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Conserved domains on  [gi|22027536|ref|NP_005934|]
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molybdenum cofactor biosynthesis protein 1 isoform 1 [Homo sapiens]

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
35-385 0e+00

Molybderin biosynthesis protein CNX2


:

Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 594.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   35 LPGLSSQEVSRRRQFLREHAAPFSAFLTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILTLARLF 114
Cdd:PLN02951  23 SSIFSASSSYAADQVDPEASNPVSDMLVDSFGRRHNYLRISLTERCNLRCQYCMPEEGVELTPKSHLLSQDEIVRLAGLF 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  115 VKEGIDKIRLTGGEPLIRPDVVDIVAQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRK 194
Cdd:PLN02951 103 VAAGVDKIRLTGGEPTLRKDIEDICLQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTRRK 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  195 GFHKVMEGIHKAIELGYNPVKVNCVVMRGLNEDELLDFAALTEGLPLDVRFIEYMPFDGNKWNFKKMVSYKEMLDTVRQQ 274
Cdd:PLN02951 183 GHDRVLESIDTAIELGYNPVKVNCVVMRGFNDDEICDFVELTRDKPINVRFIEFMPFDGNVWNVKKLVPYAEMMDRIEQR 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  275 WPELEKVPEEESSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRI 354
Cdd:PLN02951 263 FPSLKRLQDHPTDTAKNFRIDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSLRDALRSGADDDELREI 342
                        330       340       350
                 ....*....|....*....|....*....|.
gi 22027536  355 IGAAVGRKKRQHAGMFSISQMKNRPMILIGG 385
Cdd:PLN02951 343 IGAAVKRKKAAHAGMFDLAKTANRPMIHIGG 373
 
Name Accession Description Interval E-value
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
35-385 0e+00

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 594.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   35 LPGLSSQEVSRRRQFLREHAAPFSAFLTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILTLARLF 114
Cdd:PLN02951  23 SSIFSASSSYAADQVDPEASNPVSDMLVDSFGRRHNYLRISLTERCNLRCQYCMPEEGVELTPKSHLLSQDEIVRLAGLF 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  115 VKEGIDKIRLTGGEPLIRPDVVDIVAQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRK 194
Cdd:PLN02951 103 VAAGVDKIRLTGGEPTLRKDIEDICLQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTRRK 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  195 GFHKVMEGIHKAIELGYNPVKVNCVVMRGLNEDELLDFAALTEGLPLDVRFIEYMPFDGNKWNFKKMVSYKEMLDTVRQQ 274
Cdd:PLN02951 183 GHDRVLESIDTAIELGYNPVKVNCVVMRGFNDDEICDFVELTRDKPINVRFIEFMPFDGNVWNVKKLVPYAEMMDRIEQR 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  275 WPELEKVPEEESSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRI 354
Cdd:PLN02951 263 FPSLKRLQDHPTDTAKNFRIDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSLRDALRSGADDDELREI 342
                        330       340       350
                 ....*....|....*....|....*....|.
gi 22027536  355 IGAAVGRKKRQHAGMFSISQMKNRPMILIGG 385
Cdd:PLN02951 343 IGAAVKRKKAAHAGMFDLAKTANRPMIHIGG 373
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
61-385 1.80e-173

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: 486.49  E-value: 1.80e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  61 LTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIVA 140
Cdd:COG2896   5 LIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPELIA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536 141 QLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNPVKVNCVV 220
Cdd:COG2896  85 RLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVKINAVV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536 221 MRGLNEDELLDFAALTEGLPLDVRFIEYMPF-DGNKWNFKKMVSYKEMLDTVRQQWPeLEKVPEEESSTAKAFKIPGFQG 299
Cdd:COG2896 165 MRGVNDDEILDLLEFAKERGIDLRFIELMPLgEGGGWRRDQVVSAAEILERLEARFP-LEPLPARGGGPARYYRVPGGGG 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536 300 QISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHAGMFSISQMKNRP 379
Cdd:COG2896 244 RIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGHGFDEGDFPQPKRS 323

                ....*.
gi 22027536 380 MILIGG 385
Cdd:COG2896 324 MSAIGG 329
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
61-385 2.99e-144

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: 412.39  E-value: 2.99e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536    61 LTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVP-LTPKANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIV 139
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGLdFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   140 AQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKG-FHKVMEGIHKAIELGYNPVKVNC 218
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGrLEQVLAGIDAALAAGLEPVKLNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   219 VVMRGLNEDELLDFAALTEGLPLDVRFIEYMPFD-GNKWNFKKMVSYKEMLDTVRQQWPELEKVP---EEESSTAKAFKI 294
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGeGNGWREKKFVSADEILERLEQAFGPLEPVPsprGNGPAPAYRWRL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   295 PGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHAGMFSIS- 373
Cdd:TIGR02666 241 PGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRGGASDALLEAIIQAILQKKPEGHSFLRFTSp 320
                         330
                  ....*....|....
gi 22027536   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 3.59e-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: 190.51  E-value: 3.59e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   241 LDVRFIEYMPFD-GNKWNFKKMVSYKEMLDTVRQQWPELEkVPEEESSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLR 319
Cdd:pfam06463   1 IDLRFIELMPVGeGNGWRRKKFVSLDEILERIEARFPLLP-ARKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLR 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 22027536   320 ITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHA 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 2.67e-36

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: 126.50  E-value: 2.67e-36
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536 307 MSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHAGMFSISQMK 376
Cdd:cd21117   1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGASDEELREAIRAAVQRKPERHSLERGDSGTR 70
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
70-271 2.15e-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: 62.80  E-value: 2.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536     70 SYLRISLTEKCNLRCQYCM--PEEGVPLTPKANLLtTEEILTLARLFVKEG-IDKIRLTGGEPLIRP--DVVDIVAQLQR 144
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSfpSLRGKLRSRYLEAL-VREIELLAEKGEKEGlVGTVFIGGGTPTLLSpeQLEELLEAIRE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536    145 LEGLRTIGVTTNGINL----ARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGynPVKVNCVV 220
Cdd:smart00729  80 ILGLAKDVEITIETRPdtltEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAG--PIKVSTDL 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 22027536    221 MRGL---NEDELLDFAALTEGLPLD-VRFIEYMPFDG----NKWNFKKMVSYKEMLDTV 271
Cdd:smart00729 158 IVGLpgeTEEDFEETLKLLKELGPDrVSIFPLSPRPGtplaKMYKRLKPPTKEERAELL 216
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
71-281 2.05e-10

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: 61.90  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   71 YLRISLTEKCNLRCQYCMP-------EEGVPLTPKANLLTTEEILTLARLFVKE------GIDKIRLTGGEPLIRPDVVD 137
Cdd:NF033640 111 YLDLRFGNLCNLKCRMCGPhsssswaKEAKKLGGPKLGDKKKISWFEDEEFWKWleellpSLKEIYFAGGEPLLIKEHYK 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  138 IvaqLQRL--EGLR---TIGVTTNG-------INLARLLPQLQKAglsAINISLDTlVPAKFEFIvrRKGFH--KVMEGI 203
Cdd:NF033640 191 L---LEKLveKGRAkniELRYNTNLtvlpdklKDLLDLWKKFKSV---SISASIDG-VGERNEYI--RYGSKwdEIEKNL 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  204 HKAIELGYN-PVKVNCVV--MRGLNEDELLDFaALTEG---------------------LPLDVR--------------- 244
Cdd:NF033640 262 KKLKEECPNvELRINPTVsaLNVLHLPELLDW-LLELGlgpidiylnilrdpeylsiknLPKEIKqkvieklenfleknd 340
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 22027536  245 -------------FIEYMPFDGNKWNFKKMVSYKEMLDTVRQQ-----WPELEKV 281
Cdd:NF033640 341 ngfdkylikklkrLINYMNSEDNSELLKEFKKFTKKLDKIRGEnfldvFPELKEL 395
 
Name Accession Description Interval E-value
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
35-385 0e+00

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 594.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   35 LPGLSSQEVSRRRQFLREHAAPFSAFLTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILTLARLF 114
Cdd:PLN02951  23 SSIFSASSSYAADQVDPEASNPVSDMLVDSFGRRHNYLRISLTERCNLRCQYCMPEEGVELTPKSHLLSQDEIVRLAGLF 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  115 VKEGIDKIRLTGGEPLIRPDVVDIVAQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRK 194
Cdd:PLN02951 103 VAAGVDKIRLTGGEPTLRKDIEDICLQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTRRK 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  195 GFHKVMEGIHKAIELGYNPVKVNCVVMRGLNEDELLDFAALTEGLPLDVRFIEYMPFDGNKWNFKKMVSYKEMLDTVRQQ 274
Cdd:PLN02951 183 GHDRVLESIDTAIELGYNPVKVNCVVMRGFNDDEICDFVELTRDKPINVRFIEFMPFDGNVWNVKKLVPYAEMMDRIEQR 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  275 WPELEKVPEEESSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRI 354
Cdd:PLN02951 263 FPSLKRLQDHPTDTAKNFRIDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSLRDALRSGADDDELREI 342
                        330       340       350
                 ....*....|....*....|....*....|.
gi 22027536  355 IGAAVGRKKRQHAGMFSISQMKNRPMILIGG 385
Cdd:PLN02951 343 IGAAVKRKKAAHAGMFDLAKTANRPMIHIGG 373
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
61-385 1.80e-173

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: 486.49  E-value: 1.80e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  61 LTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIVA 140
Cdd:COG2896   5 LIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPELIA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536 141 QLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNPVKVNCVV 220
Cdd:COG2896  85 RLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVKINAVV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536 221 MRGLNEDELLDFAALTEGLPLDVRFIEYMPF-DGNKWNFKKMVSYKEMLDTVRQQWPeLEKVPEEESSTAKAFKIPGFQG 299
Cdd:COG2896 165 MRGVNDDEILDLLEFAKERGIDLRFIELMPLgEGGGWRRDQVVSAAEILERLEARFP-LEPLPARGGGPARYYRVPGGGG 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536 300 QISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHAGMFSISQMKNRP 379
Cdd:COG2896 244 RIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGHGFDEGDFPQPKRS 323

                ....*.
gi 22027536 380 MILIGG 385
Cdd:COG2896 324 MSAIGG 329
moaA PRK00164
GTP 3',8-cyclase MoaA;
54-385 1.51e-149

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 425.71  E-value: 1.51e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   54 AAPFSAFLTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRP 133
Cdd:PRK00164   1 PVPMTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPFLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  134 DVVDIVAQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNP 213
Cdd:PRK00164  81 DLEDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  214 VKVNCVVMRGLNEDELLDFAALTEGLPLDVRFIEYMPFD-GNKWNFKKMVSYKEMLDTVRQQWPELeKVPEEESSTAKAF 292
Cdd:PRK00164 161 VKVNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGeGNEWFRKHHLSGAEIRARLAERGWTL-QPRARSGGPAQYF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  293 KIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHAGMFSI 372
Cdd:PRK00164 240 RHPDYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSGADDEELAAAIREALQNKPEGHGLHDGN 319
                        330
                 ....*....|...
gi 22027536  373 SQMKnRPMILIGG 385
Cdd:PRK00164 320 TGPT-RHMSYIGG 331
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
61-385 2.99e-144

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: 412.39  E-value: 2.99e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536    61 LTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVP-LTPKANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIV 139
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGLdFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   140 AQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKG-FHKVMEGIHKAIELGYNPVKVNC 218
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGrLEQVLAGIDAALAAGLEPVKLNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   219 VVMRGLNEDELLDFAALTEGLPLDVRFIEYMPFD-GNKWNFKKMVSYKEMLDTVRQQWPELEKVP---EEESSTAKAFKI 294
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGeGNGWREKKFVSADEILERLEQAFGPLEPVPsprGNGPAPAYRWRL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   295 PGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHAGMFSIS- 373
Cdd:TIGR02666 241 PGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRGGASDALLEAIIQAILQKKPEGHSFLRFTSp 320
                         330
                  ....*....|....
gi 22027536   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 3.59e-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: 190.51  E-value: 3.59e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   241 LDVRFIEYMPFD-GNKWNFKKMVSYKEMLDTVRQQWPELEkVPEEESSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLR 319
Cdd:pfam06463   1 IDLRFIELMPVGeGNGWRRKKFVSLDEILERIEARFPLLP-ARKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLR 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 22027536   320 ITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHA 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 2.67e-36

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: 126.50  E-value: 2.67e-36
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536 307 MSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHAGMFSISQMK 376
Cdd:cd21117   1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGASDEELREAIRAAVQRKPERHSLERGDSGTR 70
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
71-219 1.16e-33

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: 122.70  E-value: 1.16e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  71 YLRISLTEKCNLRCQYCMPEEGVPLTPKanlLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIVAQLQRLeGLRT 150
Cdd:COG0535   1 RLQIELTNRCNLRCKHCYADAGPKRPGE---LSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAKEL-GIRV 76
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22027536 151 IgVTTNGINLAR-LLPQLQKAGLSAINISLDTLVPAKFEFIVRRKG-FHKVMEGIHKAIELGYnPVKVNCV 219
Cdd:COG0535  77 N-LSTNGTLLTEeLAERLAEAGLDHVTISLDGVDPETHDKIRGVPGaFDKVLEAIKLLKEAGI-PVGINTV 145
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
76-232 5.35e-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: 115.70  E-value: 5.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536    76 LTEKCNLRCQYCMPEEGvPLTPKANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIVAQLQRLEGL--RTIGV 153
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSI-RARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAegIRITL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   154 TTNGINLA-RLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNPVKVNCVVMRGLNEDELLDF 232
Cdd:pfam04055  80 ETNGTLLDeELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETDEDLEET 159
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
74-271 1.12e-22

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


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 94.71  E-value: 1.12e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  74 ISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILtLARLFVKEGIDKIRLTGGEPLIRPDVVDIVAQLQRLEGLRTIGV 153
Cdd:cd01335   1 LELTRGCNLNCGFCSNPASKGRGPESPPEIEEILD-IVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGFEISI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536 154 TTNG-INLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKG-FHKVMEGIHKAIELGynpVKVNCVVMRGLNEDELLD 231
Cdd:cd01335  80 ETNGtLLTEELLKELKELGLDGVGVSLDSGDEEVADKIRGSGEsFKERLEALKELREAG---LGLSTTLLVGLGDEDEED 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 22027536 232 FAALTEGL-----PLDVRFIEYMPFDGNKWNFKKMVSYKEMLDTV 271
Cdd:cd01335 157 DLEELELLaefrsPDRVSLFRLLPEEGTPLELAAPVVPAEKLLRL 201
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
74-329 7.52e-15

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 75.02  E-value: 7.52e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  74 ISLTEKCNLRCQYCMpEEGVPLTPKANLltTEEILTLARLFVKE---GIDKIRLT--GGEPLIRPDVV-DIVAQLQRLEG 147
Cdd:COG0641   5 LKPTSRCNLRCSYCY-YSEGDEGSRRRM--SEETAEKAIDFLIEssgPGKELTITffGGEPLLNFDFIkEIVEYARKYAK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536 148 LR---TIGVTTNGINL-ARLLPQLQKAGLSaINISLDTLvpakfEFI-----VRRKG---FHKVMEGIHKAIELGYnPVK 215
Cdd:COG0641  82 KGkkiRFSIQTNGTLLdDEWIDFLKENGFS-VGISLDGP-----KEIhdrnrVTKNGkgsFDRVMRNIKLLKEHGV-EVN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536 216 VNCVVMRGLNED--ELLDFAAlTEGLPlDVRFIEYMPFDGNKWNFkKMVSYKEMLDTVRQQWPELEKVPeeesstakaFK 293
Cdd:COG0641 155 IRCTVTRENLDDpeELYDFLK-ELGFR-SIQFNPVVEEGEADYSL-TPEDYGEFLIELFDEWLERDGGK---------IF 222
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 22027536 294 IPGFQGQISFITSMSEHFC-GTCNR-LRITADGNLKVC 329
Cdd:COG0641 223 VREFDILLAGLLPPCSSPCvGAGGNyLVVDPDGDIYPC 260
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
70-271 2.15e-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: 62.80  E-value: 2.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536     70 SYLRISLTEKCNLRCQYCM--PEEGVPLTPKANLLtTEEILTLARLFVKEG-IDKIRLTGGEPLIRP--DVVDIVAQLQR 144
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSfpSLRGKLRSRYLEAL-VREIELLAEKGEKEGlVGTVFIGGGTPTLLSpeQLEELLEAIRE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536    145 LEGLRTIGVTTNGINL----ARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGynPVKVNCVV 220
Cdd:smart00729  80 ILGLAKDVEITIETRPdtltEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAG--PIKVSTDL 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 22027536    221 MRGL---NEDELLDFAALTEGLPLD-VRFIEYMPFDG----NKWNFKKMVSYKEMLDTV 271
Cdd:smart00729 158 IVGLpgeTEEDFEETLKLLKELGPDrVSIFPLSPRPGtplaKMYKRLKPPTKEERAELL 216
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
76-239 2.84e-11

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: 64.09  E-value: 2.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536    76 LTEKCNLRCQYCMpeegvpLTPK---ANLLTTEEILTLARLFVKE----GIDKIRLTGGEPLIRPDVVDIVaQLQRLEGL 148
Cdd:TIGR04251  10 LTEGCNLKCRHCW------IDPKyqgEGEQHPSLDPSLFRSIIRQaiplGLTSVKLTGGEPLLHPAIGEIL-ECIGENNL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   149 RtIGVTTNGINLArllPQLQK--AGLSA--INISLDTLVPAKFEFIVRRKG-FHKVMEGIHKAIELGYNPVKVNCVVMRg 223
Cdd:TIGR04251  83 Q-LSVETNGLLCT---PQTARdlASCETpfVSVSLDGVDAATHDWMRGVKGaFDKAVRGIHNLVEAGIHPQIIMTVTRR- 157
                         170
                  ....*....|....*.
gi 22027536   224 lNEDELLDFAALTEGL 239
Cdd:TIGR04251 158 -NVGQMEQIVRLAESL 172
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
80-251 3.17e-11

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 62.89  E-value: 3.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  80 CNLRCQYCMPEEGVPLTPKANL--LTTEEILTLA--RLFVKEGIDKIRLTGGEPLIRPD-VVDIVAQLQRLeGLRTIGVt 154
Cdd:COG1180  31 CNLRCPYCHNPEISQGRPDAAGreLSPEELVEEAlkDRGFLDSCGGVTFSGGEPTLQPEfLLDLAKLAKEL-GLHTALD- 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536 155 TNGIN----LARLLPqlqkaGLSAINISLDTLVPAKFEFIVRRKGfHKVMEGIHKAIELGYnPVKVNCVVMRGLN--EDE 228
Cdd:COG1180 109 TNGYIpeeaLEELLP-----YLDAVNIDLKAFDDEFYRKLTGVSL-EPVLENLELLAESGV-HVEIRTLVIPGLNdsEEE 181
                       170       180
                ....*....|....*....|...
gi 22027536 229 LLDFAALTEGLPlDVRFIEYMPF 251
Cdd:COG1180 182 LEAIARFIAELG-DVIPVHLLPF 203
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
71-281 2.05e-10

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: 61.90  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   71 YLRISLTEKCNLRCQYCMP-------EEGVPLTPKANLLTTEEILTLARLFVKE------GIDKIRLTGGEPLIRPDVVD 137
Cdd:NF033640 111 YLDLRFGNLCNLKCRMCGPhsssswaKEAKKLGGPKLGDKKKISWFEDEEFWKWleellpSLKEIYFAGGEPLLIKEHYK 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  138 IvaqLQRL--EGLR---TIGVTTNG-------INLARLLPQLQKAglsAINISLDTlVPAKFEFIvrRKGFH--KVMEGI 203
Cdd:NF033640 191 L---LEKLveKGRAkniELRYNTNLtvlpdklKDLLDLWKKFKSV---SISASIDG-VGERNEYI--RYGSKwdEIEKNL 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  204 HKAIELGYN-PVKVNCVV--MRGLNEDELLDFaALTEG---------------------LPLDVR--------------- 244
Cdd:NF033640 262 KKLKEECPNvELRINPTVsaLNVLHLPELLDW-LLELGlgpidiylnilrdpeylsiknLPKEIKqkvieklenfleknd 340
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 22027536  245 -------------FIEYMPFDGNKWNFKKMVSYKEMLDTVRQQ-----WPELEKV 281
Cdd:NF033640 341 ngfdkylikklkrLINYMNSEDNSELLKEFKKFTKKLDKIRGEnfldvFPELKEL 395
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
80-233 5.63e-10

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


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 60.31  E-value: 5.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  80 CNLRCQYCMPEEGvpltPKANLLTTEEILTLARLFvkEGIDKI-RLTG----------GEPLIRPDVVDIVAQLQRLEGL 148
Cdd:COG2100  46 CNLNCIFCSVDAG----PHSRTRQAEYIVDPEYLV--EWFEKVaRFKGkgveahidgvGEPLLYPYIVELVKGLKEIKGV 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536 149 RTIGVTTNGINLA-RLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGF--HKVMEGIHKAI-ELGYNpVKVNCVVMRGL 224
Cdd:COG2100 120 KVVSMQTNGTLLSeKLIDELEEAGLDRINLSIDTLDPEKAKKLAGTKWYdvEKVLELAEYIArETKID-LLIAPVWLPGI 198
                       170
                ....*....|..
gi 22027536 225 NEDE---LLDFA 233
Cdd:COG2100 199 NDEDipkIIEWA 210
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
74-240 2.11e-07

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: 52.17  E-value: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536    74 ISLTEKCNLRCQYCMPEEGVPLTPkaNLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIVAQLQRlEGLRtIGV 153
Cdd:TIGR04250   7 IDITGRCNLRCRYCSHFSSAAETP--TDLETAEWLRFFRELNRCSVLRVVLSGGEPFMRSDFREIIDGIVK-NRMR-FSI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   154 TTNGInlarLLPQLQKAGLSA------INISLDTLVPAKFEfIVRRKG-FHKVMEGIhKAIELGYNPVKVNCVVMRGlNE 226
Cdd:TIGR04250  83 LSNGT----LITDAIASFLAAtrrcdyVQVSIDGSTPGTHD-RLRGTGsFLQAVEGI-ELLRKHAIPVVVRVTIHRW-NV 155
                         170
                  ....*....|....*..
gi 22027536   227 DELLDFAAL---TEGLP 240
Cdd:TIGR04250 156 DDLRPIAALlldDLGLP 172
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
80-157 4.81e-07

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: 49.75  E-value: 4.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  80 CNLRCQYC------MPEEGVPLTPkanllttEEILTLARlfvKEGIDKIRLTGGEPLIRPDVVDIVAQLQRlEGLRtIGV 153
Cdd:COG0602  30 CNLRCSWCdtkyawDGEGGKRMSA-------EEILEEVA---ALGARHVVITGGEPLLQDDLAELLEALKD-AGYE-VAL 97

                ....
gi 22027536 154 TTNG 157
Cdd:COG0602  98 ETNG 101
PFLA TIGR02493
pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain ...
80-256 1.86e-06

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: 48.52  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536    80 CNLRCQYCM------PEEGVPLTPKANLlttEEILTLARLFVKEGiDKIRLTGGEPLIRPDVVDIVAQLQRLEGLRTIgV 153
Cdd:TIGR02493  25 CPLRCQYCHnpdtwdLKGGTEVTPEELI---KEVGSYKDFFKASG-GGVTFSGGEPLLQPEFLSELFKACKELGIHTC-L 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   154 TTNGinLARLLPQLQKAGLSAINISL---DTLVPAKFEFIVRRKG-----FHKVMEGIHKAIELGYnpvkvncVVMRGL- 224
Cdd:TIGR02493 100 DTSG--FLGGCTEAADELLEYTDLVLldiKHFNPEKYKKLTGVSLqptldFAKYLAKRNKPIWIRY-------VLVPGYt 170
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 22027536   225 -NEDELLDFAALTEGLPlDVRFIEYMPFDG---NKW 256
Cdd:TIGR02493 171 dSEEDIEALAEFVKTLP-NVERVEVLPYHQlgvYKW 205
PRK13745 PRK13745
anaerobic sulfatase-maturation protein;
80-250 1.91e-06

anaerobic sulfatase-maturation protein;


Pssm-ID: 237489 [Multi-domain]  Cd Length: 412  Bit Score: 49.47  E-value: 1.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536   80 CNLRCQYCMPEEGVPLTPK-ANLLTTEEILtlaRLFVKEGID-----KIRLT--GGEPLIRPDVVDIVA-QLQR-LEGLR 149
Cdd:PRK13745  24 CNLACDYCYYLEKSKLYQEnPKHVMSDELL---EKFIKEYINsqtmpQVLFTwhGGETLMRPLSFYKKAlELQKkYARGR 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  150 TIG--VTTNGINLARLLPQLQKAGLSAINISLDTlvPAKFEFIVRRK-----GFHKVMEGIHKaieLGYNPVKVNCV-VM 221
Cdd:PRK13745 101 QIDncIQTNGTLLTDEWCEFFRENNFLVGVSIDG--PQEFHDEYRKNkmgkpSFVKVMKGINL---LKKHGVEWNAMaVV 175
                        170       180
                 ....*....|....*....|....*....
gi 22027536  222 RGLNEDELLDFAALTEglPLDVRFIEYMP 250
Cdd:PRK13745 176 NDFNADYPLDFYHFFK--ELDCHYIQFAP 202
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
80-247 1.05e-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: 46.34  E-value: 1.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  80 CNLRCQYC-MPEEGVPLTPKANLLTTEEILTLARLFVKEG------IDKIRLTG-GEPLIRPDVVDIVAQLQRLEGLrTI 151
Cdd:COG0731  34 CNFDCVYCqRGRTTDLTRERREFDDPEEILEELIEFLRKLpeearePDHITFSGsGEPTLYPNLGELIEEIKKLRGI-KT 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536 152 GVTTNGINLARllPQLQKAgLSAIN---ISLDTLVPAKFEFIVR---RKGFHKVMEGIHKAIELGYNPVKVNCVVMRGLN 225
Cdd:COG0731 113 ALLTNGSLLHR--PEVREE-LLKADqvyPSLDAADEETFRKINRphpGLSWERIIEGLELFRKLYKGRTVIETMLVKGIN 189
                       170       180
                ....*....|....*....|....
gi 22027536 226 --EDELLDFAALTEGlpLDVRFIE 247
Cdd:COG0731 190 dsEEELEAYAELIKR--INPDFVE 211
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
80-189 5.86e-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: 42.54  E-value: 5.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536    80 CNLRCQYCMPEEGvpLTPKANLLTTEEIL-TLARLFVKEGIDKIRLTGGEPLI-RPDVVDIVAQLQRLEGLRTIgVTTNG 157
Cdd:pfam13353  15 CNHHCKGCFNPET--WDFKYGKPFTEELEdEIIEDLAKPYIQGLTLSGGEPLLnAEALLELVKRVREECPEKDI-WLWTG 91
                          90       100       110
                  ....*....|....*....|....*....|..
gi 22027536   158 INLARLLPQLQKAGLSAInislDTLVPAKFEF 189
Cdd:pfam13353  92 YTFEELQSKDQLELLKLI----DVLVDGKFEQ 119
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
80-228 1.90e-04

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


Pssm-ID: 444038  Cd Length: 261  Bit Score: 42.67  E-value: 1.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536  80 CNLRCQYC--------MPEEGVPLTPKAnllTTEEILTLARlfvKEGIDKIRLTGGEPLIRPDVVdivaqLQRLEGLRTI 151
Cdd:COG5014  50 CNLRCGFCwswrfrdfPLTIGKFYSPEE---VAERLIEIAR---ERGYRQVRLSGGEPTIGFEHL-----LKVLELFSER 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22027536 152 GVT----TNGI------NLARLLPQLQKAglsAINISLDTLVPAKFEFI--VRRKGFHKVMEGIHKAIELGYNPVK-VNC 218
Cdd:COG5014 119 GLTfileTNGIligydrELARELASFRNI---VVRVSIKGCTPEEFSMLtgADPEFFELQLRALKNLVDAGLEPGReVYP 195
                       170
                ....*....|
gi 22027536 219 VVMRGLNEDE 228
Cdd:COG5014 196 AVMLSFSTEE 205
 
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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