NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489740806|ref|WP_003644871|]
View 

anaerobic ribonucleoside-triphosphate reductase activating protein [Lactiplantibacillus plantarum]

Protein Classification

4Fe-4S single cluster domain-containing protein( domain architecture ID 12135473)

4Fe-4S single cluster domain-containing protein binds iron-sulfur clusters

Gene Ontology:  GO:0051539
PubMed:  29601957

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 24-163 2.02e-79

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: 232.45  E-value: 2.02e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806   24 VDGEGVRCSLYLSGCPFHCPGCYNVAAQNFHYGQPYSQELEDQIIEDLGQDYVQGLTLLGGEPFLNTQVGIRICERIRSE 103
Cdd:pfam13353   1 VNGPGVRCSLFVSGCNHHCKGCFNPETWDFKYGKPFTEELEDEIIEDLAKPYIQGLTLSGGEPLLNAEALLELVKRVREE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806  104 FENtKDIWSWSGYTWEELQqdSEDKLKMLSLIDILVDGRFLQDKMDLSLQFRGSSNQRII 163
Cdd:pfam13353  81 CPE-KDIWLWTGYTFEELQ--SKDQLELLKLIDVLVDGKFEQSLKDPSLRFRGSSNQRII 137
 
Name Accession Description Interval E-value
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 24-163 2.02e-79

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: 232.45  E-value: 2.02e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806   24 VDGEGVRCSLYLSGCPFHCPGCYNVAAQNFHYGQPYSQELEDQIIEDLGQDYVQGLTLLGGEPFLNTQVGIRICERIRSE 103
Cdd:pfam13353   1 VNGPGVRCSLFVSGCNHHCKGCFNPETWDFKYGKPFTEELEDEIIEDLAKPYIQGLTLSGGEPLLNAEALLELVKRVREE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806  104 FENtKDIWSWSGYTWEELQqdSEDKLKMLSLIDILVDGRFLQDKMDLSLQFRGSSNQRII 163
Cdd:pfam13353  81 CPE-KDIWLWTGYTFEELQ--SKDQLELLKLIDVLVDGKFEQSLKDPSLRFRGSSNQRII 137
NrdG TIGR02491
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 14-166 2.96e-68

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055) and utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487). The two components form an alpha-2/beta-2 heterodimer. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274161 [Multi-domain]  Cd Length: 154  Bit Score: 204.89  E-value: 2.96e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806   14 YVADYKAFNFVDGEGVRCSLYLSGCPFHCPGCYNVAAQNFHYGQPYSQELEDQIIEDLGQD-YVQGLTLLGGEPFLNTQV 92
Cdd:TIGR02491   1 NYMNIKPDDIVNGEGIRVSLFVAGCKHHCEGCFNKETWNFNGGKEFTEALEKEIIRDLNDNpLIDGLTLSGGDPLYPRNV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489740806   93 G--IRICERIRSEFENtKDIWSWSGYTWEELQQDsEDKLKMLSLIDILVDGRFLQDKMDLSLQFRGSSNQRIIDVP 166
Cdd:TIGR02491  81 EelIELVKKIKAEFPE-KDIWLWTGYTWEEILED-EKHLEVLKYIDVLVDGKFELSKKDLKLKFRGSSNQRIIDLK 154
nrdG PRK11121
anaerobic ribonucleoside-triphosphate reductase-activating protein;
18-162 9.38e-51

anaerobic ribonucleoside-triphosphate reductase-activating protein;


Pssm-ID: 236853  Cd Length: 154  Bit Score: 160.16  E-value: 9.38e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806  18 YKAFNFVDGEGVRCSLYLSGCPFHCPGCYNVAAQNFHYGQPYSQELEDQIIEDLgQD---YVQGLTLLGGEPFL--NTQV 92
Cdd:PRK11121   6 YYPVDVVNGPGTRCTLFVSGCVHQCPGCYNKSTWRLNSGHPFTKEMEDQIIADL-NDtriKRQGLSLSGGDPLHpqNVPD 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806  93 GIRICERIRSEFENtKDIWSWSGYTWEELqqdSEDKLKMLSLIDILVDGRFLQDKMDLSLQFRGSSNQRI 162
Cdd:PRK11121  85 ILKLVQRVKAECPG-KDIWVWTGYKLDEL---NAAQRQVVDLIDVLVDGKFVQDLADPSLIWRGSSNQVI 150
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 14-140 6.67e-14

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 67.13  E-value: 6.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806  14 YVADYKAFNFVDGEG-VRCSLYLSGCPFHCPGCYN---VAAQNFHYGQPYS-QELEDQIIEDLGQ-DYVQGLTLLGGEPF 87
Cdd:COG1180    6 RIYGISPFSTVDGPGsIRLSVFTQGCNLRCPYCHNpeiSQGRPDAAGRELSpEELVEEALKDRGFlDSCGGVTFSGGEPT 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489740806  88 LNTQVGIRICERIRSE-FENtkdIWSWSGY-TWEELQqdsedklKMLSLID-ILVD 140
Cdd:COG1180   86 LQPEFLLDLAKLAKELgLHT---ALDTNGYiPEEALE-------ELLPYLDaVNID 131
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 37-120 3.47e-05

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: 42.71  E-value: 3.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806  37 GCPFHCPGCYNvaAQNFHYGQPYSQELEDQIIEDLGQ--DYVQGLTLLGGEPFLNTQVGIRIcERIRSEFENTKDIWSWS 114
Cdd:cd01335    6 GCNLNCGFCSN--PASKGRGPESPPEIEEILDIVLEAkeRGVEVVILTGGEPLLYPELAELL-RRLKKELPGFEISIETN 82


                 ....*.
gi 489740806 115 GYTWEE 120
Cdd:cd01335   83 GTLLTE 88
 
Name Accession Description Interval E-value
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 24-163 2.02e-79

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: 232.45  E-value: 2.02e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806   24 VDGEGVRCSLYLSGCPFHCPGCYNVAAQNFHYGQPYSQELEDQIIEDLGQDYVQGLTLLGGEPFLNTQVGIRICERIRSE 103
Cdd:pfam13353   1 VNGPGVRCSLFVSGCNHHCKGCFNPETWDFKYGKPFTEELEDEIIEDLAKPYIQGLTLSGGEPLLNAEALLELVKRVREE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806  104 FENtKDIWSWSGYTWEELQqdSEDKLKMLSLIDILVDGRFLQDKMDLSLQFRGSSNQRII 163
Cdd:pfam13353  81 CPE-KDIWLWTGYTFEELQ--SKDQLELLKLIDVLVDGKFEQSLKDPSLRFRGSSNQRII 137
NrdG TIGR02491
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 14-166 2.96e-68

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055) and utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487). The two components form an alpha-2/beta-2 heterodimer. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274161 [Multi-domain]  Cd Length: 154  Bit Score: 204.89  E-value: 2.96e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806   14 YVADYKAFNFVDGEGVRCSLYLSGCPFHCPGCYNVAAQNFHYGQPYSQELEDQIIEDLGQD-YVQGLTLLGGEPFLNTQV 92
Cdd:TIGR02491   1 NYMNIKPDDIVNGEGIRVSLFVAGCKHHCEGCFNKETWNFNGGKEFTEALEKEIIRDLNDNpLIDGLTLSGGDPLYPRNV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489740806   93 G--IRICERIRSEFENtKDIWSWSGYTWEELQQDsEDKLKMLSLIDILVDGRFLQDKMDLSLQFRGSSNQRIIDVP 166
Cdd:TIGR02491  81 EelIELVKKIKAEFPE-KDIWLWTGYTWEEILED-EKHLEVLKYIDVLVDGKFELSKKDLKLKFRGSSNQRIIDLK 154
nrdG PRK11121
anaerobic ribonucleoside-triphosphate reductase-activating protein;
18-162 9.38e-51

anaerobic ribonucleoside-triphosphate reductase-activating protein;


Pssm-ID: 236853  Cd Length: 154  Bit Score: 160.16  E-value: 9.38e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806  18 YKAFNFVDGEGVRCSLYLSGCPFHCPGCYNVAAQNFHYGQPYSQELEDQIIEDLgQD---YVQGLTLLGGEPFL--NTQV 92
Cdd:PRK11121   6 YYPVDVVNGPGTRCTLFVSGCVHQCPGCYNKSTWRLNSGHPFTKEMEDQIIADL-NDtriKRQGLSLSGGDPLHpqNVPD 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806  93 GIRICERIRSEFENtKDIWSWSGYTWEELqqdSEDKLKMLSLIDILVDGRFLQDKMDLSLQFRGSSNQRI 162
Cdd:PRK11121  85 ILKLVQRVKAECPG-KDIWVWTGYKLDEL---NAAQRQVVDLIDVLVDGKFVQDLADPSLIWRGSSNQVI 150
Fer4_14 pfam13394
4Fe-4S single cluster domain;
33-142 5.19e-42

4Fe-4S single cluster domain;


Pssm-ID: 433171 [Multi-domain]  Cd Length: 115  Bit Score: 136.72  E-value: 5.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806   33 LYLSGCPFHCPGCYNVAAQNFHYGQPYSQELEDQIIEDLGQDYV--QGLTLLGGEPF--LNTQVGIRICERIRSEFEnTK 108
Cdd:pfam13394   1 LFVSGCNHSCPGCDNKETWKFNYGEPFTEELEDQIIADLKDSYIkrQGLVLTGGEPLhpWNLPVLLKLLKRVKEEYP-SK 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489740806  109 DIWSWSGYTWEE--LQQDSEDKLKMLSLIDILVDGR 142
Cdd:pfam13394  80 DIWLETGYTLAIdfEYPDTEEQLFTLSVIDVLVDGK 115
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 14-140 6.67e-14

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 67.13  E-value: 6.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806  14 YVADYKAFNFVDGEG-VRCSLYLSGCPFHCPGCYN---VAAQNFHYGQPYS-QELEDQIIEDLGQ-DYVQGLTLLGGEPF 87
Cdd:COG1180    6 RIYGISPFSTVDGPGsIRLSVFTQGCNLRCPYCHNpeiSQGRPDAAGRELSpEELVEEALKDRGFlDSCGGVTFSGGEPT 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489740806  88 LNTQVGIRICERIRSE-FENtkdIWSWSGY-TWEELQqdsedklKMLSLID-ILVD 140
Cdd:COG1180   86 LQPEFLLDLAKLAKELgLHT---ALDTNGYiPEEALE-------ELLPYLDaVNID 131
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 37-110 2.94e-06

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: 45.21  E-value: 2.94e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489740806   37 GCPFHCPGCYNVAAQNFHYGQPYSQELEDQIIEDLGQDYVQGLTLLGGEPFLNTQVGIRICERIRSEFENTKDI 110
Cdd:pfam04055   4 GCNLRCTYCAFPSIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAEGIRI 77
RNR_activ_nrdG3 TIGR02826
anaerobic ribonucleoside-triphosphate reductase activating protein; Members of this family ...
 32-165 7.60e-06

anaerobic ribonucleoside-triphosphate reductase activating protein; Members of this family represent a set of radical SAM enzymes related to, yet architecturally different from, the activating protein for the glycine radical-containing, oxygen-sensitive ribonucleoside-triphosphate reductase (RNR) as described in model TIGR02491. Members of this family are found paired with members of a similarly divergent set of anaerobic ribonucleoside-triphosphate reductases. Identification of this protein as an RNR activitating protein is partly from pairing with a candidate RNR. It is further supported by our finding that upstream of these operons are examples of a conserved regulatory element (described Rodionov and Gelfand) that is found in nearly all bacteria and that occurs specifically upstream of operons for all three classes of RNR genes. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]


Pssm-ID: 274317  Cd Length: 147  Bit Score: 43.88  E-value: 7.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806   32 SLYLSGCPFHCPGCYNVAAQNFHYGQPYSQELEDQIIEDLGQDyVQGLTLLGGEpfLNTQVGIRICERIRSEfENTKDIW 111
Cdd:TIGR02826  19 AFYISGCPLGCPGCHSPELWHEDEGTPLTPEVLAQLLDKYRSL-ITCVLFLGGE--WEPEALLSLLKYVKEH-AGLKVCL 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489740806  112 swsgYTWEElqqdSEDKLKMLSLIDILVDGRFLQDKMDLSLQfrgSSNQRIIDV 165
Cdd:TIGR02826  95 ----YTGRE----PKDPLELVQHLDYLKTGPWIETLGGLDSP---TTNQRFYDI 137
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 38-102 8.76e-06

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: 43.74  E-value: 8.76e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489740806  38 CPFHCPGCYNvaaqnfHYGQPYSQELE----DQIIEDLGQDYVQGLTLLGGEPFLNTQVgIRICERIRS 102
Cdd:COG0535   10 CNLRCKHCYA------DAGPKRPGELSteeaKRILDELAELGVKVVGLTGGEPLLRPDL-FELVEYAKE 71
NrdG2 TIGR02495
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 15-98 1.27e-05

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055). It is often gene clustered with the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487) and presumably fulfills the identical function as NrdG, which utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in NrdD. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274164 [Multi-domain]  Cd Length: 192  Bit Score: 43.51  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806   15 VADYKAFNFVDGEG-VRCSLYLSGCPFHCPGCYNVAAQnfhYGQPYSQELEDQIIEDL--GQDYVQGLTLLGGEPFLNTQ 91
Cdd:TIGR02495   2 IAGLVPFSTVDYPGkLAFTIFLQGCNLKCPYCHNPLLI---PRRGSGEIEVEELLEFLrrRRGLLDGVVITGGEPTLQAG 78


                  ....*..
gi 489740806   92 VGIRICE 98
Cdd:TIGR02495  79 LPDFLRE 85
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 37-120 3.47e-05

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: 42.71  E-value: 3.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806  37 GCPFHCPGCYNvaAQNFHYGQPYSQELEDQIIEDLGQ--DYVQGLTLLGGEPFLNTQVGIRIcERIRSEFENTKDIWSWS 114
Cdd:cd01335    6 GCNLNCGFCSN--PASKGRGPESPPEIEEILDIVLEAkeRGVEVVILTGGEPLLYPELAELL-RRLKKELPGFEISIETN 82


                 ....*.
gi 489740806 115 GYTWEE 120
Cdd:cd01335   83 GTLLTE 88
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
 36-110 3.38e-03

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 37.27  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489740806  36 SGCPFHCPGCYnvaAQNFHYGQPY--SQELEDQIIEDLGQDYVQG----LTLLGGEPFLNTQVGIRICERIRSEFENTKD 109
Cdd:COG0641    9 SRCNLRCSYCY---YSEGDEGSRRrmSEETAEKAIDFLIESSGPGkeltITFFGGEPLLNFDFIKEIVEYARKYAKKGKK 85


                 .
gi 489740806 110 I 110
Cdd:COG0641   86 I 86
 
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