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Conserved domains on  [gi|518095985|ref|WP_019266193|]
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2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase [Methanobrevibacter smithii]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ArfB_arch_rifla NF033501
2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase; MJ0116 ...
3-227 1.57e-112

2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase; MJ0116 from Methanocaldococcus jannaschii, the founding member of this family, was shown be 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase, catalyzing the second step in archaeal riboflavin and Fo biosynthesis.


:

Pssm-ID: 411143  Cd Length: 219  Bit Score: 321.19  E-value: 1.57e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518095985   3 ELRYRAGKIKNPGVHKIGIIALGSHLENHGPALPIDTDAKIGAHIAFQASLESGAKFLGIIFPAYELDEIDHGVHVSLDE 82
Cdd:NF033501   1 ELRLNSGNILNEKVHKIGIIALGSHLENHGPALPIDTDIKIASYIALNASIKTGAKFLGVVYPATEYDYVKHGIHNSLDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518095985  83 LKGNVIKTLNSAKKyLDIEKVVIVNSHGGNIPLMTELYDIEDETGLTIIFNNKIIStegpHGGSGELSMAKVLGIVNEAE 162
Cdd:NF033501  81 LVEYIKFLLNSAKK-IGIEKFLIVNCHGGNILIEKEIKDLEEKTGLKIIMNNKIIT----HAGTGELSMGYVIGIADETK 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518095985 163 IKNQTDlSKYEEVGLYGFKQARENDPNIEEGARDVEENGVYVDEVYGKQLFDLAINSVVFDVEKL 227
Cdd:NF033501 156 LKEHTP-EKYPEIGMVGLKEARENNKNIDEEAKIVEKNGVKVDEVLGQKLLKNAINSVVNDVKKL 219
 
Name Accession Description Interval E-value
ArfB_arch_rifla NF033501
2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase; MJ0116 ...
3-227 1.57e-112

2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase; MJ0116 from Methanocaldococcus jannaschii, the founding member of this family, was shown be 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase, catalyzing the second step in archaeal riboflavin and Fo biosynthesis.


Pssm-ID: 411143  Cd Length: 219  Bit Score: 321.19  E-value: 1.57e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518095985   3 ELRYRAGKIKNPGVHKIGIIALGSHLENHGPALPIDTDAKIGAHIAFQASLESGAKFLGIIFPAYELDEIDHGVHVSLDE 82
Cdd:NF033501   1 ELRLNSGNILNEKVHKIGIIALGSHLENHGPALPIDTDIKIASYIALNASIKTGAKFLGVVYPATEYDYVKHGIHNSLDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518095985  83 LKGNVIKTLNSAKKyLDIEKVVIVNSHGGNIPLMTELYDIEDETGLTIIFNNKIIStegpHGGSGELSMAKVLGIVNEAE 162
Cdd:NF033501  81 LVEYIKFLLNSAKK-IGIEKFLIVNCHGGNILIEKEIKDLEEKTGLKIIMNNKIIT----HAGTGELSMGYVIGIADETK 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518095985 163 IKNQTDlSKYEEVGLYGFKQARENDPNIEEGARDVEENGVYVDEVYGKQLFDLAINSVVFDVEKL 227
Cdd:NF033501 156 LKEHTP-EKYPEIGMVGLKEARENNKNIDEEAKIVEKNGVKVDEVLGQKLLKNAINSVVNDVKKL 219
Creatininase pfam02633
Creatinine amidohydrolase; Creatinine amidohydrolase (EC:3.5.2.10), or creatininase, catalyzes ...
18-221 3.58e-08

Creatinine amidohydrolase; Creatinine amidohydrolase (EC:3.5.2.10), or creatininase, catalyzes the hydrolysis of creatinine to creatine.


Pssm-ID: 426892  Cd Length: 226  Bit Score: 52.25  E-value: 3.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518095985   18 KIGIIALGSHlENHGPALPIDTDAKIGAHIAFQASLESGAKFLGIIFPAYELDEIDH--GVHVSLDELKGNVIKTLNSAK 95
Cdd:pfam02633   8 DVAILPVGST-EQHGPHLPLGTDTLIAEAIAERVAERAPALVLPTLPYGVSPEHRGFpgTISLSPETLIAVLRDIVRSLA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518095985   96 KYlDIEKVVIVNSHGGNIPLMTE-LYDIEDETGLTIIF-----------------NNKIISTEGPHGGSGELSMAKVL-- 155
Cdd:pfam02633  87 RH-GFRKIVLVNGHGGNVAALKEaARELRAEHDMAVRDgflavafswsrvgalaaLLSEDEEGGGHAGEAETSLMLALrp 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518095985  156 GIVNEAEIKNQTDLSKYEEVGLYGFkqarendpniEEGARDVEENGVY-----VDEVYGKQLFDLAINSVV 221
Cdd:pfam02633 166 ELVRMDRAEDGEPAPLDPEGLPAPF----------AWDTRDLSPSGVLgdptlATAEKGEALLEAAVDALV 226
ArfB COG1402
Creatinine amidohydrolase/Fe(II)-dependent FAPy formamide hydrolase (riboflavin and F420 ...
17-230 1.04e-07

Creatinine amidohydrolase/Fe(II)-dependent FAPy formamide hydrolase (riboflavin and F420 biosynthesis) [Coenzyme transport and metabolism]; Creatinine amidohydrolase/Fe(II)-dependent FAPy formamide hydrolase (riboflavin and F420 biosynthesis) is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 441012  Cd Length: 236  Bit Score: 51.00  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518095985  17 HKIGIIALGShLENHGPALPIDTDAKIGAHIAfqasLESGAKFLGIIF-------PAYELDEIDHGVHVSLDELKGNVIK 89
Cdd:COG1402   17 DDVAILPVGS-TEQHGPHLPLGTDTLIAEAVA----ERVAERLPGVLVlptipygVSPEHLGFPGTISLSPETLIAVLRD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518095985  90 TLNSAKKYlDIEKVVIVNSHGGNIPLMT----ELYdiEDETGLTIIFNN------------KIISTEGPHGGSGELSMAK 153
Cdd:COG1402   92 IGESLARH-GFRRIVLVNGHGGNVAALKeaarELR--AEHPGMLVVVLNwwrlappglalsEGEETGGGHAGELETSLML 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518095985 154 VL--GIVNEAEIKNqtdlskyeevglygfkqARENDPNIEEGARDVEENGVYVD-----EVYGKQLFDLAINSVVFDVEK 226
Cdd:COG1402  169 ALrpELVRMDRAAD-----------------GPPAGLPIGLLSRDLTPSGVLGDptlatAEKGEALLEAAVEALVELLRE 231

                 ....
gi 518095985 227 LLDF 230
Cdd:COG1402  232 LAAA 235
 
Name Accession Description Interval E-value
ArfB_arch_rifla NF033501
2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase; MJ0116 ...
3-227 1.57e-112

2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase; MJ0116 from Methanocaldococcus jannaschii, the founding member of this family, was shown be 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase, catalyzing the second step in archaeal riboflavin and Fo biosynthesis.


Pssm-ID: 411143  Cd Length: 219  Bit Score: 321.19  E-value: 1.57e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518095985   3 ELRYRAGKIKNPGVHKIGIIALGSHLENHGPALPIDTDAKIGAHIAFQASLESGAKFLGIIFPAYELDEIDHGVHVSLDE 82
Cdd:NF033501   1 ELRLNSGNILNEKVHKIGIIALGSHLENHGPALPIDTDIKIASYIALNASIKTGAKFLGVVYPATEYDYVKHGIHNSLDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518095985  83 LKGNVIKTLNSAKKyLDIEKVVIVNSHGGNIPLMTELYDIEDETGLTIIFNNKIIStegpHGGSGELSMAKVLGIVNEAE 162
Cdd:NF033501  81 LVEYIKFLLNSAKK-IGIEKFLIVNCHGGNILIEKEIKDLEEKTGLKIIMNNKIIT----HAGTGELSMGYVIGIADETK 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518095985 163 IKNQTDlSKYEEVGLYGFKQARENDPNIEEGARDVEENGVYVDEVYGKQLFDLAINSVVFDVEKL 227
Cdd:NF033501 156 LKEHTP-EKYPEIGMVGLKEARENNKNIDEEAKIVEKNGVKVDEVLGQKLLKNAINSVVNDVKKL 219
Creatininase pfam02633
Creatinine amidohydrolase; Creatinine amidohydrolase (EC:3.5.2.10), or creatininase, catalyzes ...
18-221 3.58e-08

Creatinine amidohydrolase; Creatinine amidohydrolase (EC:3.5.2.10), or creatininase, catalyzes the hydrolysis of creatinine to creatine.


Pssm-ID: 426892  Cd Length: 226  Bit Score: 52.25  E-value: 3.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518095985   18 KIGIIALGSHlENHGPALPIDTDAKIGAHIAFQASLESGAKFLGIIFPAYELDEIDH--GVHVSLDELKGNVIKTLNSAK 95
Cdd:pfam02633   8 DVAILPVGST-EQHGPHLPLGTDTLIAEAIAERVAERAPALVLPTLPYGVSPEHRGFpgTISLSPETLIAVLRDIVRSLA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518095985   96 KYlDIEKVVIVNSHGGNIPLMTE-LYDIEDETGLTIIF-----------------NNKIISTEGPHGGSGELSMAKVL-- 155
Cdd:pfam02633  87 RH-GFRKIVLVNGHGGNVAALKEaARELRAEHDMAVRDgflavafswsrvgalaaLLSEDEEGGGHAGEAETSLMLALrp 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518095985  156 GIVNEAEIKNQTDLSKYEEVGLYGFkqarendpniEEGARDVEENGVY-----VDEVYGKQLFDLAINSVV 221
Cdd:pfam02633 166 ELVRMDRAEDGEPAPLDPEGLPAPF----------AWDTRDLSPSGVLgdptlATAEKGEALLEAAVDALV 226
ArfB COG1402
Creatinine amidohydrolase/Fe(II)-dependent FAPy formamide hydrolase (riboflavin and F420 ...
17-230 1.04e-07

Creatinine amidohydrolase/Fe(II)-dependent FAPy formamide hydrolase (riboflavin and F420 biosynthesis) [Coenzyme transport and metabolism]; Creatinine amidohydrolase/Fe(II)-dependent FAPy formamide hydrolase (riboflavin and F420 biosynthesis) is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 441012  Cd Length: 236  Bit Score: 51.00  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518095985  17 HKIGIIALGShLENHGPALPIDTDAKIGAHIAfqasLESGAKFLGIIF-------PAYELDEIDHGVHVSLDELKGNVIK 89
Cdd:COG1402   17 DDVAILPVGS-TEQHGPHLPLGTDTLIAEAVA----ERVAERLPGVLVlptipygVSPEHLGFPGTISLSPETLIAVLRD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518095985  90 TLNSAKKYlDIEKVVIVNSHGGNIPLMT----ELYdiEDETGLTIIFNN------------KIISTEGPHGGSGELSMAK 153
Cdd:COG1402   92 IGESLARH-GFRRIVLVNGHGGNVAALKeaarELR--AEHPGMLVVVLNwwrlappglalsEGEETGGGHAGELETSLML 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518095985 154 VL--GIVNEAEIKNqtdlskyeevglygfkqARENDPNIEEGARDVEENGVYVD-----EVYGKQLFDLAINSVVFDVEK 226
Cdd:COG1402  169 ALrpELVRMDRAAD-----------------GPPAGLPIGLLSRDLTPSGVLGDptlatAEKGEALLEAAVEALVELLRE 231

                 ....
gi 518095985 227 LLDF 230
Cdd:COG1402  232 LAAA 235
 
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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