moaA
PubMed:  8361352

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-322 3.66e-156

GTP 3',8-cyclase MoaA;


:

Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 439.96  E-value: 3.66e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086   1 MLVDSYGRVIDYLRISVTQRCNFRCLYCMPKTPFEWSAKENLLSFEELFMFVKVCIDEGVKKIRITGGEPLVRKDLHKFI 80
Cdd:PRK00164    7 QLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPFLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDLEDII 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  81 AMISEYKQDIDLALTTNASLLKQQAKDLKQAGLKRINISLDTLKEEVAFKLAQKNILKDVLNGINEALELGFN-IKFNTV 159
Cdd:PRK00164   87 AALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTpVKVNAV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 160 ALKGINDSEFIDLLEFAKARKSQIRFIEFMENYHAYGDLK--GLKSTEILNIIAQKYSFKQGQKSPNAPATIYELED-GY 236
Cdd:PRK00164  167 LMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRkhHLSGAEIRARLAERGWTLQPRARSGGPAQYFRHPDyGG 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 237 EFGIIDPHSHDFCDSCNRIRLSAEGLLIPCLYYDEALSIKKAIRN-KDIASACEVLKTVIKNKSEKNRWaeNDANQSSTR 315
Cdd:PRK00164  247 EIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSgADDEELAAAIREALQNKPEGHGL--HDGNTGPTR 324

                  ....*..
gi 2320288086 316 AFYQTGG 322
Cdd:PRK00164  325 HMSYIGG 331
 
Name Accession Description Interval E-value
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-322 3.66e-156

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 439.96  E-value: 3.66e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086   1 MLVDSYGRVIDYLRISVTQRCNFRCLYCMPKTPFEWSAKENLLSFEELFMFVKVCIDEGVKKIRITGGEPLVRKDLHKFI 80
Cdd:PRK00164    7 QLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPFLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDLEDII 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  81 AMISEYKQDIDLALTTNASLLKQQAKDLKQAGLKRINISLDTLKEEVAFKLAQKNILKDVLNGINEALELGFN-IKFNTV 159
Cdd:PRK00164   87 AALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTpVKVNAV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 160 ALKGINDSEFIDLLEFAKARKSQIRFIEFMENYHAYGDLK--GLKSTEILNIIAQKYSFKQGQKSPNAPATIYELED-GY 236
Cdd:PRK00164  167 LMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRkhHLSGAEIRARLAERGWTLQPRARSGGPAQYFRHPDyGG 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 237 EFGIIDPHSHDFCDSCNRIRLSAEGLLIPCLYYDEALSIKKAIRN-KDIASACEVLKTVIKNKSEKNRWaeNDANQSSTR 315
Cdd:PRK00164  247 EIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSgADDEELAAAIREALQNKPEGHGL--HDGNTGPTR 324

                  ....*..
gi 2320288086 316 AFYQTGG 322
Cdd:PRK00164  325 HMSYIGG 331
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
1-322 5.19e-148

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: 419.08  E-value: 5.19e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086   1 MLVDSYGRVIDYLRISVTQRCNFRCLYCMPKTPFEWSAKENLLSFEELFMFVKVCIDEGVKKIRITGGEPLVRKDLHKFI 80
Cdd:COG2896     4 PLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPELI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  81 AMISEYKQDIDLALTTNASLLKQQAKDLKQAGLKRINISLDTLKEEVAFKLAQKNILKDVLNGINEALELGF-NIKFNTV 159
Cdd:COG2896    84 ARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLtPVKINAV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 160 ALKGINDSEFIDLLEFAKARKSQIRFIEFME--NYHAYGDLKGLKSTEILNIIAQKYSFKQGQKSPNAPATIYELEDG-Y 236
Cdd:COG2896   164 VMRGVNDDEILDLLEFAKERGIDLRFIELMPlgEGGGWRRDQVVSAAEILERLEARFPLEPLPARGGGPARYYRVPGGgG 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 237 EFGIIDPHSHDFCDSCNRIRLSAEGLLIPCLYYDEALSIKKAIRN-KDIASACEVLKTVIKNKSEKNRWAENDANQsSTR 315
Cdd:COG2896   244 RIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSgASDEELAEAIREAIARKPEGHGFDEGDFPQ-PKR 322

                  ....*..
gi 2320288086 316 AFYQTGG 322
Cdd:COG2896   323 SMSAIGG 329
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
2-322 1.41e-135

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: 387.74  E-value: 1.41e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086   2 LVDSYGRVIDYLRISVTQRCNFRCLYCMPK-TPFEWSAKENLLSFEELFMFVKVCIDEGVKKIRITGGEPLVRKDLHKFI 80
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEgGGLDFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  81 AMISEYKQDIDLALTTNASLLKQQAKDLKQAGLKRINISLDTLKEEVAFKLAQKNI-LKDVLNGINEALELGF-NIKFNT 158
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGrLEQVLAGIDAALAAGLePVKLNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 159 VALKGINDSEFIDLLEFAKARKSQIRFIEFMENYHAYG--DLKGLKSTEILNIIAQKYSFKQ--GQKSPNAPATIYE--L 232
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGwrEKKFVSADEILERLEQAFGPLEpvPSPRGNGPAPAYRwrL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 233 EDGY-EFGIIDPHSHDFCDSCNRIRLSAEGLLIPCLYYDEALSIKKAIRN-KDIASACEVLKTVIKNKSEKNRWAE--ND 308
Cdd:TIGR02666 241 PGGKgRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRGgASDALLEAIIQAILQKKPEGHSFLRftSP 320
                         330
                  ....*....|....
gi 2320288086 309 ANQSSTRAFYQTGG 322
Cdd:TIGR02666 321 ANKRRKRAMSQIGG 334
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
182-302 1.06e-36

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: 128.10  E-value: 1.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 182 QIRFIEFMENYHAYGD--LKGLKSTEILNIIAQKYSFKQGQKSPNAPATIYELEDGY-EFGIIDPHSHDFCDSCNRIRLS 258
Cdd:pfam06463   2 DLRFIELMPVGEGNGWrrKKFVSLDEILERIEARFPLLPARKRTGGPAKRYRIPGGGgRIGFIAPVSNPFCASCNRLRLT 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2320288086 259 AEGLLIPCLYYDEALSIKKAIRNKDIASAC-EVLKTVIKNKSEKN 302
Cdd:pfam06463  82 ADGKLKTCLFAEDGIDLRDALRSGDDDEELrEAIREALARKPPRH 126
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
244-312 2.75e-21

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: 85.67  E-value: 2.75e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 244 HSHDFCDSCNRIRLSAEGLLIPCLYYDEALSIKKAIRNK-DIASACEVLKTVIKNKSEKNRWAENDANQS 312
Cdd:cd21117     1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGaSDEELREAIRAAVQRKPERHSLERGDSGTR 70
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
12-178 1.11e-13

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: 68.97  E-value: 1.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086   12 YLRISVTQRCNFRCLYCMPKT--PFEWSAKENLLSFEELFMFVKVCIDEGVKKIRITGGEPLV--RKDLHKFIAMISEYK 87
Cdd:smart00729   2 LALYIITRGCPRRCTFCSFPSlrGKLRSRYLEALVREIELLAEKGEKEGLVGTVFIGGGTPTLlsPEQLEELLEAIREIL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086   88 ---QDIDLALTTNASLL-KQQAKDLKQAGLKRINISLDTLKEEVAFKLAQKNILKDVLNGINEALELGFnIKFNT---VA 160
Cdd:smart00729  82 glaKDVEITIETRPDTLtEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAGP-IKVSTdliVG 160
                          170
                   ....*....|....*...
gi 2320288086  161 LKGINDSEFIDLLEFAKA 178
Cdd:smart00729 161 LPGETEEDFEETLKLLKE 178
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
10-125 7.05e-09

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: 56.51  E-value: 7.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  10 IDYLRISVTQRCNFRCLYCMP------------KTPFEWS--AKENLLSFEELFMFVKVCIDEgVKKIRITGGEPLVRKD 75
Cdd:NF033640  109 PRYLDLRFGNLCNLKCRMCGPhsssswakeakkLGGPKLGdkKKISWFEDEEFWKWLEELLPS-LKEIYFAGGEPLLIKE 187
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2320288086  76 LHKFIAMISE--YKQDIDLALTTNASLLKQQAKD----LKQAGLKRINISLDTLKE 125
Cdd:NF033640  188 HYKLLEKLVEkgRAKNIELRYNTNLTVLPDKLKDlldlWKKFKSVSISASIDGVGE 243
 
Name Accession Description Interval E-value
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-322 3.66e-156

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 439.96  E-value: 3.66e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086   1 MLVDSYGRVIDYLRISVTQRCNFRCLYCMPKTPFEWSAKENLLSFEELFMFVKVCIDEGVKKIRITGGEPLVRKDLHKFI 80
Cdd:PRK00164    7 QLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPFLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDLEDII 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  81 AMISEYKQDIDLALTTNASLLKQQAKDLKQAGLKRINISLDTLKEEVAFKLAQKNILKDVLNGINEALELGFN-IKFNTV 159
Cdd:PRK00164   87 AALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTpVKVNAV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 160 ALKGINDSEFIDLLEFAKARKSQIRFIEFMENYHAYGDLK--GLKSTEILNIIAQKYSFKQGQKSPNAPATIYELED-GY 236
Cdd:PRK00164  167 LMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRkhHLSGAEIRARLAERGWTLQPRARSGGPAQYFRHPDyGG 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 237 EFGIIDPHSHDFCDSCNRIRLSAEGLLIPCLYYDEALSIKKAIRN-KDIASACEVLKTVIKNKSEKNRWaeNDANQSSTR 315
Cdd:PRK00164  247 EIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSgADDEELAAAIREALQNKPEGHGL--HDGNTGPTR 324

                  ....*..
gi 2320288086 316 AFYQTGG 322
Cdd:PRK00164  325 HMSYIGG 331
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
1-322 5.19e-148

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: 419.08  E-value: 5.19e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086   1 MLVDSYGRVIDYLRISVTQRCNFRCLYCMPKTPFEWSAKENLLSFEELFMFVKVCIDEGVKKIRITGGEPLVRKDLHKFI 80
Cdd:COG2896     4 PLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPELI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  81 AMISEYKQDIDLALTTNASLLKQQAKDLKQAGLKRINISLDTLKEEVAFKLAQKNILKDVLNGINEALELGF-NIKFNTV 159
Cdd:COG2896    84 ARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLtPVKINAV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 160 ALKGINDSEFIDLLEFAKARKSQIRFIEFME--NYHAYGDLKGLKSTEILNIIAQKYSFKQGQKSPNAPATIYELEDG-Y 236
Cdd:COG2896   164 VMRGVNDDEILDLLEFAKERGIDLRFIELMPlgEGGGWRRDQVVSAAEILERLEARFPLEPLPARGGGPARYYRVPGGgG 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 237 EFGIIDPHSHDFCDSCNRIRLSAEGLLIPCLYYDEALSIKKAIRN-KDIASACEVLKTVIKNKSEKNRWAENDANQsSTR 315
Cdd:COG2896   244 RIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSgASDEELAEAIREAIARKPEGHGFDEGDFPQ-PKR 322

                  ....*..
gi 2320288086 316 AFYQTGG 322
Cdd:COG2896   323 SMSAIGG 329
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
2-322 1.41e-135

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: 387.74  E-value: 1.41e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086   2 LVDSYGRVIDYLRISVTQRCNFRCLYCMPK-TPFEWSAKENLLSFEELFMFVKVCIDEGVKKIRITGGEPLVRKDLHKFI 80
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEgGGLDFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  81 AMISEYKQDIDLALTTNASLLKQQAKDLKQAGLKRINISLDTLKEEVAFKLAQKNI-LKDVLNGINEALELGF-NIKFNT 158
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGrLEQVLAGIDAALAAGLePVKLNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 159 VALKGINDSEFIDLLEFAKARKSQIRFIEFMENYHAYG--DLKGLKSTEILNIIAQKYSFKQ--GQKSPNAPATIYE--L 232
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGwrEKKFVSADEILERLEQAFGPLEpvPSPRGNGPAPAYRwrL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 233 EDGY-EFGIIDPHSHDFCDSCNRIRLSAEGLLIPCLYYDEALSIKKAIRN-KDIASACEVLKTVIKNKSEKNRWAE--ND 308
Cdd:TIGR02666 241 PGGKgRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRGgASDALLEAIIQAILQKKPEGHSFLRftSP 320
                         330
                  ....*....|....
gi 2320288086 309 ANQSSTRAFYQTGG 322
Cdd:TIGR02666 321 ANKRRKRAMSQIGG 334
moaA_archaeal TIGR02668
probable molybdenum cofactor biosynthesis protein A, archaeal; This model describes an ...
2-300 2.25e-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: 218.33  E-value: 2.25e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086   2 LVDSYGRVIDYLRISVTQRCNFRCLYC-MPKTPFEWsakENLLSFEELFMFVKVCIDEGVKKIRITGGEPLVRKDLHKFI 80
Cdd:TIGR02668   1 LYDRFGRPVTSLRISVTDRCNLSCFYChMEGEDRSG---GNELSPEEIERIVRVASEFGVRKVKITGGEPLLRKDLIEII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  81 AMISEYkQDIDLALTTNASLLKQQAKDLKQAGLKRINISLDTLKEEVAFKLAQKNILKDVLNGINEALELGFN-IKFNTV 159
Cdd:TIGR02668  78 RRIKDY-GIKDVSMTTNGILLEKLAKKLKEAGLDRVNVSLDTLDPEKYKKITGRGALDRVIEGIESAVDAGLTpVKLNMV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 160 ALKGINDSEFIDLLEFAKARKSQIRFIEFM------ENYHAYGDlkglKSTEILNIIAQKYSFKQGQKSPNAPatIYELE 233
Cdd:TIGR02668 157 VLKGINDNEIPDMVEFAAEGGAILQLIELMppgegeKEFKKYHE----DIDPIEEELEKMADRVRTRRMHNRP--KYFIP 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2320288086 234 DGYEFGIIDP-HSHDFCDSCNRIRLSAEGLLIPCLYYDEAL-SIKKAIRNKDIASACEVLKTVIKNKSE 300
Cdd:TIGR02668 231 GGVEVEVVKPmDNPVFCAHCTRLRLTSDGKLKTCLLRDDNLvDILDALRNGEDDELREAFREAVARREP 299
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
1-280 4.27e-69

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 219.63  E-value: 4.27e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086   1 MLVDSYGRVIDYLRISVTQRCNFRCLYCMPKTPFEWSAKENLLSFEELFMFVKVCIDEGVKKIRITGGEPLVRKDLHKFI 80
Cdd:PLN02951   48 MLVDSFGRRHNYLRISLTERCNLRCQYCMPEEGVELTPKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDIC 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  81 AMISEYKQDIDLALTTNASLLKQQAKDLKQAGLKRINISLDTLKEEVAFKLAQKNILKDVLNGINEALELGFN-IKFNTV 159
Cdd:PLN02951  128 LQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTRRKGHDRVLESIDTAIELGYNpVKVNCV 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 160 ALKGINDSEFIDLLEFAKARKSQIRFIEFME-NYHAYGDLKGLKSTEILNIIAQKY-SFKQGQKSPNAPATIYELeDGY- 236
Cdd:PLN02951  208 VMRGFNDDEICDFVELTRDKPINVRFIEFMPfDGNVWNVKKLVPYAEMMDRIEQRFpSLKRLQDHPTDTAKNFRI-DGHc 286
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2320288086 237 -EFGIIDPHSHDFCDSCNRIRLSAEGLLIPCLYYDEALSIKKAIR 280
Cdd:PLN02951  287 gSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSLRDALR 331
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
182-302 1.06e-36

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: 128.10  E-value: 1.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 182 QIRFIEFMENYHAYGD--LKGLKSTEILNIIAQKYSFKQGQKSPNAPATIYELEDGY-EFGIIDPHSHDFCDSCNRIRLS 258
Cdd:pfam06463   2 DLRFIELMPVGEGNGWrrKKFVSLDEILERIEARFPLLPARKRTGGPAKRYRIPGGGgRIGFIAPVSNPFCASCNRLRLT 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2320288086 259 AEGLLIPCLYYDEALSIKKAIRNKDIASAC-EVLKTVIKNKSEKN 302
Cdd:pfam06463  82 ADGKLKTCLFAEDGIDLRDALRSGDDDEELrEAIREALARKPPRH 126
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
12-159 8.63e-31

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: 113.84  E-value: 8.63e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  12 YLRISVTQRCNFRCLYCMPKtpfEWSAKENLLSFEELFMFVKVCIDEGVKKIRITGGEPLVRKDLHKFIAMISEYkqDID 91
Cdd:COG0535     1 RLQIELTNRCNLRCKHCYAD---AGPKRPGELSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAKEL--GIR 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  92 LALTTNASLL-KQQAKDLKQAGLKRINISLDTLKEEVAFKLA-QKNILKDVLNGINEALELGFNIKFNTV 159
Cdd:COG0535    76 VNLSTNGTLLtEELAERLAEAGLDHVTISLDGVDPETHDKIRgVPGAFDKVLEAIKLLKEAGIPVGINTV 145
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
17-172 4.40e-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: 4.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  17 VTQRCNFRCLYCMPKTPFEWSaKENLLSFEELFMFVKVCIDEGVKKIRITGGEPLVRKDLHKFIAMISE--YKQDIDLAL 94
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARG-KGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKleLAEGIRITL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  95 TTNASLL-KQQAKDLKQAGLKRINISLDTLKEEVAFKLAQKNILKDVLNGINEALELGF-NIKFNTVALKGINDSEFIDL 172
Cdd:pfam04055  80 ETNGTLLdEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIpVVTDNIVGLPGETDEDLEET 159
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
244-312 2.75e-21

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: 85.67  E-value: 2.75e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086 244 HSHDFCDSCNRIRLSAEGLLIPCLYYDEALSIKKAIRNK-DIASACEVLKTVIKNKSEKNRWAENDANQS 312
Cdd:cd21117     1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGaSDEELREAIRAAVQRKPERHSLERGDSGTR 70
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
15-211 1.54e-20

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: 87.77  E-value: 1.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  15 ISVTQRCNFRCLYCmpktPFEWSAKENLLSFEELFMFVKVC---IDEGVKKIRITGGEPLVRKDLHKFIAMISEYKQDID 91
Cdd:cd01335     1 LELTRGCNLNCGFC----SNPASKGRGPESPPEIEEILDIVleaKERGVEVVILTGGEPLLYPELAELLRRLKKELPGFE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  92 LALTTNASLLKQ-QAKDLKQAGLKRINISLDTLKEEVAFKLAQKNI-LKDVLNGINEALELGFNIKFNTVALKGINDSE- 168
Cdd:cd01335    77 ISIETNGTLLTEeLLKELKELGLDGVGVSLDSGDEEVADKIRGSGEsFKERLEALKELREAGLGLSTTLLVGLGDEDEEd 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2320288086 169 ----FIDLLEFAKARKSQIRFIEFMENYHAYGDLKGLKSTEILNIIA 211
Cdd:cd01335   157 dleeLELLAEFRSPDRVSLFRLLPEEGTPLELAAPVVPAEKLLRLIA 203
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
12-178 1.11e-13

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: 68.97  E-value: 1.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086   12 YLRISVTQRCNFRCLYCMPKT--PFEWSAKENLLSFEELFMFVKVCIDEGVKKIRITGGEPLV--RKDLHKFIAMISEYK 87
Cdd:smart00729   2 LALYIITRGCPRRCTFCSFPSlrGKLRSRYLEALVREIELLAEKGEKEGLVGTVFIGGGTPTLlsPEQLEELLEAIREIL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086   88 ---QDIDLALTTNASLL-KQQAKDLKQAGLKRINISLDTLKEEVAFKLAQKNILKDVLNGINEALELGFnIKFNT---VA 160
Cdd:smart00729  82 glaKDVEITIETRPDTLtEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAGP-IKVSTdliVG 160
                          170
                   ....*....|....*...
gi 2320288086  161 LKGINDSEFIDLLEFAKA 178
Cdd:smart00729 161 LPGETEEDFEETLKLLKE 178
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
21-177 9.89e-12

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


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 64.93  E-value: 9.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  21 CNFRCLYCM----PKTPFEWSA----KENLLS-FEELFMF----VKVCIDeGVkkiritgGEPLVRKDLHKFIAMISEYK 87
Cdd:COG2100    46 CNLNCIFCSvdagPHSRTRQAEyivdPEYLVEwFEKVARFkgkgVEAHID-GV-------GEPLLYPYIVELVKGLKEIK 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  88 QDIDLALTTNASLL-KQQAKDLKQAGLKRINISLDTLKEEVAFKLAQKNILkdvlnGINEALELGFNIKFNT-------- 158
Cdd:COG2100   118 GVKVVSMQTNGTLLsEKLIDELEEAGLDRINLSIDTLDPEKAKKLAGTKWY-----DVEKVLELAEYIARETkidlliap 192
                         170
                  ....*....|....*....
gi 2320288086 159 VALKGINDSEFIDLLEFAK 177
Cdd:COG2100   193 VWLPGINDEDIPKIIEWAL 211
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
15-214 2.45e-10

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 60.77  E-value: 2.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  15 ISVTQRCNFRCLYCmpktpFEWSAKEN---LLSFEELFMFVKVCID--EGVKKIRIT--GGEPLVRKDL-HKFIAMISEY 86
Cdd:COG0641     5 LKPTSRCNLRCSYC-----YYSEGDEGsrrRMSEETAEKAIDFLIEssGPGKELTITffGGEPLLNFDFiKEIVEYARKY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  87 ---KQDIDLALTTNASLLKQQ-AKDLKQAGLkRINISLDTLKEevafkLAQKN-ILKD-------VLNGINEALELGFNI 154
Cdd:COG0641    80 akkGKKIRFSIQTNGTLLDDEwIDFLKENGF-SVGISLDGPKE-----IHDRNrVTKNgkgsfdrVMRNIKLLKEHGVEV 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2320288086 155 KFNTVALKGiNDSEFIDLLEFAKAR-KSQIRFIEFMENYHAYGDLKGLKSTEILNIIAQKY 214
Cdd:COG0641   154 NIRCTVTRE-NLDDPEELYDFLKELgFRSIQFNPVVEEGEADYSLTPEDYGEFLIELFDEW 213
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
20-187 2.42e-09

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: 56.74  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  20 RCNFRCLYC--MPKTPFEWSAKEnLLSFEELFMFVKVCIDEGVKKIR------ITG-GEPLVRKDLHKFIAMISEYkQDI 90
Cdd:COG0731    33 TCNFDCVYCqrGRTTDLTRERRE-FDDPEEILEELIEFLRKLPEEARepdhitFSGsGEPTLYPNLGELIEEIKKL-RGI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  91 DLALTTNASLLKQQAkdlKQAGLKRIN---ISLDTLKEEVaFKLAQKNILKDVLNGINEALELgFNIKFN------TVAL 161
Cdd:COG0731   111 KTALLTNGSLLHRPE---VREELLKADqvyPSLDAADEET-FRKINRPHPGLSWERIIEGLEL-FRKLYKgrtvieTMLV 185
                         170       180
                  ....*....|....*....|....*..
gi 2320288086 162 KGINDSEfIDLLEFAKA-RKSQIRFIE 187
Cdd:COG0731   186 KGINDSE-EELEAYAELiKRINPDFVE 211
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
10-217 2.82e-09

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 56.73  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  10 IDY---LRISV-TQRCNFRCLYCM-PKT-PFEWSAKENLLSFEELFMFVK--VCIDEGVKKIRITGGEPLVRKD-LHKFI 80
Cdd:COG1180    16 VDGpgsIRLSVfTQGCNLRCPYCHnPEIsQGRPDAAGRELSPEELVEEALkdRGFLDSCGGVTFSGGEPTLQPEfLLDLA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  81 AMISEykQDIDLALTTNASLLKQQAKDLkqagLKRIN-ISLDtLK---EEVAFKLAQKNiLKDVLNGINEALELGFNIKF 156
Cdd:COG1180    96 KLAKE--LGLHTALDTNGYIPEEALEEL----LPYLDaVNID-LKafdDEFYRKLTGVS-LEPVLENLELLAESGVHVEI 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2320288086 157 NTVALKGINDS--EFIDLLEFAKARKSQIRfIEFMeNYHAYGDLKGLKST---EILNI--IAQKYSFK 217
Cdd:COG1180   168 RTLVIPGLNDSeeELEAIARFIAELGDVIP-VHLL-PFHPLYKLEDVPPPspeTLERAreIAREYGLK 233
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
10-125 7.05e-09

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: 56.51  E-value: 7.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  10 IDYLRISVTQRCNFRCLYCMP------------KTPFEWS--AKENLLSFEELFMFVKVCIDEgVKKIRITGGEPLVRKD 75
Cdd:NF033640  109 PRYLDLRFGNLCNLKCRMCGPhsssswakeakkLGGPKLGdkKKISWFEDEEFWKWLEELLPS-LKEIYFAGGEPLLIKE 187
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2320288086  76 LHKFIAMISE--YKQDIDLALTTNASLLKQQAKD----LKQAGLKRINISLDTLKE 125
Cdd:NF033640  188 HYKLLEKLVEkgRAKNIELRYNTNLTVLPDKLKDlldlWKKFKSVSISASIDGVGE 243
BioB COG0502
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
25-122 3.23e-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: 48.12  E-value: 3.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  25 CLYCmP-----KTPFEwsaKENLLSFEELFMFVKVCIDEGVKKIRI-TGGEPLVRKDLHKFIAMISEYKQDIDLALTtnA 98
Cdd:COG0502    54 CKYC-GqsahnKTGIE---RYRLLSVEEILEAARAAKEAGARRFCLvASGRDPSDRDFEKVLEIVRAIKEELGLEVC--A 127
                          90       100
                  ....*....|....*....|....*..
gi 2320288086  99 SL--LKQ-QAKDLKQAGLKRINISLDT 122
Cdd:COG0502   128 SLgeLSEeQAKRLKEAGVDRYNHNLET 154
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
12-177 1.25e-05

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


Pssm-ID: 440655 [Multi-domain]  Cd Length: 394  Bit Score: 46.48  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  12 YLRISV-TQR-CNFRCLYCMpkTPFEWSAKENLLSFEELFMFVKVCIDE-GVKKIRITGGEPLV-RKDLHKFIAMISEYK 87
Cdd:COG1032   173 HRRASIeTSRgCPFGCSFCS--ISALYGRKVRYRSPESVVEEIEELVKRyGIREIFFVDDNFNVdKKRLKELLEELIERG 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  88 QDIDLALTTNASLLKQQ-AKDLKQAGLKRINISLDTLKEEVAfKLAQKNI-LKDVLNGINEALELGFNIKFN-TVALKGI 164
Cdd:COG1032   251 LNVSFPSEVRVDLLDEElLELLKKAGCRGLFIGIESGSQRVL-KAMNKGItVEDILEAVRLLKKAGIRVKLYfIIGLPGE 329
                         170
                  ....*....|...
gi 2320288086 165 NDSEFIDLLEFAK 177
Cdd:COG1032   330 TEEDIEETIEFIK 342
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
18-186 1.66e-05

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: 45.13  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  18 TQRCNFRCLYCmpKTPFEWSAKE-NLLSFEELFMFVKvciDEGVKKIRITGGEPLVRKDLHKFIAMISEykQDIDLALTT 96
Cdd:COG0602    27 LAGCNLRCSWC--DTKYAWDGEGgKRMSAEEILEEVA---ALGARHVVITGGEPLLQDDLAELLEALKD--AGYEVALET 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  97 NASLlkqqakDLkQAGLKRINISldtLKEEVAFKLAQKNILKDVLNGINEalelgfnIKFnTVAlkgiNDSEFIDLLEFA 176
Cdd:COG0602   100 NGTL------PI-PAGIDWVTVS---PKLPSSGEEEDNRENLEVLRRADE-------LKF-VVA----DETDLEEAEELL 157
                         170
                  ....*....|
gi 2320288086 177 KARKSQIRFI 186
Cdd:COG0602   158 ARLDFRCPVY 167
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
15-101 8.23e-05

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: 43.69  E-value: 8.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  15 ISVTQRCNFRCLYCM-----PKTPFEWSAKENLLSFEELfmfvKVCideGVKKIRITGGEPLVRKDLHKFIAMIseYKQD 89
Cdd:TIGR04250   7 IDITGRCNLRCRYCShfssaAETPTDLETAEWLRFFREL----NRC---SVLRVVLSGGEPFMRSDFREIIDGI--VKNR 77
                          90
                  ....*....|..
gi 2320288086  90 IDLALTTNASLL 101
Cdd:TIGR04250  78 MRFSILSNGTLI 89
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
21-108 2.60e-04

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


Pssm-ID: 444038  Cd Length: 261  Bit Score: 41.90  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  21 CNFRCLYCmpktpfeWSAKE--------NLLSFEELF-MFVKVCIDEGVKKIRITGGEP-LVRKDLHKFIAMISEYkqDI 90
Cdd:COG5014    50 CNLRCGFC-------WSWRFrdfpltigKFYSPEEVAeRLIEIARERGYRQVRLSGGEPtIGFEHLLKVLELFSER--GL 120
                          90       100
                  ....*....|....*....|.
gi 2320288086  91 DLALTTNASLL---KQQAKDL 108
Cdd:COG5014   121 TFILETNGILIgydRELAREL 141
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
17-151 5.37e-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: 5.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  17 VTQRCNFRCLYCMpKTPFEWSAKENLLSFEelFMFVKVCIDE----GVKKIRITGGEPLVRKDLHKFIAMISEykQDIDL 92
Cdd:TIGR04251  10 LTEGCNLKCRHCW-IDPKYQGEGEQHPSLD--PSLFRSIIRQaiplGLTSVKLTGGEPLLHPAIGEILECIGE--NNLQL 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2320288086  93 ALTTNASLLKQQ-AKDLKQAGLKRINISLDTLKEEV-AFKLAQKNILKDVLNGINEALELG 151
Cdd:TIGR04251  85 SVETNGLLCTPQtARDLASCETPFVSVSLDGVDAAThDWMRGVKGAFDKAVRGIHNLVEAG 145
viperin TIGR04278
antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, ...
18-127 1.59e-03

antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, Iterferon-inducible) is a radical SAM enzyme found in human and other vertebrates. It is both induced by interferon and demonstrably active in blocking replication by several types of virus, apparently by modifying lipid chemistries in lipid droplets and membrane rafts.


Pssm-ID: 212001  Cd Length: 347  Bit Score: 39.71  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  18 TQRCNFRCLYCM--PKTPFewsakenLLSFEELFMFVKVCIDEGVKKIRITGGEPLVRkDLHKFIAMISEY-KQDIDL-- 92
Cdd:TIGR04278  66 TRQCNYKCGFCFhtAKTSF-------VLPLEEAKRGLRLLKEAGMEKINFSGGEPFLH-DRGEFLGKLVQFcKEELQLps 137
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2320288086  93 -ALTTNASLLKQqaKDLKQAG--LKRINISLDTLKEEV 127
Cdd:TIGR04278 138 vSIVSNGSLIRE--RWFKKYGeyLDILAISCDSFDEQV 173
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
21-121 3.45e-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: 37.15  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  21 CNFRCLYCM-PKTpfeWSAKENLLSFEEL-FMFVKVCIDEGVKKIRITGGEPLV-RKDLHKFIAMISEYKQDIDLAL--- 94
Cdd:pfam13353  15 CNHHCKGCFnPET---WDFKYGKPFTEELeDEIIEDLAKPYIQGLTLSGGEPLLnAEALLELVKRVREECPEKDIWLwtg 91
                          90       100
                  ....*....|....*....|....*..
gi 2320288086  95 TTNASLLKQQAKDLkqagLKRINISLD 121
Cdd:pfam13353  92 YTFEELQSKDQLEL----LKLIDVLVD 114
Fer4_14 pfam13394
4Fe-4S single cluster domain;
20-124 4.93e-03

4Fe-4S single cluster domain;


Pssm-ID: 433171 [Multi-domain]  Cd Length: 115  Bit Score: 36.19  E-value: 4.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2320288086  20 RCNFRCLYCMPKTPFEWSAKE-NLLSFEELFMFVKVCIDEGVKKIRITGGEPLVRKDLH---KFIAMISEYKQDIDLALT 95
Cdd:pfam13394   5 GCNHSCPGCDNKETWKFNYGEpFTEELEDQIIADLKDSYIKRQGLVLTGGEPLHPWNLPvllKLLKRVKEEYPSKDIWLE 84
                          90       100
                  ....*....|....*....|....*....
gi 2320288086  96 TNASLlkqqAKDLKQAGLKRINISLDTLK 124
Cdd:pfam13394  85 TGYTL----AIDFEYPDTEEQLFTLSVID 109
 
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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