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Conserved domains on  [gi|161484622|ref|NP_082740|]
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molybdenum cofactor biosynthesis protein 1 isoform 2 [Mus musculus]

Protein Classification

PLN02951 family protein( domain architecture ID 11477312)

PLN02951 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
16-385 0e+00

Molybderin biosynthesis protein CNX2


:

Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 602.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  16 SNARGCSSGAPVTQPRPGEP--SRPTREGLSLRLQFLQEHAAPFSAFLTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGV 93
Cdd:PLN02951   2 SKLADLRLGFRSSSFQLQEPgsSIFSASSSYAADQVDPEASNPVSDMLVDSFGRRHNYLRISLTERCNLRCQYCMPEEGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  94 PLTPKADLLTTEEILTLARLFVKEGVDKIRLTGGEPLIRPDVVDIVARLHGLEGLRTIGLTTNGINLARLLPRLQQAGLN 173
Cdd:PLN02951  82 ELTPKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDICLQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 174 AVNISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYKPVKVNCVVMRGLNEDELLDFVALTEGLPLDVRFIEYMPFDG 253
Cdd:PLN02951 162 SLNISLDTLVPAKFEFLTRRKGHDRVLESIDTAIELGYNPVKVNCVVMRGFNDDEICDFVELTRDKPINVRFIEFMPFDG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 254 NKWNFKKMVSYKEMLDTIRQRWPGLEKLPEEDSSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGN 333
Cdd:PLN02951 242 NVWNVKKLVPYAEMMDRIEQRFPSLKRLQDHPTDTAKNFRIDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGP 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 161484622 334 SEVSLRDHLRAGASEEELLRIIGAAVGRKKRQHAGMFNIAQMKNRPMILIGG 385
Cdd:PLN02951 322 SEVSLRDALRSGADDDELREIIGAAVKRKKAAHAGMFDLAKTANRPMIHIGG 373
 
Name Accession Description Interval E-value
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
16-385 0e+00

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 602.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  16 SNARGCSSGAPVTQPRPGEP--SRPTREGLSLRLQFLQEHAAPFSAFLTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGV 93
Cdd:PLN02951   2 SKLADLRLGFRSSSFQLQEPgsSIFSASSSYAADQVDPEASNPVSDMLVDSFGRRHNYLRISLTERCNLRCQYCMPEEGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  94 PLTPKADLLTTEEILTLARLFVKEGVDKIRLTGGEPLIRPDVVDIVARLHGLEGLRTIGLTTNGINLARLLPRLQQAGLN 173
Cdd:PLN02951  82 ELTPKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDICLQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 174 AVNISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYKPVKVNCVVMRGLNEDELLDFVALTEGLPLDVRFIEYMPFDG 253
Cdd:PLN02951 162 SLNISLDTLVPAKFEFLTRRKGHDRVLESIDTAIELGYNPVKVNCVVMRGFNDDEICDFVELTRDKPINVRFIEFMPFDG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 254 NKWNFKKMVSYKEMLDTIRQRWPGLEKLPEEDSSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGN 333
Cdd:PLN02951 242 NVWNVKKLVPYAEMMDRIEQRFPSLKRLQDHPTDTAKNFRIDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGP 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 161484622 334 SEVSLRDHLRAGASEEELLRIIGAAVGRKKRQHAGMFNIAQMKNRPMILIGG 385
Cdd:PLN02951 322 SEVSLRDALRSGADDDELREIIGAAVKRKKAAHAGMFDLAKTANRPMIHIGG 373
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
61-385 3.37e-176

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: 493.04  E-value: 3.37e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  61 LTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKADLLTTEEILTLARLFVKEGVDKIRLTGGEPLIRPDVVDIVA 140
Cdd:COG2896    5 LIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPELIA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 141 RLHGLEGLRTIGLTTNGINLARLLPRLQQAGLNAVNISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYKPVKVNCVV 220
Cdd:COG2896   85 RLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVKINAVV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 221 MRGLNEDELLDFVALTEGLPLDVRFIEYMPF-DGNKWNFKKMVSYKEMLDTIRQRWPgLEKLPEEDSSTAKAFKIPGFQG 299
Cdd:COG2896  165 MRGVNDDEILDLLEFAKERGIDLRFIELMPLgEGGGWRRDQVVSAAEILERLEARFP-LEPLPARGGGPARYYRVPGGGG 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 300 QISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEEELLRIIGAAVGRKKRQHagMFNIAQMK--N 377
Cdd:COG2896  244 RIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGH--GFDEGDFPqpK 321

                 ....*...
gi 161484622 378 RPMILIGG 385
Cdd:COG2896  322 RSMSAIGG 329
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
61-385 1.40e-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: 408.15  E-value: 1.40e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622   61 LTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVP-LTPKADLLTTEEILTLARLFVKEGVDKIRLTGGEPLIRPDVVDIV 139
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGLdFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  140 ARLHGLEGLRTIGLTTNGINLARLLPRLQQAGLNAVNISLDTLVPAKFEFIVRRKG-FHKVMEGIHKAIELGYKPVKVNC 218
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGrLEQVLAGIDAALAAGLEPVKLNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  219 VVMRGLNEDELLDFVALTEGLPLDVRFIEYMPFD-GNKWNFKKMVSYKEMLDTIRQRWPGLEKLP-EEDSSTAKAFK--I 294
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGeGNGWREKKFVSADEILERLEQAFGPLEPVPsPRGNGPAPAYRwrL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  295 PGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEEELLRIIGAAVGRKKRQHAGMFNIA- 373
Cdd:TIGR02666 241 PGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRGGASDALLEAIIQAILQKKPEGHSFLRFTSp 320
                         330
                  ....*....|....
gi 161484622  374 --QMKNRPMILIGG 385
Cdd:TIGR02666 321 anKRRKRAMSQIGG 334
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
241-367 1.80e-60

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: 191.28  E-value: 1.80e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  241 LDVRFIEYMPFD-GNKWNFKKMVSYKEMLDTIRQRWPgLEKLPEEDSSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLR 319
Cdd:pfam06463   1 IDLRFIELMPVGeGNGWRRKKFVSLDEILERIEARFP-LLPARKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLR 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 161484622  320 ITADGNLKVCLFGNSEVSLRDHLRAGASEEELLRIIGAAVGRKKRQHA 367
Cdd:pfam06463  80 LTADGKLKTCLFAEDGIDLRDALRSGDDDEELREAIREALARKPPRHS 127
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
307-376 7.22e-37

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: 128.05  E-value: 7.22e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 307 MSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEEELLRIIGAAVGRKKRQHAGMFNIAQMK 376
Cdd:cd21117    1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGASDEELREAIRAAVQRKPERHSLERGDSGTR 70
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
70-271 1.49e-11

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: 63.19  E-value: 1.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622    70 SYLRISLTEKCNLRCQYCM--PEEGVPLTPKADLLtTEEILTLARLFVKEG-VDKIRLTGGEPLIRP--DVVDIVARLHG 144
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSfpSLRGKLRSRYLEAL-VREIELLAEKGEKEGlVGTVFIGGGTPTLLSpeQLEELLEAIRE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622   145 LEGLRTIGLTTNGINL----ARLLPRLQQAGLNAVNISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGykPVKVNCVV 220
Cdd:smart00729  80 ILGLAKDVEITIETRPdtltEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAG--PIKVSTDL 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 161484622   221 MRGL---NEDELLDFVALTEGLPLD-VRFIEYMPFDG----NKWNFKKMVSYKEMLDTI 271
Cdd:smart00729 158 IVGLpgeTEEDFEETLKLLKELGPDrVSIFPLSPRPGtplaKMYKRLKPPTKEERAELL 216
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
42-283 1.85e-08

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: 55.74  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  42 GLSLRLQFLQEHAAPFSAFL--TDSFGR---QHSYLRISLTEKCNLRCQYCMP-------EEGVPLTPKADLLTTEEILT 109
Cdd:NF033640  77 GRSLRQESNERWAKHIEDAIksTDEDGSddvNPRYLDLRFGNLCNLKCRMCGPhsssswaKEAKKLGGPKLGDKKKISWF 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 110 LARLFVKE------GVDKIRLTGGEPLIRPDVVDIVARL--HGLEGLRTIGLTTNG-------INLARLLPRLQQAGLNA 174
Cdd:NF033640 157 EDEEFWKWleellpSLKEIYFAGGEPLLIKEHYKLLEKLveKGRAKNIELRYNTNLtvlpdklKDLLDLWKKFKSVSISA 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 175 vniSLDTlVPAKFEFIvrRKGFH--KVMEGIHKAIELGYK-PVKVNCVV--MRGLNEDELLDFVaLTEG----------- 238
Cdd:NF033640 237 ---SIDG-VGERNEYI--RYGSKwdEIEKNLKKLKEECPNvELRINPTVsaLNVLHLPELLDWL-LELGlgpidiylnil 309
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 239 ----------LPLDVR----------------------------FIEYMPFDGNKWNFKKMVSYKEMLDTIR-QRWpgLE 279
Cdd:NF033640 310 rdpeylsiknLPKEIKqkvieklenflekndngfdkylikklkrLINYMNSEDNSELLKEFKKFTKKLDKIRgENF--LD 387

                 ....
gi 161484622 280 KLPE 283
Cdd:NF033640 388 VFPE 391
 
Name Accession Description Interval E-value
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
16-385 0e+00

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 602.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  16 SNARGCSSGAPVTQPRPGEP--SRPTREGLSLRLQFLQEHAAPFSAFLTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGV 93
Cdd:PLN02951   2 SKLADLRLGFRSSSFQLQEPgsSIFSASSSYAADQVDPEASNPVSDMLVDSFGRRHNYLRISLTERCNLRCQYCMPEEGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  94 PLTPKADLLTTEEILTLARLFVKEGVDKIRLTGGEPLIRPDVVDIVARLHGLEGLRTIGLTTNGINLARLLPRLQQAGLN 173
Cdd:PLN02951  82 ELTPKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDICLQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 174 AVNISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYKPVKVNCVVMRGLNEDELLDFVALTEGLPLDVRFIEYMPFDG 253
Cdd:PLN02951 162 SLNISLDTLVPAKFEFLTRRKGHDRVLESIDTAIELGYNPVKVNCVVMRGFNDDEICDFVELTRDKPINVRFIEFMPFDG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 254 NKWNFKKMVSYKEMLDTIRQRWPGLEKLPEEDSSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGN 333
Cdd:PLN02951 242 NVWNVKKLVPYAEMMDRIEQRFPSLKRLQDHPTDTAKNFRIDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGP 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 161484622 334 SEVSLRDHLRAGASEEELLRIIGAAVGRKKRQHAGMFNIAQMKNRPMILIGG 385
Cdd:PLN02951 322 SEVSLRDALRSGADDDELREIIGAAVKRKKAAHAGMFDLAKTANRPMIHIGG 373
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
61-385 3.37e-176

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: 493.04  E-value: 3.37e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  61 LTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKADLLTTEEILTLARLFVKEGVDKIRLTGGEPLIRPDVVDIVA 140
Cdd:COG2896    5 LIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPELIA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 141 RLHGLEGLRTIGLTTNGINLARLLPRLQQAGLNAVNISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYKPVKVNCVV 220
Cdd:COG2896   85 RLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVKINAVV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 221 MRGLNEDELLDFVALTEGLPLDVRFIEYMPF-DGNKWNFKKMVSYKEMLDTIRQRWPgLEKLPEEDSSTAKAFKIPGFQG 299
Cdd:COG2896  165 MRGVNDDEILDLLEFAKERGIDLRFIELMPLgEGGGWRRDQVVSAAEILERLEARFP-LEPLPARGGGPARYYRVPGGGG 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 300 QISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEEELLRIIGAAVGRKKRQHagMFNIAQMK--N 377
Cdd:COG2896  244 RIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGH--GFDEGDFPqpK 321

                 ....*...
gi 161484622 378 RPMILIGG 385
Cdd:COG2896  322 RSMSAIGG 329
moaA PRK00164
GTP 3',8-cyclase MoaA;
54-385 1.12e-150

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 428.79  E-value: 1.12e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  54 AAPFSAFLTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKADLLTTEEILTLARLFVKEGVDKIRLTGGEPLIRP 133
Cdd:PRK00164   1 PVPMTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPFLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 134 DVVDIVARLHGLEGLRTIGLTTNGINLARLLPRLQQAGLNAVNISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYKP 213
Cdd:PRK00164  81 DLEDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 214 VKVNCVVMRGLNEDELLDFVALTEGLPLDVRFIEYMPFD-GNKWNFKKMVSYKEMLDTIRQRWPGLEKLPeEDSSTAKAF 292
Cdd:PRK00164 161 VKVNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGeGNEWFRKHHLSGAEIRARLAERGWTLQPRA-RSGGPAQYF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 293 KIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEEELLRIIGAAVGRKKRQHAGMFNI 372
Cdd:PRK00164 240 RHPDYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSGADDEELAAAIREALQNKPEGHGLHDGN 319
                        330
                 ....*....|...
gi 161484622 373 AQMKnRPMILIGG 385
Cdd:PRK00164 320 TGPT-RHMSYIGG 331
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
61-385 1.40e-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: 408.15  E-value: 1.40e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622   61 LTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVP-LTPKADLLTTEEILTLARLFVKEGVDKIRLTGGEPLIRPDVVDIV 139
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGLdFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  140 ARLHGLEGLRTIGLTTNGINLARLLPRLQQAGLNAVNISLDTLVPAKFEFIVRRKG-FHKVMEGIHKAIELGYKPVKVNC 218
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGrLEQVLAGIDAALAAGLEPVKLNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  219 VVMRGLNEDELLDFVALTEGLPLDVRFIEYMPFD-GNKWNFKKMVSYKEMLDTIRQRWPGLEKLP-EEDSSTAKAFK--I 294
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGeGNGWREKKFVSADEILERLEQAFGPLEPVPsPRGNGPAPAYRwrL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  295 PGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEEELLRIIGAAVGRKKRQHAGMFNIA- 373
Cdd:TIGR02666 241 PGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRGGASDALLEAIIQAILQKKPEGHSFLRFTSp 320
                         330
                  ....*....|....
gi 161484622  374 --QMKNRPMILIGG 385
Cdd:TIGR02666 321 anKRRKRAMSQIGG 334
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
241-367 1.80e-60

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: 191.28  E-value: 1.80e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  241 LDVRFIEYMPFD-GNKWNFKKMVSYKEMLDTIRQRWPgLEKLPEEDSSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLR 319
Cdd:pfam06463   1 IDLRFIELMPVGeGNGWRRKKFVSLDEILERIEARFP-LLPARKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLR 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 161484622  320 ITADGNLKVCLFGNSEVSLRDHLRAGASEEELLRIIGAAVGRKKRQHA 367
Cdd:pfam06463  80 LTADGKLKTCLFAEDGIDLRDALRSGDDDEELREAIREALARKPPRHS 127
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
307-376 7.22e-37

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: 128.05  E-value: 7.22e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 307 MSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEEELLRIIGAAVGRKKRQHAGMFNIAQMK 376
Cdd:cd21117    1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGASDEELREAIRAAVQRKPERHSLERGDSGTR 70
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
71-219 2.77e-34

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


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 124.25  E-value: 2.77e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  71 YLRISLTEKCNLRCQYCMPEEGVPLTPKadlLTTEEILTLARLFVKEGVDKIRLTGGEPLIRPDVVDIVARLHGLeGLRT 150
Cdd:COG0535    1 RLQIELTNRCNLRCKHCYADAGPKRPGE---LSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAKEL-GIRV 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161484622 151 IgLTTNGINLAR-LLPRLQQAGLNAVNISLDTLVPAKFEFIVRRKG-FHKVMEGIHKAIELGYkPVKVNCV 219
Cdd:COG0535   77 N-LSTNGTLLTEeLAERLAEAGLDHVTISLDGVDPETHDKIRGVPGaFDKVLEAIKLLKEAGI-PVGINTV 145
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
76-232 1.10e-31

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: 117.63  E-value: 1.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622   76 LTEKCNLRCQYCMPEEGvPLTPKADLLTTEEILTLARLFVKEGVDKIRLTGGEPLIRPDVVDIVARLHGLEGL--RTIGL 153
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSI-RARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAegIRITL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  154 TTNGINLA-RLLPRLQQAGLNAVNISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYKPVKVNCVVMRGLNEDELLDF 232
Cdd:pfam04055  80 ETNGTLLDeELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETDEDLEET 159
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
74-272 2.31e-21

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: 90.86  E-value: 2.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  74 ISLTEKCNLRCQYCMPEEGVPLTPKADLLTTEEILtLARLFVKEGVDKIRLTGGEPLIRPDVVDIVARLHGLEGLRTIGL 153
Cdd:cd01335    1 LELTRGCNLNCGFCSNPASKGRGPESPPEIEEILD-IVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGFEISI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 154 TTNG-INLARLLPRLQQAGLNAVNISLDTLVPAKFEFIVRRKG-FHKVMEGIHKAIELGykpVKVNCVVMRGLNEDELLD 231
Cdd:cd01335   80 ETNGtLLTEELLKELKELGLDGVGVSLDSGDEEVADKIRGSGEsFKERLEALKELREAG---LGLSTTLLVGLGDEDEED 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 161484622 232 FVALTEGL-----PLDVRFIEYMP-FDGNKWNFKKMVSYKEMLDTIR 272
Cdd:cd01335  157 DLEELELLaefrsPDRVSLFRLLPeEGTPLELAAPVVPAEKLLRLIA 203
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
74-329 4.38e-14

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 72.71  E-value: 4.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  74 ISLTEKCNLRCQYCMpEEGVPLTPKADLltTEEILTLARLFVKE---GVDKIRLT--GGEPLIRPDVV-DIVARL--HGL 145
Cdd:COG0641    5 LKPTSRCNLRCSYCY-YSEGDEGSRRRM--SEETAEKAIDFLIEssgPGKELTITffGGEPLLNFDFIkEIVEYArkYAK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 146 EGLR-TIGLTTNGINL-ARLLPRLQQAGLNaVNISLDTLvpakfEFI-----VRRKG---FHKVMEGIHKAIELGyKPVK 215
Cdd:COG0641   82 KGKKiRFSIQTNGTLLdDEWIDFLKENGFS-VGISLDGP-----KEIhdrnrVTKNGkgsFDRVMRNIKLLKEHG-VEVN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 216 VNCVVMRGlNEDELLDFV-ALTE-GLPlDVRFIEYMPFDGNKWNFkKMVSYKEMLDTIRQRWpgLEKLPEEdsstakaFK 293
Cdd:COG0641  155 IRCTVTRE-NLDDPEELYdFLKElGFR-SIQFNPVVEEGEADYSL-TPEDYGEFLIELFDEW--LERDGGK-------IF 222
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 161484622 294 IPGFQGQISFITSMSEHFC-GTCNR-LRITADGNLKVC 329
Cdd:COG0641  223 VREFDILLAGLLPPCSSPCvGAGGNyLVVDPDGDIYPC 260
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
80-251 1.83e-12

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 66.36  E-value: 1.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  80 CNLRCQYCMPEEGVPLTPKADL--LTTEEILTLA--RLFVKEGVDKIRLTGGEPLIRPD-VVDIVARLHGLeGLRTiGLT 154
Cdd:COG1180   31 CNLRCPYCHNPEISQGRPDAAGreLSPEELVEEAlkDRGFLDSCGGVTFSGGEPTLQPEfLLDLAKLAKEL-GLHT-ALD 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 155 TNGIN----LARLLPrlqqaGLNAVNISLDTLVPAKFEFIVRRKGfHKVMEGIHKAIELGyKPVKVNCVVMRGLN--EDE 228
Cdd:COG1180  109 TNGYIpeeaLEELLP-----YLDAVNIDLKAFDDEFYRKLTGVSL-EPVLENLELLAESG-VHVEIRTLVIPGLNdsEEE 181
                        170       180
                 ....*....|....*....|...
gi 161484622 229 LLDFVALTEGLPlDVRFIEYMPF 251
Cdd:COG1180  182 LEAIARFIAELG-DVIPVHLLPF 203
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
76-239 4.55e-12

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: 66.79  E-value: 4.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622   76 LTEKCNLRCQYCMpeegvpLTPK----ADLLTTEEIlTLARLFVKE----GVDKIRLTGGEPLIRPDVVDIVARLhGLEG 147
Cdd:TIGR04251  10 LTEGCNLKCRHCW------IDPKyqgeGEQHPSLDP-SLFRSIIRQaiplGLTSVKLTGGEPLLHPAIGEILECI-GENN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  148 LRtIGLTTNGI----NLARllpRLQQAGLNAVNISLDTLVPAKFEFIVRRKG-FHKVMEGIHKAIELGYKPVKVNCVVMR 222
Cdd:TIGR04251  82 LQ-LSVETNGLlctpQTAR---DLASCETPFVSVSLDGVDAATHDWMRGVKGaFDKAVRGIHNLVEAGIHPQIIMTVTRR 157
                         170
                  ....*....|....*..
gi 161484622  223 glNEDELLDFVALTEGL 239
Cdd:TIGR04251 158 --NVGQMEQIVRLAESL 172
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
70-271 1.49e-11

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: 63.19  E-value: 1.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622    70 SYLRISLTEKCNLRCQYCM--PEEGVPLTPKADLLtTEEILTLARLFVKEG-VDKIRLTGGEPLIRP--DVVDIVARLHG 144
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSfpSLRGKLRSRYLEAL-VREIELLAEKGEKEGlVGTVFIGGGTPTLLSpeQLEELLEAIRE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622   145 LEGLRTIGLTTNGINL----ARLLPRLQQAGLNAVNISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGykPVKVNCVV 220
Cdd:smart00729  80 ILGLAKDVEITIETRPdtltEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAG--PIKVSTDL 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 161484622   221 MRGL---NEDELLDFVALTEGLPLD-VRFIEYMPFDG----NKWNFKKMVSYKEMLDTI 271
Cdd:smart00729 158 IVGLpgeTEEDFEETLKLLKELGPDrVSIFPLSPRPGtplaKMYKRLKPPTKEERAELL 216
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
80-229 2.61e-10

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


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 61.08  E-value: 2.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  80 CNLRCQYCMPEEGvPL--TPKAD-------LLttEEILTLARlFVKEGVDKIRLTGGEPLIRPDVVDIVARLHGLEGLRT 150
Cdd:COG2100   46 CNLNCIFCSVDAG-PHsrTRQAEyivdpeyLV--EWFEKVAR-FKGKGVEAHIDGVGEPLLYPYIVELVKGLKEIKGVKV 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 151 IGLTTNGINLA-RLLPRLQQAGLNAVNISLDTLVPAKFEFIVRRKGF--HKVMEGIHKAIELGYKPVKVNCVVMRGLNED 227
Cdd:COG2100  122 VSMQTNGTLLSeKLIDELEEAGLDRINLSIDTLDPEKAKKLAGTKWYdvEKVLELAEYIARETKIDLLIAPVWLPGINDE 201

                 ..
gi 161484622 228 EL 229
Cdd:COG2100  202 DI 203
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
42-283 1.85e-08

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: 55.74  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  42 GLSLRLQFLQEHAAPFSAFL--TDSFGR---QHSYLRISLTEKCNLRCQYCMP-------EEGVPLTPKADLLTTEEILT 109
Cdd:NF033640  77 GRSLRQESNERWAKHIEDAIksTDEDGSddvNPRYLDLRFGNLCNLKCRMCGPhsssswaKEAKKLGGPKLGDKKKISWF 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 110 LARLFVKE------GVDKIRLTGGEPLIRPDVVDIVARL--HGLEGLRTIGLTTNG-------INLARLLPRLQQAGLNA 174
Cdd:NF033640 157 EDEEFWKWleellpSLKEIYFAGGEPLLIKEHYKLLEKLveKGRAKNIELRYNTNLtvlpdklKDLLDLWKKFKSVSISA 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 175 vniSLDTlVPAKFEFIvrRKGFH--KVMEGIHKAIELGYK-PVKVNCVV--MRGLNEDELLDFVaLTEG----------- 238
Cdd:NF033640 237 ---SIDG-VGERNEYI--RYGSKwdEIEKNLKKLKEECPNvELRINPTVsaLNVLHLPELLDWL-LELGlgpidiylnil 309
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 239 ----------LPLDVR----------------------------FIEYMPFDGNKWNFKKMVSYKEMLDTIR-QRWpgLE 279
Cdd:NF033640 310 rdpeylsiknLPKEIKqkvieklenflekndngfdkylikklkrLINYMNSEDNSELLKEFKKFTKKLDKIRgENF--LD 387

                 ....
gi 161484622 280 KLPE 283
Cdd:NF033640 388 VFPE 391
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
80-157 7.94e-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: 52.06  E-value: 7.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  80 CNLRCQYC------MPEEGVPLTPkadllttEEILTLARlfvKEGVDKIRLTGGEPLIRPDVVDIVARLHGlEGLRtIGL 153
Cdd:COG0602   30 CNLRCSWCdtkyawDGEGGKRMSA-------EEILEEVA---ALGARHVVITGGEPLLQDDLAELLEALKD-AGYE-VAL 97

                 ....
gi 161484622 154 TTNG 157
Cdd:COG0602   98 ETNG 101
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
74-240 2.95e-06

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: 48.70  E-value: 2.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622   74 ISLTEKCNLRCQYCMPEEGVPLTPKAdlLTTEEILTLARLFVKEGVDKIRLTGGEPLIRPDVVDIvarLHGLEGLRT-IG 152
Cdd:TIGR04250   7 IDITGRCNLRCRYCSHFSSAAETPTD--LETAEWLRFFRELNRCSVLRVVLSGGEPFMRSDFREI---IDGIVKNRMrFS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  153 LTTNGI----NLARLLPRLQQAglNAVNISLDTLVPAKFEfIVRRKG-FHKVMEGIhKAIELGYKPVKVNCVVMRGlNED 227
Cdd:TIGR04250  82 ILSNGTlitdAIASFLAATRRC--DYVQVSIDGSTPGTHD-RLRGTGsFLQAVEGI-ELLRKHAIPVVVRVTIHRW-NVD 156
                         170
                  ....*....|....*.
gi 161484622  228 ELLDFVAL---TEGLP 240
Cdd:TIGR04250 157 DLRPIAALlldDLGLP 172
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
80-228 1.15e-05

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


Pssm-ID: 444038  Cd Length: 261  Bit Score: 46.52  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  80 CNLRCQYC--------MPEEGVPLTPKAdllTTEEILTLARlfvKEGVDKIRLTGGEPLIRPD-VVDIvarlhgLEGLRT 150
Cdd:COG5014   50 CNLRCGFCwswrfrdfPLTIGKFYSPEE---VAERLIEIAR---ERGYRQVRLSGGEPTIGFEhLLKV------LELFSE 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 151 IGLT----TNGI------NLARLLPRLQQAglnAVNISLDTLVPAKFEFI--VRRKGFHKVMEGIHKAIELGYKPVK-VN 217
Cdd:COG5014  118 RGLTfileTNGIligydrELARELASFRNI---VVRVSIKGCTPEEFSMLtgADPEFFELQLRALKNLVDAGLEPGReVY 194
                        170
                 ....*....|.
gi 161484622 218 CVVMRGLNEDE 228
Cdd:COG5014  195 PAVMLSFSTEE 205
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
80-247 1.91e-05

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: 45.57  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  80 CNLRCQYC-------MPEEGVPLTPKADLLttEEILTLARLFVKEG--VDKIRLTG-GEPLIRPDVVDIVARLHGLEGLr 149
Cdd:COG0731   34 CNFDCVYCqrgrttdLTRERREFDDPEEIL--EELIEFLRKLPEEArePDHITFSGsGEPTLYPNLGELIEEIKKLRGI- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 150 TIGLTTNGINLARllPRLQQA--GLNAVNISLDTLVPAKFEFIVR---RKGFHKVMEGIHKAIELGYKPVKVNCVVMRGL 224
Cdd:COG0731  111 KTALLTNGSLLHR--PEVREEllKADQVYPSLDAADEETFRKINRphpGLSWERIIEGLELFRKLYKGRTVIETMLVKGI 188
                        170       180
                 ....*....|....*....|....*
gi 161484622 225 N--EDELLDFVALTEGlpLDVRFIE 247
Cdd:COG0731  189 NdsEEELEAYAELIKR--INPDFVE 211
PFLA TIGR02493
pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain ...
80-256 3.89e-05

pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain (pfam04055). A single glycine residue in EC 2.3.1.54, formate C-acetyltransferase (formate-pyruvate lyase), is oxidized to the corresponding radical by transfer of H from its CH2 to AdoMet with concomitant cleavage of the latter. The reaction requires Fe2+. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5-yl radical, which then abstracts a hydrogen radical from the glycine residue. [Energy metabolism, Anaerobic, Protein fate, Protein modification and repair]


Pssm-ID: 131546 [Multi-domain]  Cd Length: 235  Bit Score: 44.67  E-value: 3.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622   80 CNLRCQYCM------PEEGVPLTPkADLLttEEILTLARLFVKEGvDKIRLTGGEPLIRPDVVDIVARLHGLEGLRTIgL 153
Cdd:TIGR02493  25 CPLRCQYCHnpdtwdLKGGTEVTP-EELI--KEVGSYKDFFKASG-GGVTFSGGEPLLQPEFLSELFKACKELGIHTC-L 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  154 TTNG-----INLARLLprLQQAGLNAVNI-SLDtlvPAKFEFIVRRKGfHKVMEGIHKAIELGyKPVKVNCVVMRGL--N 225
Cdd:TIGR02493 100 DTSGflggcTEAADEL--LEYTDLVLLDIkHFN---PEKYKKLTGVSL-QPTLDFAKYLAKRN-KPIWIRYVLVPGYtdS 172
                         170       180       190
                  ....*....|....*....|....*....|....
gi 161484622  226 EDELLDFVALTEGLPlDVRFIEYMPFDG---NKW 256
Cdd:TIGR02493 173 EEDIEALAEFVKTLP-NVERVEVLPYHQlgvYKW 205
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
80-189 7.45e-05

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: 42.16  E-value: 7.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622   80 CNLRCQYCMPEEGVPLTPkADLLTTEEILTLARLFVKEGVDKIRLTGGEPLI-RPDVVDIVARLHGLEGLRTIGLTTnGI 158
Cdd:pfam13353  15 CNHHCKGCFNPETWDFKY-GKPFTEELEDEIIEDLAKPYIQGLTLSGGEPLLnAEALLELVKRVREECPEKDIWLWT-GY 92
                          90       100       110
                  ....*....|....*....|....*....|.
gi 161484622  159 NLARLLPRLQQAGLNavniSLDTLVPAKFEF 189
Cdd:pfam13353  93 TFEELQSKDQLELLK----LIDVLVDGKFEQ 119
PRK13745 PRK13745
anaerobic sulfatase-maturation protein;
80-250 3.57e-04

anaerobic sulfatase-maturation protein;


Pssm-ID: 237489 [Multi-domain]  Cd Length: 412  Bit Score: 42.54  E-value: 3.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  80 CNLRCQYCMPEEGVPLTPK-ADLLTTEEILtlaRLFVKEGVD-----KIRLT--GGEPLIRPdvvdIVARLHGLE----- 146
Cdd:PRK13745  24 CNLACDYCYYLEKSKLYQEnPKHVMSDELL---EKFIKEYINsqtmpQVLFTwhGGETLMRP----LSFYKKALElqkky 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622 147 -GLRTIG--LTTNGINLARLLPRLQQAGLNAVNISLDTlvPAKFEFIVRRK-----GFHKVMEGIHKAIELGykpVKVNC 218
Cdd:PRK13745  97 aRGRQIDncIQTNGTLLTDEWCEFFRENNFLVGVSIDG--PQEFHDEYRKNkmgkpSFVKVMKGINLLKKHG---VEWNA 171
                        170       180       190
                 ....*....|....*....|....*....|...
gi 161484622 219 V-VMRGLNEDELLDFVALTEglPLDVRFIEYMP 250
Cdd:PRK13745 172 MaVVNDFNADYPLDFYHFFK--ELDCHYIQFAP 202
COG2108 COG2108
Uncharacterized radical SAM domain-containing protein [Function unknown];
76-173 7.98e-03

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


Pssm-ID: 441711 [Multi-domain]  Cd Length: 361  Bit Score: 38.02  E-value: 7.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484622  76 LTEKCNLRCQYC-MPEE----GVPLTPKADLLTTEEILTLARLFVKEGVDkirLTGGEPLIRPDVVdivarLHGLEGLRT 150
Cdd:COG2108   33 ITGLCNRNCFYCpLSEErkgkDVIYANERPVESDEDVIEEARRMGALGAG---ITGGEPLLVLDRT-----LEYIRLLKE 104
                         90       100       110
                 ....*....|....*....|....*....|.
gi 161484622 151 -------IGLTTNGINLAR-LLPRLQQAGLN 173
Cdd:COG2108  105 efgpdhhIHLYTNGILADEdVLRKLADAGLD 135
 
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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