NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1181163972|ref|WP_084511483|]
View 

SPASM domain-containing protein [Desulfatibacillum aliphaticivorans]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 39-172 5.90e-12

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: 63.00  E-value: 5.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181163972  39 ACPCNCSHCPVGSTPAENRTMrfgaraiDLGLFEKIAAETGCHDWASLRIhSVGEPVLWPGLPEALQIAHKNNARPWLFT 118
Cdd:COG0535     9 RCNLRCKHCYADAGPKRPGEL-------STEEAKRILDELAELGVKVVGL-TGGEPLLRPDLFELVEYAKELGIRVNLST 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1181163972 119 CGVTNRRDYLDAICDYA-SIVEVSVNSIDSGNYLETKGID-AFELVCENIGYIHKR 172
Cdd:COG0535    81 NGTLLTEELAERLAEAGlDHVTISLDGVDPETHDKIRGVPgAFDKVLEAIKLLKEA 136
SPASM cd21109
Iron-sulfur cluster-binding SPASM domain; This iron-sulfur cluster-binding domain is named ...
 237-314 1.92e-10

Iron-sulfur cluster-binding SPASM domain; This iron-sulfur cluster-binding domain is named SPASM after the biochemically characterized members, AlbA, PqqE, anSME, and MftC, which are involved in Subtilosin A, Pyrroloquinoline quinone, Anaerobic Sulfatase, and Mycofactocin maturation, respectively. SPASM occurs as an additional C-terminal domain in many peptide-modifying enzymes of the radical S-adenosylmethionine (SAM) superfamily. 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. Radical SAM enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster.


:

Pssm-ID: 410609 [Multi-domain]  Cd Length: 65  Bit Score: 55.89  E-value: 1.92e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1181163972 237 PCLVHWARFNIGITGDAVVCFNELFKEslhpgVVMGDVKKHSISEIWHNEKYRALRKAELLNDYSgfaqaealPCLNC 314
Cdd:cd21109     1 PCPAPWTSLYITPDGDVYPCCFDVNEE-----LKLGNIREQSLKEIWNSEKYREFRKLLLDGKIK--------LCKNC 65
 
Name Accession Description Interval E-value
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 39-172 5.90e-12

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: 63.00  E-value: 5.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181163972  39 ACPCNCSHCPVGSTPAENRTMrfgaraiDLGLFEKIAAETGCHDWASLRIhSVGEPVLWPGLPEALQIAHKNNARPWLFT 118
Cdd:COG0535     9 RCNLRCKHCYADAGPKRPGEL-------STEEAKRILDELAELGVKVVGL-TGGEPLLRPDLFELVEYAKELGIRVNLST 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1181163972 119 CGVTNRRDYLDAICDYA-SIVEVSVNSIDSGNYLETKGID-AFELVCENIGYIHKR 172
Cdd:COG0535    81 NGTLLTEELAERLAEAGlDHVTISLDGVDPETHDKIRGVPgAFDKVLEAIKLLKEA 136
SPASM cd21109
Iron-sulfur cluster-binding SPASM domain; This iron-sulfur cluster-binding domain is named ...
 237-314 1.92e-10

Iron-sulfur cluster-binding SPASM domain; This iron-sulfur cluster-binding domain is named SPASM after the biochemically characterized members, AlbA, PqqE, anSME, and MftC, which are involved in Subtilosin A, Pyrroloquinoline quinone, Anaerobic Sulfatase, and Mycofactocin maturation, respectively. SPASM occurs as an additional C-terminal domain in many peptide-modifying enzymes of the radical S-adenosylmethionine (SAM) superfamily. 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. Radical SAM enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster.


Pssm-ID: 410609 [Multi-domain]  Cd Length: 65  Bit Score: 55.89  E-value: 1.92e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1181163972 237 PCLVHWARFNIGITGDAVVCFNELFKEslhpgVVMGDVKKHSISEIWHNEKYRALRKAELLNDYSgfaqaealPCLNC 314
Cdd:cd21109     1 PCPAPWTSLYITPDGDVYPCCFDVNEE-----LKLGNIREQSLKEIWNSEKYREFRKLLLDGKIK--------LCKNC 65
SPASM pfam13186
Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur ...
 238-314 3.82e-09

Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur cluster binding domain in many radical SAM domain, pfam04055 proteins. The domain occurs in a number of proteins that modify a protein to become an active enzyme, or a peptide to become a ribosomal natural product. The domain is named SPASM because it occurs in the maturases of Subilitosin, PQQ, Anaerobic Sulfatases, and Mycofactocin.


Pssm-ID: 433020 [Multi-domain]  Cd Length: 66  Bit Score: 52.48  E-value: 3.82e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1181163972 238 CLVHWARFNIGITGDAVVCFNELFKEslhpGVVMGDVKKHSISEIWHNEKYRALRKAELLNDYSgfaqaealPCLNC 314
Cdd:pfam13186   1 CFAGWTSLVILPDGDVYPCFDDDFVG----PIVLGNIREQSLAEIWNSPKYREFRKLGKFALIE--------LCRDC 65
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 33-146 8.74e-07

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: 48.87  E-value: 8.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181163972  33 VEVFRGaCPCNCSHCPVGSTPaenrtmRFGARAIDLGLFEKIAAETGCHDWASLRIHSVGEPVLWPGLPEALQIAHKNNA 112
Cdd:cd01335     1 LELTRG-CNLNCGFCSNPASK------GRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELP 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1181163972 113 RPWLF--TCGVTNRRDYLDAICDYA-SIVEVSVNSID 146
Cdd:cd01335    74 GFEISieTNGTLLTEELLKELKELGlDGVGVSLDSGD 110
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 40-194 2.07e-05

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: 44.05  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181163972  40 CPCNCSHCPVGSTPAENRtmrfgARAIDLGLFEKIAAEtgCHDWASLRIHSV-GEPVLWPGLPEALQIAHKNNARPWLFT 118
Cdd:pfam04055   5 CNLRCTYCAFPSIRARGK-----GRELSPEEILEEAKE--LKRLGVEVVILGgGEPLLLPDLVELLERLLKLELAEGIRI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181163972 119 CGVTN----RRDYLDAICDY-ASIVEVSVNSIDSGNYLETKGIDAFELVCENIGYIHKRISKRGSNRLIVSRVQSQDPVL 193
Cdd:pfam04055  78 TLETNgtllDEELLELLKEAgLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETDEDLE 157


                  .
gi 1181163972 194 D 194
Cdd:pfam04055 158 E 158
 
Name Accession Description Interval E-value
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 39-172 5.90e-12

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: 63.00  E-value: 5.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181163972  39 ACPCNCSHCPVGSTPAENRTMrfgaraiDLGLFEKIAAETGCHDWASLRIhSVGEPVLWPGLPEALQIAHKNNARPWLFT 118
Cdd:COG0535     9 RCNLRCKHCYADAGPKRPGEL-------STEEAKRILDELAELGVKVVGL-TGGEPLLRPDLFELVEYAKELGIRVNLST 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1181163972 119 CGVTNRRDYLDAICDYA-SIVEVSVNSIDSGNYLETKGID-AFELVCENIGYIHKR 172
Cdd:COG0535    81 NGTLLTEELAERLAEAGlDHVTISLDGVDPETHDKIRGVPgAFDKVLEAIKLLKEA 136
SPASM cd21109
Iron-sulfur cluster-binding SPASM domain; This iron-sulfur cluster-binding domain is named ...
 237-314 1.92e-10

Iron-sulfur cluster-binding SPASM domain; This iron-sulfur cluster-binding domain is named SPASM after the biochemically characterized members, AlbA, PqqE, anSME, and MftC, which are involved in Subtilosin A, Pyrroloquinoline quinone, Anaerobic Sulfatase, and Mycofactocin maturation, respectively. SPASM occurs as an additional C-terminal domain in many peptide-modifying enzymes of the radical S-adenosylmethionine (SAM) superfamily. 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. Radical SAM enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster.


Pssm-ID: 410609 [Multi-domain]  Cd Length: 65  Bit Score: 55.89  E-value: 1.92e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1181163972 237 PCLVHWARFNIGITGDAVVCFNELFKEslhpgVVMGDVKKHSISEIWHNEKYRALRKAELLNDYSgfaqaealPCLNC 314
Cdd:cd21109     1 PCPAPWTSLYITPDGDVYPCCFDVNEE-----LKLGNIREQSLKEIWNSEKYREFRKLLLDGKIK--------LCKNC 65
SPASM pfam13186
Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur ...
 238-314 3.82e-09

Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur cluster binding domain in many radical SAM domain, pfam04055 proteins. The domain occurs in a number of proteins that modify a protein to become an active enzyme, or a peptide to become a ribosomal natural product. The domain is named SPASM because it occurs in the maturases of Subilitosin, PQQ, Anaerobic Sulfatases, and Mycofactocin.


Pssm-ID: 433020 [Multi-domain]  Cd Length: 66  Bit Score: 52.48  E-value: 3.82e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1181163972 238 CLVHWARFNIGITGDAVVCFNELFKEslhpGVVMGDVKKHSISEIWHNEKYRALRKAELLNDYSgfaqaealPCLNC 314
Cdd:pfam13186   1 CFAGWTSLVILPDGDVYPCFDDDFVG----PIVLGNIREQSLAEIWNSPKYREFRKLGKFALIE--------LCRDC 65
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 33-146 8.74e-07

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: 48.87  E-value: 8.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181163972  33 VEVFRGaCPCNCSHCPVGSTPaenrtmRFGARAIDLGLFEKIAAETGCHDWASLRIHSVGEPVLWPGLPEALQIAHKNNA 112
Cdd:cd01335     1 LELTRG-CNLNCGFCSNPASK------GRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELP 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1181163972 113 RPWLF--TCGVTNRRDYLDAICDYA-SIVEVSVNSID 146
Cdd:cd01335    74 GFEISieTNGTLLTEELLKELKELGlDGVGVSLDSGD 110
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 40-194 2.07e-05

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: 44.05  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181163972  40 CPCNCSHCPVGSTPAENRtmrfgARAIDLGLFEKIAAEtgCHDWASLRIHSV-GEPVLWPGLPEALQIAHKNNARPWLFT 118
Cdd:pfam04055   5 CNLRCTYCAFPSIRARGK-----GRELSPEEILEEAKE--LKRLGVEVVILGgGEPLLLPDLVELLERLLKLELAEGIRI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181163972 119 CGVTN----RRDYLDAICDY-ASIVEVSVNSIDSGNYLETKGIDAFELVCENIGYIHKRISKRGSNRLIVSRVQSQDPVL 193
Cdd:pfam04055  78 TLETNgtllDEELLELLKEAgLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETDEDLE 157


                  .
gi 1181163972 194 D 194
Cdd:pfam04055 158 E 158
SPASM_rSAM cd21126
Iron-sulfur cluster-binding SPASM domain of an uncharacterized group of radical SAM proteins; ...
 249-315 3.11e-05

Iron-sulfur cluster-binding SPASM domain of an uncharacterized group of radical SAM proteins; Members of this group are radical S-adenosylmethionine (SAM) enzymes with a SPASM domain, named after the biochemically characterized members, AlbA, PqqE, anSME, and MftC, which are involved in Subtilosin A, Pyrroloquinoline quinone, Anaerobic Sulfatase, and Mycofactocin maturation, respectively. 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. Radical SAM enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster. This group appears to contain one auxillary Fe-S cluster, similar to the auxillary 4Fe-4S cluster in Bacillus circulans butirosin biosynthetic enzyme BtrN.


Pssm-ID: 410617 [Multi-domain]  Cd Length: 70  Bit Score: 41.30  E-value: 3.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181163972 249 ITGDAVV---CFNelfKESLHpgvVMGDVKKHSISEIWHNEKYRALRKAeLLNDYSGFAQaealpCLNCS 315
Cdd:cd21126    12 ITWDGKVvpcCFD---KDASH---KLGDLKTQSFKELWCGKKYQQFRKQ-LLKSRSEIEI-----CKNCT 69
SPASM_BtrN cd21129
Iron-sulfur cluster-binding SPASM domain of butirosin biosynthesis protein N; Butirosin ...
 238-316 5.70e-05

Iron-sulfur cluster-binding SPASM domain of butirosin biosynthesis protein N; Butirosin biosynthesis protein N (BtrN), also called S-adenosyl-L-methionine-dependent 2-deoxy-scyllo-inosamine dehydrogenase (EC 1.1.99.38), is a radical S-adenosylmethionine (SAM) enzyme that catalyzes the two-electron oxidation of 2-deoxy-scyllo-inosamine (DOIA) to amino-dideoxy-scyllo-inosose (amino-DOI) in the biosynthetic pathway of the aminoglycoside antibiotic butirosin. 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. Radical SAM enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster. BtrN contains one auxillary 4Fe-4S cluster.


Pssm-ID: 410620 [Multi-domain]  Cd Length: 87  Bit Score: 41.25  E-value: 5.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1181163972 238 CLVHWARFNIGITGDAVVCFnelfkESLHPGVVMGDVKKHSISEIWHNEKYRALRKAeLLNDYSGFAQAealpCLNCSN 316
Cdd:cd21129     6 CMVPSNLAVVTVLGNVLPCF-----EDFNQKMVMGNIGEQHISDIWHNDKFTSFRKM-LKEGHRGKSDL----CKNCNN 74
SPASM_Cmo-like cd21121
Iron-sulfur cluster-binding SPASM domain of tungsten-containing aldehyde ferredoxin ...
 267-314 1.52e-03

Iron-sulfur cluster-binding SPASM domain of tungsten-containing aldehyde ferredoxin oxidoreductase cofactor-modifying protein and similar proteins; This group is composed of Pyrococcus furiosus tungsten-containing aldehyde ferredoxin oxidoreductase (AOR; EC 1.2.7.5) cofactor-modifying protein, encoded by the cmo gene, and similar proteins. AOR cofactor-modifying protein is involved in the biosynthesis of a molybdopterin-based tungsten cofactor. Members of this group are radical S-adenosylmethionine (SAM) enzymes with a SPASM domain. 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. Radical SAM enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster. This group appears to contain one auxillary Fe-S cluster, similar to the auxillary 4Fe-4S cluster in Bacillus circulans butirosin biosynthetic enzyme BtrN.


Pssm-ID: 410612 [Multi-domain]  Cd Length: 80  Bit Score: 36.89  E-value: 1.52e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1181163972 267 PGVVMGDVKKHSISEIWHNEKYRALRKAELLNDYSgfaqaealPCLNC 314
Cdd:cd21121    41 KRVIFGNVKEESLLEIWNSPEYRAFRENVLRGDYP--------PCRDC 80
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH