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Conserved domains on  [gi|489192602|ref|WP_003101947|]
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MULTISPECIES: folate-binding protein YgfZ [Pseudomonas]

Protein Classification

YgfZ/GcvT domain-containing protein( domain architecture ID 11417472)

YgfZ/GcvT domain-containing protein with similarity to Escherichia coli tRNA-modifying protein YgfZ and GcvT family member, mitochondrial putative transferase CAF17

CATH:  3.30.1360.120
Gene Ontology:  GO:0016740|GO:0005739|GO:0016226

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YgfZ COG0354
Folate-binding protein YgfZ, synthesis and repair of Fe-S clusters [Posttranslational ...
2-308 1.09e-100

Folate-binding protein YgfZ, synthesis and repair of Fe-S clusters [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440123 [Multi-domain]  Cd Length: 317  Bit Score: 298.34  E-value: 1.09e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602   2 ADPAFHTPLVHEGILAVRGPDAAKFLQGQLTCNLAYLNDETSSLGGRCNIKGRLLSSFRILPEGDGLLLAMAGELLEAQL 81
Cdd:COG0354   12 LAGAALVDLSDRGVIRVSGPDALKFLQGQLTNDVRALAPGQARLAALLTPKGRVLADFRVFRDGDGYLLDVPADLAEALL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602  82 ADLKKYAVFSKASLADESAAWLRIGL--RDASEALRALG-IDTPAESGRIArhGDLLAVALGDARVELWVPAQRAEAVLA 158
Cdd:COG0354   92 KRLKKYRLRSKVEIEDASDDLAVLGLagPAAAAALAALGaLADPAAHAVAD--GGTIRLPRPAPGYLLIVPAAAAAALWE 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602 159 TLREHSREAPLDDWLLGQVRAGIGQVFGATRELFIPQMINLQAVGGVSFKKGCYTGQEIVARMQYLGRLKRRLYRLALDA 238
Cdd:COG0354  170 ALAAGAAPAGSAAWEALRIAAGIPRIGADTDEDFIPQELNLDALGGVSFKKGCYPGQETVARMHYRGKVKRRLVLLHLDG 249
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489192602 239 DEVPAPGTGLFSPvhSTSVGEVVLAARTPENSVELLAVLQDDAV-ADGRISLGSAEGaPLVLLNLPYTLDS 308
Cdd:COG0354  250 SALPAPGTELLAG--GRPVGTVTSAARHPEGGPIALAVLRRDAAdAGAELRVGGAAA-TVIVLPLPYRLPE 317
 
Name Accession Description Interval E-value
YgfZ COG0354
Folate-binding protein YgfZ, synthesis and repair of Fe-S clusters [Posttranslational ...
2-308 1.09e-100

Folate-binding protein YgfZ, synthesis and repair of Fe-S clusters [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440123 [Multi-domain]  Cd Length: 317  Bit Score: 298.34  E-value: 1.09e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602   2 ADPAFHTPLVHEGILAVRGPDAAKFLQGQLTCNLAYLNDETSSLGGRCNIKGRLLSSFRILPEGDGLLLAMAGELLEAQL 81
Cdd:COG0354   12 LAGAALVDLSDRGVIRVSGPDALKFLQGQLTNDVRALAPGQARLAALLTPKGRVLADFRVFRDGDGYLLDVPADLAEALL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602  82 ADLKKYAVFSKASLADESAAWLRIGL--RDASEALRALG-IDTPAESGRIArhGDLLAVALGDARVELWVPAQRAEAVLA 158
Cdd:COG0354   92 KRLKKYRLRSKVEIEDASDDLAVLGLagPAAAAALAALGaLADPAAHAVAD--GGTIRLPRPAPGYLLIVPAAAAAALWE 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602 159 TLREHSREAPLDDWLLGQVRAGIGQVFGATRELFIPQMINLQAVGGVSFKKGCYTGQEIVARMQYLGRLKRRLYRLALDA 238
Cdd:COG0354  170 ALAAGAAPAGSAAWEALRIAAGIPRIGADTDEDFIPQELNLDALGGVSFKKGCYPGQETVARMHYRGKVKRRLVLLHLDG 249
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489192602 239 DEVPAPGTGLFSPvhSTSVGEVVLAARTPENSVELLAVLQDDAV-ADGRISLGSAEGaPLVLLNLPYTLDS 308
Cdd:COG0354  250 SALPAPGTELLAG--GRPVGTVTSAARHPEGGPIALAVLRRDAAdAGAELRVGGAAA-TVIVLPLPYRLPE 317
PRK09559 PRK09559
putative global regulator; Reviewed
20-307 6.51e-55

putative global regulator; Reviewed


Pssm-ID: 236567 [Multi-domain]  Cd Length: 327  Bit Score: 181.42  E-value: 6.51e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602  20 GPDAAKFLQGQLTCNLAYLNDETSSLGGRCNIKGRLLSSFRILPEGDGLLLAMAGELLEAQLADLKKYAVFSKASLA-DE 98
Cdd:PRK09559  34 GADSEKYLQGQVTADVSQLTEDQHLLAAHCDAKGKMWSNLRLFRRGDGFAWIERRSVRENQLTELKKYAVFSKVTIApDD 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602  99 SAAWLRIGLRDASEALRALGIDTPAESGRIARHGD--LLAVALGDARVELWVPAQRAEAVLATLREhsrEAPLDD---WL 173
Cdd:PRK09559 114 ERVLLGVAGFQARAALANLFSELPDAEKPVVQEGAttLLWFEHPAERFLLVTDEATANMLTEKLRG---EAQLNNsqqWL 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602 174 LGQVRAGIGQVFGATRELFIPQMINLQAVGGVSFKKGCYTGQEIVARMQYLGRLKRRLYRLALDADEVPAPGTGLfspvh 253
Cdd:PRK09559 191 ALDIEAGFPVIDAANSGQFIPQATNLQALGGISFKKGCYTGQEMVARAKFRGANKRALWWLAGKASRVPEAGEDL----- 265
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489192602 254 STSVGE------VVLAA-RTPENSVELLAVLQDDAVADGRISLGSAEGAPLVLLNLPYTLD 307
Cdd:PRK09559 266 ELKMGEnwrrtgTVLAAvQLDDGQVWVQVVMNNDLEADSVFRVRDDAGNTLHIQPLPYSLE 326
ygfZ_signature TIGR03317
folate-binding protein YgfZ; YgfZ is a protein from Escherichia coli, homologous to the ...
170-234 5.90e-31

folate-binding protein YgfZ; YgfZ is a protein from Escherichia coli, homologous to the glycine cleavage system T protein, or aminomethyltransferase, GcvT (TIGR00528). Homologs of YgfZ other than members of the GcvT family share a well-conserved signature region that includes the motif, KGCYxGQE. Elsewhere, sequence diverge and length variation are substantial. Members of this family are mostly bacterial, largely absent from the Firmicutes and otherwise usually present. A few eukaryotic examples are found among the Apicomplexa, and a few archaeal sequences are found. Two functions implicated for this folate-binding protein are RNA modification (a function likely to be conserved) and replication initiation (a function likely to be highly variable). Many members of this family are, at the time of construction of this model, misnamed as the glycine cleavage system T protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 274518 [Multi-domain]  Cd Length: 67  Bit Score: 111.09  E-value: 5.90e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489192602  170 DDWLLGQVRAGIGQVFGATRELFIPQMINLQAVGGVSFKKGCYTGQEIVARMQYLGRLKRRLYRL 234
Cdd:TIGR03317   1 EAWELLRIAAGIPEGGAETSGEFIPQELNLDALGGVSFDKGCYVGQEVVARMHYRGKVKRRLVPL 65
GCV_T pfam01571
Aminomethyltransferase folate-binding domain; This is a family of glycine cleavage T-proteins, ...
12-162 7.52e-04

Aminomethyltransferase folate-binding domain; This is a family of glycine cleavage T-proteins, part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes. GCV catalyzes the catabolism of glycine in eukaryotes. The T-protein is an aminomethyl transferase.


Pssm-ID: 460255  Cd Length: 254  Bit Score: 40.26  E-value: 7.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602   12 HEGILAVRGPDAAKFLQGQLTCNLAYLNDETSSLGGRCNIKGRLLSSFRILPEGDGLLLAMAGE-LLEAQLADLKKYAVF 90
Cdd:pfam01571  46 HMGKIEVSGPDAAAFLQRLTTNDVSKLKPGRATYTLMLNERGGVIDDLTVYRLGDDHFLLVVNAaNREKDLAWLRKHAEK 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602   91 SKASLADESAAWLRIGL--------------RDASEALRALG---IDTPAESGRIARHGdllavALGDARVELWVPAQRA 153
Cdd:pfam01571 126 LDVVVVDVTDDYALLALqgpkarevlekltdGDLLEALPFFSfreIEIGGVPVRVSRTG-----YTGEDGFEIYVPAEDA 200

                  ....*....
gi 489192602  154 EAVLATLRE 162
Cdd:pfam01571 201 VELWEALLE 209
 
Name Accession Description Interval E-value
YgfZ COG0354
Folate-binding protein YgfZ, synthesis and repair of Fe-S clusters [Posttranslational ...
2-308 1.09e-100

Folate-binding protein YgfZ, synthesis and repair of Fe-S clusters [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440123 [Multi-domain]  Cd Length: 317  Bit Score: 298.34  E-value: 1.09e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602   2 ADPAFHTPLVHEGILAVRGPDAAKFLQGQLTCNLAYLNDETSSLGGRCNIKGRLLSSFRILPEGDGLLLAMAGELLEAQL 81
Cdd:COG0354   12 LAGAALVDLSDRGVIRVSGPDALKFLQGQLTNDVRALAPGQARLAALLTPKGRVLADFRVFRDGDGYLLDVPADLAEALL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602  82 ADLKKYAVFSKASLADESAAWLRIGL--RDASEALRALG-IDTPAESGRIArhGDLLAVALGDARVELWVPAQRAEAVLA 158
Cdd:COG0354   92 KRLKKYRLRSKVEIEDASDDLAVLGLagPAAAAALAALGaLADPAAHAVAD--GGTIRLPRPAPGYLLIVPAAAAAALWE 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602 159 TLREHSREAPLDDWLLGQVRAGIGQVFGATRELFIPQMINLQAVGGVSFKKGCYTGQEIVARMQYLGRLKRRLYRLALDA 238
Cdd:COG0354  170 ALAAGAAPAGSAAWEALRIAAGIPRIGADTDEDFIPQELNLDALGGVSFKKGCYPGQETVARMHYRGKVKRRLVLLHLDG 249
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489192602 239 DEVPAPGTGLFSPvhSTSVGEVVLAARTPENSVELLAVLQDDAV-ADGRISLGSAEGaPLVLLNLPYTLDS 308
Cdd:COG0354  250 SALPAPGTELLAG--GRPVGTVTSAARHPEGGPIALAVLRRDAAdAGAELRVGGAAA-TVIVLPLPYRLPE 317
PRK09559 PRK09559
putative global regulator; Reviewed
20-307 6.51e-55

putative global regulator; Reviewed


Pssm-ID: 236567 [Multi-domain]  Cd Length: 327  Bit Score: 181.42  E-value: 6.51e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602  20 GPDAAKFLQGQLTCNLAYLNDETSSLGGRCNIKGRLLSSFRILPEGDGLLLAMAGELLEAQLADLKKYAVFSKASLA-DE 98
Cdd:PRK09559  34 GADSEKYLQGQVTADVSQLTEDQHLLAAHCDAKGKMWSNLRLFRRGDGFAWIERRSVRENQLTELKKYAVFSKVTIApDD 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602  99 SAAWLRIGLRDASEALRALGIDTPAESGRIARHGD--LLAVALGDARVELWVPAQRAEAVLATLREhsrEAPLDD---WL 173
Cdd:PRK09559 114 ERVLLGVAGFQARAALANLFSELPDAEKPVVQEGAttLLWFEHPAERFLLVTDEATANMLTEKLRG---EAQLNNsqqWL 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602 174 LGQVRAGIGQVFGATRELFIPQMINLQAVGGVSFKKGCYTGQEIVARMQYLGRLKRRLYRLALDADEVPAPGTGLfspvh 253
Cdd:PRK09559 191 ALDIEAGFPVIDAANSGQFIPQATNLQALGGISFKKGCYTGQEMVARAKFRGANKRALWWLAGKASRVPEAGEDL----- 265
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489192602 254 STSVGE------VVLAA-RTPENSVELLAVLQDDAVADGRISLGSAEGAPLVLLNLPYTLD 307
Cdd:PRK09559 266 ELKMGEnwrrtgTVLAAvQLDDGQVWVQVVMNNDLEADSVFRVRDDAGNTLHIQPLPYSLE 326
ygfZ_signature TIGR03317
folate-binding protein YgfZ; YgfZ is a protein from Escherichia coli, homologous to the ...
170-234 5.90e-31

folate-binding protein YgfZ; YgfZ is a protein from Escherichia coli, homologous to the glycine cleavage system T protein, or aminomethyltransferase, GcvT (TIGR00528). Homologs of YgfZ other than members of the GcvT family share a well-conserved signature region that includes the motif, KGCYxGQE. Elsewhere, sequence diverge and length variation are substantial. Members of this family are mostly bacterial, largely absent from the Firmicutes and otherwise usually present. A few eukaryotic examples are found among the Apicomplexa, and a few archaeal sequences are found. Two functions implicated for this folate-binding protein are RNA modification (a function likely to be conserved) and replication initiation (a function likely to be highly variable). Many members of this family are, at the time of construction of this model, misnamed as the glycine cleavage system T protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 274518 [Multi-domain]  Cd Length: 67  Bit Score: 111.09  E-value: 5.90e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489192602  170 DDWLLGQVRAGIGQVFGATRELFIPQMINLQAVGGVSFKKGCYTGQEIVARMQYLGRLKRRLYRL 234
Cdd:TIGR03317   1 EAWELLRIAAGIPEGGAETSGEFIPQELNLDALGGVSFDKGCYVGQEVVARMHYRGKVKRRLVPL 65
GCV_T pfam01571
Aminomethyltransferase folate-binding domain; This is a family of glycine cleavage T-proteins, ...
12-162 7.52e-04

Aminomethyltransferase folate-binding domain; This is a family of glycine cleavage T-proteins, part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes. GCV catalyzes the catabolism of glycine in eukaryotes. The T-protein is an aminomethyl transferase.


Pssm-ID: 460255  Cd Length: 254  Bit Score: 40.26  E-value: 7.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602   12 HEGILAVRGPDAAKFLQGQLTCNLAYLNDETSSLGGRCNIKGRLLSSFRILPEGDGLLLAMAGE-LLEAQLADLKKYAVF 90
Cdd:pfam01571  46 HMGKIEVSGPDAAAFLQRLTTNDVSKLKPGRATYTLMLNERGGVIDDLTVYRLGDDHFLLVVNAaNREKDLAWLRKHAEK 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192602   91 SKASLADESAAWLRIGL--------------RDASEALRALG---IDTPAESGRIARHGdllavALGDARVELWVPAQRA 153
Cdd:pfam01571 126 LDVVVVDVTDDYALLALqgpkarevlekltdGDLLEALPFFSfreIEIGGVPVRVSRTG-----YTGEDGFEIYVPAEDA 200

                  ....*....
gi 489192602  154 EAVLATLRE 162
Cdd:pfam01571 201 VELWEALLE 209
 
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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