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Conserved domains on  [gi|1332876550|ref|WP_102838827|]
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ComF family protein [Stutzerimonas frequens]

Protein Classification

ComF family protein( domain architecture ID 16072570)

ComF family protein is a predicted amidophosphoribosyltransferase; similar to Haemophilus influenzae competence protein F, which is involved in DNA transformation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 38-231 1.24e-66

DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];


:

Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 204.29  E-value: 1.24e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550  38 RCTVCAvpLPSRGLVCGECLKrppsydhvEVPWRFAFPVDALITRFKHQARWPYGRLLGERLAHHLEHAFadgLPRPDLL 117
Cdd:COG1040    16 RCLLCG--AAPGGGLCPDCRA--------KAAFRYEGPLRRLILALKYRGRLDLARLLARLLARALREAL---LPRPDLI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550 118 LPVPLARRRLRQRGFNQAQMLADWLSRPLGIATDARVLERVLDTPAQQQLDAATRRRNLRQAFAIATGADIKGRHLALVD 197
Cdd:COG1040    83 VPVPLHRRRLRRRGFNQAELLARALARALGIPVLPDLLRRVRATPSQAGLSRAERRRNLRGAFAVRPPARLAGKHVLLVD 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1332876550 198 DVLTTGATAEALARLLKRAGAERVDVYCLARTPK 231
Cdd:COG1040   163 DVLTTGATLAEAARALKAAGAARVDVLVLARTPR 196
DZR_2 pfam18912
Double zinc ribbon domain; This domain family is found in bacteria, archaea and eukaryotes, ...
 11-57 2.84e-06

Double zinc ribbon domain; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 60 amino acids in length. The family is found in association with pfam00156. This entry corresponds to two zinc ribbon motifs. This domain is found at the N-terminus of the ComF operon protein 3.


:

Pssm-ID: 465906 [Multi-domain]  Cd Length: 56  Bit Score: 43.43  E-value: 2.84e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1332876550  11 HCLLCDER-CEGQPLCSHCEADLPWLDG-RCTVCAVPLPSrGLVCGECL 57
Cdd:pfam18912   9 RCPLCGAIvAEGGGLCAACWAELPFITEpRCPRCGKPLEE-GELCGDCL 56
 
Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 38-231 1.24e-66

DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 204.29  E-value: 1.24e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550  38 RCTVCAvpLPSRGLVCGECLKrppsydhvEVPWRFAFPVDALITRFKHQARWPYGRLLGERLAHHLEHAFadgLPRPDLL 117
Cdd:COG1040    16 RCLLCG--AAPGGGLCPDCRA--------KAAFRYEGPLRRLILALKYRGRLDLARLLARLLARALREAL---LPRPDLI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550 118 LPVPLARRRLRQRGFNQAQMLADWLSRPLGIATDARVLERVLDTPAQQQLDAATRRRNLRQAFAIATGADIKGRHLALVD 197
Cdd:COG1040    83 VPVPLHRRRLRRRGFNQAELLARALARALGIPVLPDLLRRVRATPSQAGLSRAERRRNLRGAFAVRPPARLAGKHVLLVD 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1332876550 198 DVLTTGATAEALARLLKRAGAERVDVYCLARTPK 231
Cdd:COG1040   163 DVLTTGATLAEAARALKAAGAARVDVLVLARTPR 196
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 11-229 6.10e-49

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 160.20  E-value: 6.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550  11 HCLLCDercegQPL-------CSHCEADLPWLDGRCTVCAVPLPSRGLVCGECLKRPPSYDHVEVPWRFAFPVDALITRF 83
Cdd:PRK11595    7 LCWLCR-----MPLalshwgiCSVCSRALRTLKTCCPQCGLPATHPHLPCGRCLQKPPPWQRLVFVSDYAPPLSGLIHQL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550  84 KHQARWPYGRLLGERLAHHLEHAFADG-LPRPDLLLPVPLARRRLRQRGFNQAQMLADWLSRPLGIATDARVLERVLDTP 162
Cdd:PRK11595   82 KFSRRSELASVLARLLLLEWLQARRSTgLQKPDRIISVPLHQRRHWRRGFNQSDLLCRPLARWLGCDYDSEALTRTRATA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1332876550 163 AQQQLDAATRRRNLRQAFAIAtgADIKGRHLALVDDVLTTGATAEALARLLKRAGAERVDVYCLART 229
Cdd:PRK11595  162 TQHFLSARLRKRNLKNAFRLE--LPVQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASVQVWCLCRT 226
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 39-228 6.81e-30

comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus influenzae) or do not (E. coli, Borrelia burgdorferi) have described systems for natural transformation with exogenous DNA. It is involved in competence for transformation in Bacillus subtilis. [Cellular processes, DNA transformation]


Pssm-ID: 272958 [Multi-domain]  Cd Length: 190  Bit Score: 109.92  E-value: 6.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550  39 CTVCAVPLPSRGLVCGEClKRPPSYDHVEVPWR--------FAFPVDALITRFKHQARWPYGRLLGERLAHHLEHAFADg 110
Cdd:TIGR00201   1 CSLCGRPYQSVHALCRQC-GSWRTRIRDSLCLRqnlvsvytYNEPLKELISRFKFRGQAEIIRALASLLSLTVSKAYRD- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550 111 lpRPDLLLPVPLARRRLRQRGFNQAQMLADWLSRPLgiATDARVLERVlDTPAQQQLDAATRRRNLRQAFAIATgADIKG 190
Cdd:TIGR00201  79 --LPDVIVPVPLSKEREWRRGFNQADLLAQCLSRWL--FNYHNIVIRL-NNETQSKLKATLRFLNLENAFDLKN-NSFQG 152

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1332876550 191 RHLALVDDVLTTGATAEALARLLKRAGAERVDVYCLAR 228
Cdd:TIGR00201 153 RNIVLVDDVVTTGATLHEIARLLLELGAASVQVWTLAR 190
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 95-234 3.51e-18

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 77.44  E-value: 3.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550  95 LGERLAHHLEHAFADglprPDLLLPVPLarrrlrqRGFNQAQMLADWLSRPLGIATDARvlervldtpaqqqlDAATRRR 174
Cdd:cd06223     1 AGRLLAEEIREDLLE----PDVVVGILR-------GGLPLAAALARALGLPLAFIRKER--------------KGPGRTP 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550 175 NLRQAFAIATGADIKGRHLALVDDVLTTGATAEALARLLKRAGAERVDVYCLARTPKPGE 234
Cdd:cd06223    56 SEPYGLELPLGGDVKGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGA 115
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 186-230 1.83e-06

Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.


Pssm-ID: 425489 [Multi-domain]  Cd Length: 150  Bit Score: 46.20  E-value: 1.83e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1332876550 186 ADIKGRHLALVDDVLTTGATAEALARLLKRAGAERVDVYCLARTP 230
Cdd:pfam00156  78 PDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKP 122
DZR_2 pfam18912
Double zinc ribbon domain; This domain family is found in bacteria, archaea and eukaryotes, ...
 11-57 2.84e-06

Double zinc ribbon domain; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 60 amino acids in length. The family is found in association with pfam00156. This entry corresponds to two zinc ribbon motifs. This domain is found at the N-terminus of the ComF operon protein 3.


Pssm-ID: 465906 [Multi-domain]  Cd Length: 56  Bit Score: 43.43  E-value: 2.84e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1332876550  11 HCLLCDER-CEGQPLCSHCEADLPWLDG-RCTVCAVPLPSrGLVCGECL 57
Cdd:pfam18912   9 RCPLCGAIvAEGGGLCAACWAELPFITEpRCPRCGKPLEE-GELCGDCL 56
 
Name Accession Description Interval E-value
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 38-231 1.24e-66

DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 204.29  E-value: 1.24e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550  38 RCTVCAvpLPSRGLVCGECLKrppsydhvEVPWRFAFPVDALITRFKHQARWPYGRLLGERLAHHLEHAFadgLPRPDLL 117
Cdd:COG1040    16 RCLLCG--AAPGGGLCPDCRA--------KAAFRYEGPLRRLILALKYRGRLDLARLLARLLARALREAL---LPRPDLI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550 118 LPVPLARRRLRQRGFNQAQMLADWLSRPLGIATDARVLERVLDTPAQQQLDAATRRRNLRQAFAIATGADIKGRHLALVD 197
Cdd:COG1040    83 VPVPLHRRRLRRRGFNQAELLARALARALGIPVLPDLLRRVRATPSQAGLSRAERRRNLRGAFAVRPPARLAGKHVLLVD 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1332876550 198 DVLTTGATAEALARLLKRAGAERVDVYCLARTPK 231
Cdd:COG1040   163 DVLTTGATLAEAARALKAAGAARVDVLVLARTPR 196
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 11-229 6.10e-49

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 160.20  E-value: 6.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550  11 HCLLCDercegQPL-------CSHCEADLPWLDGRCTVCAVPLPSRGLVCGECLKRPPSYDHVEVPWRFAFPVDALITRF 83
Cdd:PRK11595    7 LCWLCR-----MPLalshwgiCSVCSRALRTLKTCCPQCGLPATHPHLPCGRCLQKPPPWQRLVFVSDYAPPLSGLIHQL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550  84 KHQARWPYGRLLGERLAHHLEHAFADG-LPRPDLLLPVPLARRRLRQRGFNQAQMLADWLSRPLGIATDARVLERVLDTP 162
Cdd:PRK11595   82 KFSRRSELASVLARLLLLEWLQARRSTgLQKPDRIISVPLHQRRHWRRGFNQSDLLCRPLARWLGCDYDSEALTRTRATA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1332876550 163 AQQQLDAATRRRNLRQAFAIAtgADIKGRHLALVDDVLTTGATAEALARLLKRAGAERVDVYCLART 229
Cdd:PRK11595  162 TQHFLSARLRKRNLKNAFRLE--LPVQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASVQVWCLCRT 226
comF TIGR00201
comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus ...
 39-228 6.81e-30

comF family protein; This protein is found in species that do (Bacillus subtilis, Haemophilus influenzae) or do not (E. coli, Borrelia burgdorferi) have described systems for natural transformation with exogenous DNA. It is involved in competence for transformation in Bacillus subtilis. [Cellular processes, DNA transformation]


Pssm-ID: 272958 [Multi-domain]  Cd Length: 190  Bit Score: 109.92  E-value: 6.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550  39 CTVCAVPLPSRGLVCGEClKRPPSYDHVEVPWR--------FAFPVDALITRFKHQARWPYGRLLGERLAHHLEHAFADg 110
Cdd:TIGR00201   1 CSLCGRPYQSVHALCRQC-GSWRTRIRDSLCLRqnlvsvytYNEPLKELISRFKFRGQAEIIRALASLLSLTVSKAYRD- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550 111 lpRPDLLLPVPLARRRLRQRGFNQAQMLADWLSRPLgiATDARVLERVlDTPAQQQLDAATRRRNLRQAFAIATgADIKG 190
Cdd:TIGR00201  79 --LPDVIVPVPLSKEREWRRGFNQADLLAQCLSRWL--FNYHNIVIRL-NNETQSKLKATLRFLNLENAFDLKN-NSFQG 152

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1332876550 191 RHLALVDDVLTTGATAEALARLLKRAGAERVDVYCLAR 228
Cdd:TIGR00201 153 RNIVLVDDVVTTGATLHEIARLLLELGAASVQVWTLAR 190
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 95-234 3.51e-18

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 77.44  E-value: 3.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550  95 LGERLAHHLEHAFADglprPDLLLPVPLarrrlrqRGFNQAQMLADWLSRPLGIATDARvlervldtpaqqqlDAATRRR 174
Cdd:cd06223     1 AGRLLAEEIREDLLE----PDVVVGILR-------GGLPLAAALARALGLPLAFIRKER--------------KGPGRTP 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550 175 NLRQAFAIATGADIKGRHLALVDDVLTTGATAEALARLLKRAGAERVDVYCLARTPKPGE 234
Cdd:cd06223    56 SEPYGLELPLGGDVKGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGA 115
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 189-233 5.49e-08

Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism]; Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440269  Cd Length: 171  Bit Score: 50.84  E-value: 5.49e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1332876550 189 KGRHLALVDDVLTTGATAEALARLLKRAGAERVDVYCLARTPKPG 233
Cdd:COG0503   111 PGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLG 155
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 185-230 6.15e-08

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 50.75  E-value: 6.15e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1332876550 185 GAD---IKGRHLALVDDVLTTGATAEALARLLKRAGA---------------ERVDVYCLARTP 230
Cdd:PRK07322  112 GADaekLKGKRVAIVDDVVSTGGTLTALERLVERAGGqvvakaaifaegdasNRLDVIYLAHLP 175
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 182-226 3.65e-07

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 48.53  E-value: 3.65e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1332876550 182 IATGADIKGRHLALVDDVLTTGATAEALARLLKRAGAERVDVYCL 226
Cdd:PRK02304  106 IHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFV 150
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 187-225 1.53e-06

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 47.99  E-value: 1.53e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1332876550 187 DIKGRHLALVDDVLTTGAT-AEAlARLLKRAGAERVDVYC 225
Cdd:PRK00934  201 DVKGKDVLIVDDIISTGGTmATA-IKILKEQGAKKVYVAC 239
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 186-230 1.83e-06

Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.


Pssm-ID: 425489 [Multi-domain]  Cd Length: 150  Bit Score: 46.20  E-value: 1.83e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1332876550 186 ADIKGRHLALVDDVLTTGATAEALARLLKRAGAERVDVYCLARTP 230
Cdd:pfam00156  78 PDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKP 122
DZR_2 pfam18912
Double zinc ribbon domain; This domain family is found in bacteria, archaea and eukaryotes, ...
 11-57 2.84e-06

Double zinc ribbon domain; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 60 amino acids in length. The family is found in association with pfam00156. This entry corresponds to two zinc ribbon motifs. This domain is found at the N-terminus of the ComF operon protein 3.


Pssm-ID: 465906 [Multi-domain]  Cd Length: 56  Bit Score: 43.43  E-value: 2.84e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1332876550  11 HCLLCDER-CEGQPLCSHCEADLPWLDG-RCTVCAVPLPSrGLVCGECL 57
Cdd:pfam18912   9 RCPLCGAIvAEGGGLCAACWAELPFITEpRCPRCGKPLEE-GELCGDCL 56
COG1926 COG1926
Predicted phosphoribosyltransferase [General function prediction only];
148-221 2.92e-06

Predicted phosphoribosyltransferase [General function prediction only];


Pssm-ID: 441529  Cd Length: 209  Bit Score: 46.61  E-value: 2.92e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1332876550 148 IATDARVLERVLDTPAQQQLDAATRRRNL-RQAFAIAtgaDIKGRHLALVDDVLTTGATAEALARLLKRAGAERV 221
Cdd:COG1926    81 LIRRLGISEEYIEAEKAREREELERRRRRyRGGRPPP---DLKGRTVILVDDGIATGATMRAALRALRRQGPARI 152
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 187-225 3.16e-05

Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis


Pssm-ID: 440230 [Multi-domain]  Cd Length: 311  Bit Score: 43.89  E-value: 3.16e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1332876550 187 DIKGRHLALVDDVLTTGATAEALARLLKRAGAERVDVYC 225
Cdd:COG0462   208 DVEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYAAA 246
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 187-233 3.76e-05

Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; Hypoxanthine-guanine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440399  Cd Length: 176  Bit Score: 42.71  E-value: 3.76e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1332876550 187 DIKGRHLALVDDVLTTGATAEALARLLKRAGAERVDVYCLARtpKPG 233
Cdd:COG0634    88 DIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLD--KPE 132
PRK07199 PRK07199
ribose-phosphate diphosphokinase;
135-223 6.64e-05

ribose-phosphate diphosphokinase;


Pssm-ID: 235960 [Multi-domain]  Cd Length: 301  Bit Score: 43.00  E-value: 6.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550 135 AQMLADWL----SRPLGIATDARVLERVLDTPAQQQLDAA----TRRRNLRQAFAIATGADIKGRHLALVDDVLTTGATA 206
Cdd:PRK07199  148 APAIAAWIrahvPRPLLIGPDEESEQWVAAVAERAGAPHAvlrkTRHGDRDVEISLPDAAPWAGRTPVLVDDIVSTGRTL 227

                          90
                  ....*....|....*..
gi 1332876550 207 EALARLLKRAGAERVDV 223
Cdd:PRK07199  228 IEAARQLRAAGAASPDC 244
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 185-226 6.81e-05

Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440229  Cd Length: 201  Bit Score: 42.45  E-value: 6.81e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1332876550 185 GADIKGRHLALVDDVLTTGATAEALARLLKRAGAERVDVYCL 226
Cdd:COG0461   107 GGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVI 148
PLN02293 PLN02293
adenine phosphoribosyltransferase
 185-231 1.42e-04

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 41.20  E-value: 1.42e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1332876550 185 GADIKGRHLALVDDVLTTGATAEALARLLKRAGAERVDVYCLARTPK 231
Cdd:PLN02293  120 GAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVECACVIELPE 166
PRK04923 PRK04923
ribose-phosphate diphosphokinase;
142-225 2.08e-04

ribose-phosphate diphosphokinase;


Pssm-ID: 179893 [Multi-domain]  Cd Length: 319  Bit Score: 41.45  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876550 142 LSRPLGIATDARVLERVLDTPAQQQLDAATRRRNLRQAFAIAtgADIKGRHLALVDDVLTTGATAEALARLLKRAGAERV 221
Cdd:PRK04923  171 VSPDVGGVVRARAVAKRLDDADLAIIDKRRPRANVATVMNII--GDVQGKTCVLVDDLVDTAGTLCAAAAALKQRGALKV 248


                  ....
gi 1332876550 222 DVYC 225
Cdd:PRK04923  249 VAYI 252
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 186-223 2.86e-04

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 40.41  E-value: 2.86e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1332876550 186 ADIKGRHLALVDDVLTTGATAEALARLLKRAGAERVDV 223
Cdd:PLN02238   93 IDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSV 130
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
187-225 8.83e-04

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 39.72  E-value: 8.83e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1332876550 187 DIKGRHLALVDDVLTTGATAEALARLLKRAGAERVDVYC 225
Cdd:PRK01259  205 DVEGRDCILVDDMIDTAGTLCKAAEALKERGAKSVYAYA 243
PRK02812 PRK02812
ribose-phosphate pyrophosphokinase; Provisional
 187-221 1.25e-03

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235072 [Multi-domain]  Cd Length: 330  Bit Score: 39.34  E-value: 1.25e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1332876550 187 DIKGRHLALVDDVLTTGATAEALARLLKRAGAERV 221
Cdd:PRK02812  227 DVKGKTAILVDDMIDTGGTICEGARLLRKEGAKQV 261
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 184-226 1.45e-03

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 38.60  E-value: 1.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1332876550 184 TGADIKGRHLALVDDVLTTGATAEALARLLKRAGAERVDVYCL 226
Cdd:PRK00455  107 EGRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVI 149
PLN02297 PLN02297
ribose-phosphate pyrophosphokinase
 187-225 3.06e-03

ribose-phosphate pyrophosphokinase


Pssm-ID: 177934 [Multi-domain]  Cd Length: 326  Bit Score: 38.13  E-value: 3.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1332876550 187 DIKGRHLALVDDVLTTGATAEALARLLKRAGAERVDVYC 225
Cdd:PLN02297  227 NPAGRHVVIVDDLVQSGGTLIECQKVLAAHGAAKVSAYV 265
PRK06031 PRK06031
phosphoribosyltransferase; Provisional
 188-221 3.83e-03

phosphoribosyltransferase; Provisional


Pssm-ID: 235678  Cd Length: 233  Bit Score: 37.43  E-value: 3.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1332876550 188 IKGRHLALVDDVLTTGATAEALARLLKRAGAERV 221
Cdd:PRK06031  152 LEGRRVALIDDVISSGASIVAGLRLLAACGIEPA 185
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
187-221 5.30e-03

ribose-phosphate diphosphokinase;


Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 37.23  E-value: 5.30e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1332876550 187 DIKGRHLALVDDVLTTGATAEALARLLKRAGAERV 221
Cdd:PRK03092  198 DVEGRTCVLVDDMIDTGGTIAGAVRALKEAGAKDV 232
PRK02458 PRK02458
ribose-phosphate pyrophosphokinase; Provisional
 152-227 5.31e-03

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235039 [Multi-domain]  Cd Length: 323  Bit Score: 37.41  E-value: 5.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1332876550 152 ARVLERVLDTPAQQqLDAATRRRNLRQAFAIAtgaDIKGRHLALVDDVLTTGAT-AEAlARLLKRAGAerVDVYCLA 227
Cdd:PRK02458  184 ARSLAEYLDAPIAI-IDYAQDDSEREEGYIIG---DVAGKKAILIDDILNTGKTfAEA-AKIVEREGA--TEIYAVA 253
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 187-226 6.31e-03

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 36.60  E-value: 6.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1332876550 187 DIKGRHLALVDDVLTTGATAEALARLLKRAGAERVDVYCL 226
Cdd:PRK00129  121 DIDERTVIVVDPMLATGGSAIAAIDLLKKRGAKNIKVLCL 160
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
 189-226 8.45e-03

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 36.51  E-value: 8.45e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1332876550 189 KGRHLALVDDVLTTGATAEALARLLKRAGAERVDVYCL 226
Cdd:PRK08558  175 KGDRVLIVDDIIRSGETQRALLDLARQAGADVVGVFFL 212
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 186-221 9.17e-03

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 36.00  E-value: 9.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1332876550 186 ADIKGRHLALVDDVLTTGATAEALARLLKRAGAERV 221
Cdd:PRK02277  136 ASVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPV 171
 
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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