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Conserved domains on  [gi|2500652|sp|Q60335|]
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RecName: Full=RNA 3'-terminal phosphate cyclase; Short=RNA cyclase; Short=RNA-3'-phosphate cyclase

Protein Classification

RNA 3'-terminal phosphate cyclase( domain architecture ID 11480222)

RNA 3'-terminal phosphate cyclase catalyzes the ATP-dependent conversion of terminal 3'-phosphate of RNA to the 2',3'-cyclic phosphodiester

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK04204 PRK04204
RNA 3'-terminal phosphate cyclase;
2-337 0e+00

RNA 3'-terminal phosphate cyclase;


:

Pssm-ID: 235255 [Multi-domain]  Cd Length: 343  Bit Score: 525.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652     2 DFIVIDGSYLEGGGQIIRTAVSLSALTQKPVKIINIRKKRKNKGLAPQHVSAVKAVKKLCNAEVFGLNVGSEELTFIPSK 81
Cdd:PRK04204   1 RMIEIDGSYGEGGGQILRTALALSAITGKPFRITNIRANRPNPGLLRQHLTAVKAAAEICNAEVEGAELGSQELVFIPGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    82 LSPKDFTIDIGTAGSISLVIQTLLPLSLGINKKFTVKIKGGTDVKRAPPIDYVKNVTLKILRNFGVLTELKVLKRGFYPE 161
Cdd:PRK04204  81 IRGGDYRFDIGTAGSITLVLQTVLPALLFADGPSRVTITGGTDVPWAPPIDYIRRVTLPLLRRMGIEAEIELLRRGFYPA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652   162 GGGEVIFEVKPSKIKKFDLIEHSKSNLVEGISYVQNLDESIARRMRKKAVDLLNKEKLLPNI---KIECSKGISTGAGIV 238
Cdd:PRK04204 161 GGGEVALEVEPSKLRPLELLERGELLRIRGISHVANLPEHVAERQAKAAAELLALSLGLIEIeinVEELSRGLGPGSGIV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652   239 LW----NDTLGGSCLGEKGLRAEIVAERAVNELLKERESGMALDKYMGDQIIPFLAF--GKGIVGVSEITNHTKTNMWVV 312
Cdd:PRK04204 241 LWaeseHITEGFDALGERGKPAEVVGEEAAEELLRYLASGAAVDEHLADQLILPMALagGEGSFTVAELTSHLLTNIWVV 320
                        330       340
                 ....*....|....*....|....*
gi 2500652   313 KHFLDVDFEIKEYkenncNGFTIEV 337
Cdd:PRK04204 321 EKFLPVKFEVEEY-----DGVVIKV 340
 
Name Accession Description Interval E-value
PRK04204 PRK04204
RNA 3'-terminal phosphate cyclase;
2-337 0e+00

RNA 3'-terminal phosphate cyclase;


Pssm-ID: 235255 [Multi-domain]  Cd Length: 343  Bit Score: 525.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652     2 DFIVIDGSYLEGGGQIIRTAVSLSALTQKPVKIINIRKKRKNKGLAPQHVSAVKAVKKLCNAEVFGLNVGSEELTFIPSK 81
Cdd:PRK04204   1 RMIEIDGSYGEGGGQILRTALALSAITGKPFRITNIRANRPNPGLLRQHLTAVKAAAEICNAEVEGAELGSQELVFIPGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    82 LSPKDFTIDIGTAGSISLVIQTLLPLSLGINKKFTVKIKGGTDVKRAPPIDYVKNVTLKILRNFGVLTELKVLKRGFYPE 161
Cdd:PRK04204  81 IRGGDYRFDIGTAGSITLVLQTVLPALLFADGPSRVTITGGTDVPWAPPIDYIRRVTLPLLRRMGIEAEIELLRRGFYPA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652   162 GGGEVIFEVKPSKIKKFDLIEHSKSNLVEGISYVQNLDESIARRMRKKAVDLLNKEKLLPNI---KIECSKGISTGAGIV 238
Cdd:PRK04204 161 GGGEVALEVEPSKLRPLELLERGELLRIRGISHVANLPEHVAERQAKAAAELLALSLGLIEIeinVEELSRGLGPGSGIV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652   239 LW----NDTLGGSCLGEKGLRAEIVAERAVNELLKERESGMALDKYMGDQIIPFLAF--GKGIVGVSEITNHTKTNMWVV 312
Cdd:PRK04204 241 LWaeseHITEGFDALGERGKPAEVVGEEAAEELLRYLASGAAVDEHLADQLILPMALagGEGSFTVAELTSHLLTNIWVV 320
                        330       340
                 ....*....|....*....|....*
gi 2500652   313 KHFLDVDFEIKEYkenncNGFTIEV 337
Cdd:PRK04204 321 EKFLPVKFEVEEY-----DGVVIKV 340
RNA_3prim_cycl TIGR03399
RNA 3'-phosphate cyclase; Members of this protein family are RNA 3'-phosphate cyclase (6.5.1.4) ...
4-321 2.84e-176

RNA 3'-phosphate cyclase; Members of this protein family are RNA 3'-phosphate cyclase (6.5.1.4), an enzyme whose function is conserved from E. coli to human. The modification this enzyme performs enables certain RNA ligations to occur, although the full biological roll for this enzyme is not fully described. This model separates this enzyme from a related protein, present only in eukaryotes, localized to the nucleolus, and involved in ribosomal modification. [Transcription, RNA processing]


Pssm-ID: 274563 [Multi-domain]  Cd Length: 326  Bit Score: 491.40  E-value: 2.84e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652      4 IVIDGSYLEGGGQIIRTAVSLSALTQKPVKIINIRKKRKNKGLAPQHVSAVKAVKKLCNAEVFGLNVGSEELTFIPSKLS 83
Cdd:TIGR03399   1 IEIDGSYGEGGGQILRTALSLSALTGKPVRIYNIRANRPKPGLAPQHLTAVKAAAEICNAEVEGAELGSTELEFIPGKIR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652     84 PKDFTIDIGTAGSISLVIQTLLPLSLGINKKFTVKIKGGTDVKRAPPIDYVKNVTLKILRNFGVLTELKVLKRGFYPEGG 163
Cdd:TIGR03399  81 GGDYRFDIGTAGSVTLVLQTLLPALLFANGPSRVTVSGGTDVPWAPPVDYLRNVFLPLLERMGIRAELELLRRGFYPRGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    164 GEVIFEVKP-SKIKKFDLIEHSKSNLVEGISYVQNLDESIARRMRKKAVDLLNKEKLLPNIKIEC-SKGISTGAGIVLWN 241
Cdd:TIGR03399 161 GEVRLRVEPvKKLKPLELEERGELLRVSGIAHAANLPAHVAERMAKAAREELRKLGLDPEIEIEVlDKGLGPGSGIVLWA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    242 DT----LGGSCLGEKGLRAEIVAERAVNELLKERESGMALDKYMGDQIIPFLAF--GKGIVGVSEITNHTKTNMWVVKHF 315
Cdd:TIGR03399 241 ETehcrLGFSALGEKGKSAEKVGEEAAEQLLAELRSGAAVDEHLADQLILYMALasGESRFTTSELTMHLRTNIWVIEQF 320

                  ....*.
gi 2500652    316 LDVDFE 321
Cdd:TIGR03399 321 LPVRFE 326
RCL1 COG0430
RNA 3'-terminal phosphate cyclase [RNA processing and modification];
4-337 3.02e-173

RNA 3'-terminal phosphate cyclase [RNA processing and modification];


Pssm-ID: 440199  Cd Length: 340  Bit Score: 484.24  E-value: 3.02e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    4 IVIDGSYLEGGGQIIRTAVSLSALTQKPVKIINIRKKRKNKGLAPQHVSAVKAVKKLCNAEVFGLNVGSEELTFIPSKLS 83
Cdd:COG0430   2 IEIDGSYGEGGGQILRTALALSALTGKPVRITNIRAGRPKPGLRPQHLTAVKAAAEICGAEVEGAELGSTELTFRPGPVR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652   84 PKDFTIDIGTAGSISLVIQTLLPLSLGINKKFTVKIKGGTDVKRAPPIDYVKNVTLKILRNFGVLTELKVLKRGFYPEGG 163
Cdd:COG0430  82 GGDYRFDIGTAGSTTLVLQTLLPALALADGPSRLTLTGGTHVPWSPPFDYLERVFLPLLRRMGAEAELELLRRGFYPAGG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652  164 GEVIFEVKPSK-IKKFDLIEHSKSNLVEGISYVQNLDESIARRMRKKAVDLLNKEKLLPNIKIECSKGISTGAGIVLW-- 240
Cdd:COG0430 162 GEVTLTVEPSAlLRPLDLLERGELLRVRGISLVANLPAHVAERQAEAARERLGEAGLEVEIEVEVRPALGPGSGIVLWae 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652  241 --NDTLGGSCLGEKGLRAEIVAERAVNELLKERESGMALDKYMGDQIIPFLAF--GKGIVGVSEITNHTKTNMWVVKHFL 316
Cdd:COG0430 242 yeHGTEGFDALGERGKPAERVGEEAAEELLEFLASGAAVDEHLADQLLLPLALagGEGRFTVSELTDHLLTNIWVIEQFL 321
                       330       340
                ....*....|....*....|.
gi 2500652  317 DVDFEIKEYKEnncNGFTIEV 337
Cdd:COG0430 322 GVRIEVEGEEG---GPGRVTV 339
RNA_Cyclase_Class_II cd00874
RNA 3' phosphate cyclase domain (class II). These proteins function as RNA cyclase to catalyze ...
6-324 1.09e-170

RNA 3' phosphate cyclase domain (class II). These proteins function as RNA cyclase to catalyze the ATP-dependent conversion of 3'-phosphate to a 2'.3'-cyclic phosphodiester at the end of RNA molecule. A conserved catalytic histidine residue is found in all members of this subfamily.


Pssm-ID: 238446 [Multi-domain]  Cd Length: 326  Bit Score: 477.10  E-value: 1.09e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    6 IDGSYLEGGGQIIRTAVSLSALTQKPVKIINIRKKRKNKGLAPQHVSAVKAVKKLCNAEVFGLNVGSEELTFIPSKLSPK 85
Cdd:cd00874   1 IDGSYGEGGGQILRTALALSAVTGKPVRIVNIRANRSNPGLSRQHLTAVRAAARICNAEVEGAELGSTELEFEPGKIKGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652   86 DFTIDIGTAGSISLVIQTLLPLSLGINKKFTVKIKGGTDVKRAPPIDYVKNVTLKILRNFGVLTELKVLKRGFYPEGGGE 165
Cdd:cd00874  81 DYEFDIGTAGSITLVLQTLLPALLFADGPSTVTISGGTDVPWAPPIDYLRNVTLPLLERMGIEAELEVLRRGFYPRGGGE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652  166 VIFEVKPSKIKKFDLIEHSKSNL-VEGISYVQNLDESIARRMRKKAVDLLNKE-KLLPNIKIECSKGISTGAGIVLWNDT 243
Cdd:cd00874 161 VVLTVEPSKLLPPLLLEERGEIEkIRGISHAANLPPHVAERQAEAAAALLRKAlGLQIEIEPEDQSALGPGSGIVLWAEY 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652  244 ----LGGSCLGEKGLRAEIVAERAVNELLKERESGMALDKYMGDQIIPFLAF-GKGIVGVSEITNHTKTNMWVVKHFLDV 318
Cdd:cd00874 241 ehsrLGFSALGKKGVPAEKVGEEAAEELLAYLSSGAAVDEHLADQLIPFMALaGGSEFRTGELTLHLQTNIWVIEKFLGV 320

                ....*.
gi 2500652  319 DFEIKE 324
Cdd:cd00874 321 KFRIEE 326
RTC pfam01137
RNA 3'-terminal phosphate cyclase; RNA cyclases are a family of RNA-modifying enzymes that are ...
10-322 3.57e-150

RNA 3'-terminal phosphate cyclase; RNA cyclases are a family of RNA-modifying enzymes that are conserved in all cellular organizms. They catalyze the ATP-dependent conversion of the 3'-phosphate to the 2',3'-cyclic phosphodiester at the end of RNA, in a reaction involving formation of the covalent AMP-cyclase intermediate. The structure of RTC demonstrates that RTCs are comprised two domain. The larger domain contains an insert domain of approximately 100 amino acids.


Pssm-ID: 460079 [Multi-domain]  Cd Length: 324  Bit Score: 425.00  E-value: 3.57e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652     10 YLEGGGQIIRTAVSLSALTQKPVKIINIRKKRKNKGLAPQHVSAVKAVKKLCNAEVFGLNVGSEELTFIPSKLSPKDFTI 89
Cdd:pfam01137   1 YGEGGGQILRTALALSALTGKPVRIENIRANRPKPGLRPQHLTAVRLLAKICNAEVEGAEIGSTELTFKPGTIKGGDYRF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652     90 DIGTAGSISLVIQTLLPLSLGINKKFTVKIKGGTDVKRAPPIDYVKNVTLKILRNFGVLTELKVLKRGFYPEGGGEVIFE 169
Cdd:pfam01137  81 DIGTAGSITLVLQTLLPLLLFAKGPSTLTLRGGTNVPWAPSVDYLRTVFLPLLKRFGVDLELKILRRGFYPRGGGEVTLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    170 VKPSKIKKFDLIEHSKSNLVEGISYVQNLDESIARRMRKKAVDLLNKEKLLPNIKIE---------CSKGISTGAGIVLW 240
Cdd:pfam01137 161 VEPSSLKPIQLLERGKVKRIRGIAYVARLPPSIANRMVAAAAGLLLRFLPDVYIITDvekgeesgkGGGGGIVLVAETTE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    241 NDTLGGSCLGEKGLRAEIVAERAVNELLKERESGMALDKYMGDQIIPFLAFGKG--IVGVSEITNHTKTNMWVVKHFLDV 318
Cdd:pfam01137 241 GCILGASALGERGKPAEDVGEEAAEELLEELESGGCVDEHLQDQLILFMALAGGesVFRTGPLTLHTITNIRVIEQFLGV 320

                  ....
gi 2500652    319 DFEI 322
Cdd:pfam01137 321 KFKI 324
 
Name Accession Description Interval E-value
PRK04204 PRK04204
RNA 3'-terminal phosphate cyclase;
2-337 0e+00

RNA 3'-terminal phosphate cyclase;


Pssm-ID: 235255 [Multi-domain]  Cd Length: 343  Bit Score: 525.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652     2 DFIVIDGSYLEGGGQIIRTAVSLSALTQKPVKIINIRKKRKNKGLAPQHVSAVKAVKKLCNAEVFGLNVGSEELTFIPSK 81
Cdd:PRK04204   1 RMIEIDGSYGEGGGQILRTALALSAITGKPFRITNIRANRPNPGLLRQHLTAVKAAAEICNAEVEGAELGSQELVFIPGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    82 LSPKDFTIDIGTAGSISLVIQTLLPLSLGINKKFTVKIKGGTDVKRAPPIDYVKNVTLKILRNFGVLTELKVLKRGFYPE 161
Cdd:PRK04204  81 IRGGDYRFDIGTAGSITLVLQTVLPALLFADGPSRVTITGGTDVPWAPPIDYIRRVTLPLLRRMGIEAEIELLRRGFYPA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652   162 GGGEVIFEVKPSKIKKFDLIEHSKSNLVEGISYVQNLDESIARRMRKKAVDLLNKEKLLPNI---KIECSKGISTGAGIV 238
Cdd:PRK04204 161 GGGEVALEVEPSKLRPLELLERGELLRIRGISHVANLPEHVAERQAKAAAELLALSLGLIEIeinVEELSRGLGPGSGIV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652   239 LW----NDTLGGSCLGEKGLRAEIVAERAVNELLKERESGMALDKYMGDQIIPFLAF--GKGIVGVSEITNHTKTNMWVV 312
Cdd:PRK04204 241 LWaeseHITEGFDALGERGKPAEVVGEEAAEELLRYLASGAAVDEHLADQLILPMALagGEGSFTVAELTSHLLTNIWVV 320
                        330       340
                 ....*....|....*....|....*
gi 2500652   313 KHFLDVDFEIKEYkenncNGFTIEV 337
Cdd:PRK04204 321 EKFLPVKFEVEEY-----DGVVIKV 340
RNA_3prim_cycl TIGR03399
RNA 3'-phosphate cyclase; Members of this protein family are RNA 3'-phosphate cyclase (6.5.1.4) ...
4-321 2.84e-176

RNA 3'-phosphate cyclase; Members of this protein family are RNA 3'-phosphate cyclase (6.5.1.4), an enzyme whose function is conserved from E. coli to human. The modification this enzyme performs enables certain RNA ligations to occur, although the full biological roll for this enzyme is not fully described. This model separates this enzyme from a related protein, present only in eukaryotes, localized to the nucleolus, and involved in ribosomal modification. [Transcription, RNA processing]


Pssm-ID: 274563 [Multi-domain]  Cd Length: 326  Bit Score: 491.40  E-value: 2.84e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652      4 IVIDGSYLEGGGQIIRTAVSLSALTQKPVKIINIRKKRKNKGLAPQHVSAVKAVKKLCNAEVFGLNVGSEELTFIPSKLS 83
Cdd:TIGR03399   1 IEIDGSYGEGGGQILRTALSLSALTGKPVRIYNIRANRPKPGLAPQHLTAVKAAAEICNAEVEGAELGSTELEFIPGKIR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652     84 PKDFTIDIGTAGSISLVIQTLLPLSLGINKKFTVKIKGGTDVKRAPPIDYVKNVTLKILRNFGVLTELKVLKRGFYPEGG 163
Cdd:TIGR03399  81 GGDYRFDIGTAGSVTLVLQTLLPALLFANGPSRVTVSGGTDVPWAPPVDYLRNVFLPLLERMGIRAELELLRRGFYPRGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    164 GEVIFEVKP-SKIKKFDLIEHSKSNLVEGISYVQNLDESIARRMRKKAVDLLNKEKLLPNIKIEC-SKGISTGAGIVLWN 241
Cdd:TIGR03399 161 GEVRLRVEPvKKLKPLELEERGELLRVSGIAHAANLPAHVAERMAKAAREELRKLGLDPEIEIEVlDKGLGPGSGIVLWA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    242 DT----LGGSCLGEKGLRAEIVAERAVNELLKERESGMALDKYMGDQIIPFLAF--GKGIVGVSEITNHTKTNMWVVKHF 315
Cdd:TIGR03399 241 ETehcrLGFSALGEKGKSAEKVGEEAAEQLLAELRSGAAVDEHLADQLILYMALasGESRFTTSELTMHLRTNIWVIEQF 320

                  ....*.
gi 2500652    316 LDVDFE 321
Cdd:TIGR03399 321 LPVRFE 326
RCL1 COG0430
RNA 3'-terminal phosphate cyclase [RNA processing and modification];
4-337 3.02e-173

RNA 3'-terminal phosphate cyclase [RNA processing and modification];


Pssm-ID: 440199  Cd Length: 340  Bit Score: 484.24  E-value: 3.02e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    4 IVIDGSYLEGGGQIIRTAVSLSALTQKPVKIINIRKKRKNKGLAPQHVSAVKAVKKLCNAEVFGLNVGSEELTFIPSKLS 83
Cdd:COG0430   2 IEIDGSYGEGGGQILRTALALSALTGKPVRITNIRAGRPKPGLRPQHLTAVKAAAEICGAEVEGAELGSTELTFRPGPVR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652   84 PKDFTIDIGTAGSISLVIQTLLPLSLGINKKFTVKIKGGTDVKRAPPIDYVKNVTLKILRNFGVLTELKVLKRGFYPEGG 163
Cdd:COG0430  82 GGDYRFDIGTAGSTTLVLQTLLPALALADGPSRLTLTGGTHVPWSPPFDYLERVFLPLLRRMGAEAELELLRRGFYPAGG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652  164 GEVIFEVKPSK-IKKFDLIEHSKSNLVEGISYVQNLDESIARRMRKKAVDLLNKEKLLPNIKIECSKGISTGAGIVLW-- 240
Cdd:COG0430 162 GEVTLTVEPSAlLRPLDLLERGELLRVRGISLVANLPAHVAERQAEAARERLGEAGLEVEIEVEVRPALGPGSGIVLWae 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652  241 --NDTLGGSCLGEKGLRAEIVAERAVNELLKERESGMALDKYMGDQIIPFLAF--GKGIVGVSEITNHTKTNMWVVKHFL 316
Cdd:COG0430 242 yeHGTEGFDALGERGKPAERVGEEAAEELLEFLASGAAVDEHLADQLLLPLALagGEGRFTVSELTDHLLTNIWVIEQFL 321
                       330       340
                ....*....|....*....|.
gi 2500652  317 DVDFEIKEYKEnncNGFTIEV 337
Cdd:COG0430 322 GVRIEVEGEEG---GPGRVTV 339
RNA_Cyclase_Class_II cd00874
RNA 3' phosphate cyclase domain (class II). These proteins function as RNA cyclase to catalyze ...
6-324 1.09e-170

RNA 3' phosphate cyclase domain (class II). These proteins function as RNA cyclase to catalyze the ATP-dependent conversion of 3'-phosphate to a 2'.3'-cyclic phosphodiester at the end of RNA molecule. A conserved catalytic histidine residue is found in all members of this subfamily.


Pssm-ID: 238446 [Multi-domain]  Cd Length: 326  Bit Score: 477.10  E-value: 1.09e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    6 IDGSYLEGGGQIIRTAVSLSALTQKPVKIINIRKKRKNKGLAPQHVSAVKAVKKLCNAEVFGLNVGSEELTFIPSKLSPK 85
Cdd:cd00874   1 IDGSYGEGGGQILRTALALSAVTGKPVRIVNIRANRSNPGLSRQHLTAVRAAARICNAEVEGAELGSTELEFEPGKIKGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652   86 DFTIDIGTAGSISLVIQTLLPLSLGINKKFTVKIKGGTDVKRAPPIDYVKNVTLKILRNFGVLTELKVLKRGFYPEGGGE 165
Cdd:cd00874  81 DYEFDIGTAGSITLVLQTLLPALLFADGPSTVTISGGTDVPWAPPIDYLRNVTLPLLERMGIEAELEVLRRGFYPRGGGE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652  166 VIFEVKPSKIKKFDLIEHSKSNL-VEGISYVQNLDESIARRMRKKAVDLLNKE-KLLPNIKIECSKGISTGAGIVLWNDT 243
Cdd:cd00874 161 VVLTVEPSKLLPPLLLEERGEIEkIRGISHAANLPPHVAERQAEAAAALLRKAlGLQIEIEPEDQSALGPGSGIVLWAEY 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652  244 ----LGGSCLGEKGLRAEIVAERAVNELLKERESGMALDKYMGDQIIPFLAF-GKGIVGVSEITNHTKTNMWVVKHFLDV 318
Cdd:cd00874 241 ehsrLGFSALGKKGVPAEKVGEEAAEELLAYLSSGAAVDEHLADQLIPFMALaGGSEFRTGELTLHLQTNIWVIEKFLGV 320

                ....*.
gi 2500652  319 DFEIKE 324
Cdd:cd00874 321 KFRIEE 326
RTC pfam01137
RNA 3'-terminal phosphate cyclase; RNA cyclases are a family of RNA-modifying enzymes that are ...
10-322 3.57e-150

RNA 3'-terminal phosphate cyclase; RNA cyclases are a family of RNA-modifying enzymes that are conserved in all cellular organizms. They catalyze the ATP-dependent conversion of the 3'-phosphate to the 2',3'-cyclic phosphodiester at the end of RNA, in a reaction involving formation of the covalent AMP-cyclase intermediate. The structure of RTC demonstrates that RTCs are comprised two domain. The larger domain contains an insert domain of approximately 100 amino acids.


Pssm-ID: 460079 [Multi-domain]  Cd Length: 324  Bit Score: 425.00  E-value: 3.57e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652     10 YLEGGGQIIRTAVSLSALTQKPVKIINIRKKRKNKGLAPQHVSAVKAVKKLCNAEVFGLNVGSEELTFIPSKLSPKDFTI 89
Cdd:pfam01137   1 YGEGGGQILRTALALSALTGKPVRIENIRANRPKPGLRPQHLTAVRLLAKICNAEVEGAEIGSTELTFKPGTIKGGDYRF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652     90 DIGTAGSISLVIQTLLPLSLGINKKFTVKIKGGTDVKRAPPIDYVKNVTLKILRNFGVLTELKVLKRGFYPEGGGEVIFE 169
Cdd:pfam01137  81 DIGTAGSITLVLQTLLPLLLFAKGPSTLTLRGGTNVPWAPSVDYLRTVFLPLLKRFGVDLELKILRRGFYPRGGGEVTLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    170 VKPSKIKKFDLIEHSKSNLVEGISYVQNLDESIARRMRKKAVDLLNKEKLLPNIKIE---------CSKGISTGAGIVLW 240
Cdd:pfam01137 161 VEPSSLKPIQLLERGKVKRIRGIAYVARLPPSIANRMVAAAAGLLLRFLPDVYIITDvekgeesgkGGGGGIVLVAETTE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    241 NDTLGGSCLGEKGLRAEIVAERAVNELLKERESGMALDKYMGDQIIPFLAFGKG--IVGVSEITNHTKTNMWVVKHFLDV 318
Cdd:pfam01137 241 GCILGASALGERGKPAEDVGEEAAEELLEELESGGCVDEHLQDQLILFMALAGGesVFRTGPLTLHTITNIRVIEQFLGV 320

                  ....
gi 2500652    319 DFEI 322
Cdd:pfam01137 321 KFKI 324
RNA_Cyclase cd00295
RNA 3' phosphate cyclase domain - RNA phosphate cyclases are enzymes that catalyze the ...
6-324 5.88e-46

RNA 3' phosphate cyclase domain - RNA phosphate cyclases are enzymes that catalyze the ATP-dependent conversion of 3'-phosphate at the end of RNA into 2', 3'-cyclic phosphodiester bond. The enzymes are conserved in eucaryotes, bacteria and archaea. The exact biological role of this enzyme is unknown, but it has been proposed that it is likely to function in cellular RNA metabolism and processing. RNA phosphate cyclase has been characterized in human (with at least three isozymes), and E. coli, and it seems to be taxonomically widespread. The crystal structure of RNA phospate cyclase shows that it consists of two domains. The larger domain contains three repeats of a fold originally identified in the bacterial translation initiation factor IF3.


Pssm-ID: 238183 [Multi-domain]  Cd Length: 338  Bit Score: 159.44  E-value: 5.88e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    6 IDGSYLEGGGQIIRTAVSLSALTQKPVKIINIRKKRKNKGLAPQHVSAVKAVKKLCNAEVFGLNVGSEELTFIPSKLSPK 85
Cdd:cd00295   1 LDGAKGEGGCEILRHALSLAMISGQPFRIEGIRADEADPGLKDQHLSALKAAEEICGASVEEAELGGQRFIFRPGNIIGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652   86 DFTIDIGTAGSISLVIQTLLPLSLGINKKFTVKIKGGTDVKRAPPIDYVKNVTLKILRNFGVLTELKVLKRGFYPEGGGE 165
Cdd:cd00295  81 DVRFACGSAGGCGLFLEPILIACLFADGPSRLELSGGTDNNEAIGADFIRRSLEPLLAKIFIHGDELELRHGFRGAAGGG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652  166 VIFEVKP-SKIKKFDLIEHSKSNLV----EGISYVQNLDESIARRMRKKAVDLLNKEK----LLPNIKIECSKGISTGAG 236
Cdd:cd00295 161 GAEENFLcASFKELLLGERGSEFGRqfrgEGIAAGTRVPPAFAEREIASAAGSFNLFEpdifILPDDQRGDECGNGPGNS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652  237 IVLWNDTLGGSC-----LGEKGLRAEIVAERAVNELLKERESGMALDKYMGDQ-IIPFLAFGKG----IVGVSEITNHTK 306
Cdd:cd00295 241 ISLEAESEKGCSeaaehCGEAGESAEDVAAFCAKELKEVIASGAAVDEYLADQlLLGMALAGEAgefiVAGPLCHLLQLT 320
                       330
                ....*....|....*...
gi 2500652  307 TNMWVVKHFLDVDFEIKE 324
Cdd:cd00295 321 NFARDVEAFFNCEFRFIE 338
18S_RNA_Rcl1p TIGR03400
18S rRNA biogenesis protein RCL1; Members of this strictly eukaryotic protein family are not ...
24-335 1.44e-33

18S rRNA biogenesis protein RCL1; Members of this strictly eukaryotic protein family are not RNA 3'-phosphate cyclase (6.5.1.4), but rather a homolog with a distinct function, found in the nucleolus and required for ribosomal RNA processing. Homo sapiens has both a member of this RCL (RNA terminal phosphate cyclase like) family and EC 6.5.1.4, while Saccharomyces has a member of this family only.


Pssm-ID: 274564 [Multi-domain]  Cd Length: 360  Bit Score: 126.95  E-value: 1.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652     24 LSALTQKPVKIINIRKKRKNKGLAPQHVSAVKAVKKLCNAEVFGLNVGSEELTFIPSKLSPKDFTIDIGTAGSISLVIQT 103
Cdd:TIGR03400  15 LSTLSGKPVRITKIRSDDENPGLRDYEVSFLRLLEKVTNGSKIEISYTGTTVIYKPGLITGGSVTHECPTSRGIGYYLEP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    104 LLPLSLGINKKFTVKIKGGTDVKRAPPIDYVKNVTLKILRNFGVLT---ELKVLKRGFYPEGGGEVIFEVKPSK-IKKFD 179
Cdd:TIGR03400  95 LLLLAPFSKKPLSITLKGITNSTGDPSVDTIRTATLPLLKKFGIPDeglELKILKRGAPPLGGGEVELRCPVIKqLKTIH 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    180 LIEHSKSNLVEGISYVQNLDESIARRMRKKAVDLLNkeKLLPNIKI--ECSKGI----STGAGIVLWNDTLGGSCL---- 249
Cdd:TIGR03400 175 LTERGRVKRIRGVAYSTRVSPSLANRMIDAARGVLN--NLLPDVYIttDVWKGKnsgkSPGYGLSLVAETTNGCIIsaea 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    250 ----GEKGLrAEIVAERAVNELLKERESGMALDKYMGDQIIPFLAFGKGIVG---VSEITNHTKTNMWVVKHFLDVDFEI 322
Cdd:TIGR03400 253 vsspGEPSL-PEDLGKRAAYLLLEEIYKGGCVDSTHQPLALLLMALGQEDVSklrLGKLSEYTVEFLRDIKEFFGVTFKL 331
                         330
                  ....*....|...
gi 2500652    323 KEYKENNCNGFTI 335
Cdd:TIGR03400 332 KDDKSDNGSGKVL 344
RNA_Cyclase_Class_I cd00875
RNA 3' phosphate cyclase domain (class I) This subfamily of cyclase-like proteins are encoded ...
13-297 2.84e-27

RNA 3' phosphate cyclase domain (class I) This subfamily of cyclase-like proteins are encoded in eukaryotic genomes. They lack a conserved catalytic histidine residue required for cyclase activity, so probably do not function as cyclases. They are believed to play a role in ribosomal RNA processing and assembly.


Pssm-ID: 238447 [Multi-domain]  Cd Length: 341  Bit Score: 109.32  E-value: 2.84e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652   13 GGGQIIRTAVSLSALTQKPVKIINIRKKRKNKGLAPQHVSAVKAVKKLCNAEVFGLNVGSEELTFIPSKLSPKDFTIDIG 92
Cdd:cd00875   8 KGSNFFRQRLVLATLSGKPIIIKKIRSDDTNPGLRDHEVSFLRLLEKVTNGSVIEISYTGTTLIYKPGLITGGVLNHDCP 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652   93 TAGSISLVIQTLLPLSLGINKKFTVKIKGGTDVKRAPPIDYVKNVTLKILRNFGVLT---ELKVLKRGFYPEGGGEVIFE 169
Cdd:cd00875  88 VSRGIGYFLEPLLLLAPFGKKPLSITLKGITNSTGDPSVDSIRTATLPLLKKFGIPDeelELKILKRGVAPGGGGEVGFR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652  170 V---KPSKIKKFDLIEHSKSnlVEGISYVQNLDESIARRMRKKAVDLLNkeKLLPNIKIEC------SKGISTGAGIVLW 240
Cdd:cd00875 168 CpvrKPLTPHLNDSPGRIKR--IRGVAYSTRVSPSIANRMIDAARGVLN--PFIPDVYIYTdvrkgdNSGKSPGFGISLV 243
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2500652  241 NDTLGGSCL--------GEKGLRAEIVAERAVNELLKERESGMALDKYMGDQIIPFLAFGKGIVG 297
Cdd:cd00875 244 AETTTGVLYsaenvspaGGESEVPEDLGRECAYQLLEEISRGGCVDSYQQPLALLLMALGSEDVG 308
EPT_RTPC-like cd01553
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ...
6-184 1.71e-26

This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate cyclase family (RTPC). These 2 families differ in that EPT is formed by 3 repeats of an alpha-beta structural domain while RTPC has 3 similar repeats with a 4th slightly different domain inserted between the 2nd and 3rd repeat. They evidently share the same active site location, although the catalytic residues differ.


Pssm-ID: 238794  Cd Length: 211  Bit Score: 104.28  E-value: 1.71e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    6 IDGSYLEGGGQIIRTAVSLSALTQKPVKIINIRKKRKNKGLAPQHVSAVKAVKKLCNAEVFGLNVGSEELTFIPSKLSPK 85
Cdd:cd01553   1 LDGAGGKGGGQILRSFLVLAAISGGPITVTGIRPDRAKPGLLRQHLTFLKALEKICGATVEGGELGSDRISFRPGTVRGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652   86 DFTIDIGTAGSISLVIQTLLPLSLGINKKFTVKIKGGTDVKRAPPIDYVKNVTLKILRNFGVLTELKVLKRGFYPEGGGE 165
Cdd:cd01553  81 DVRFAIGSAGSCTDVLQTILPLLLFAKGPTRLTVTGGTDNPSAPPADFIRFVLEPELAKIGAHQEETLLRHGFYPAGGGV 160
                       170
                ....*....|....*....
gi 2500652  166 VIFEVKPSKIKKFDLIEHS 184
Cdd:cd01553 161 VATEVSPVEKLNTAQLRQL 179
RTC_insert pfam05189
RNA 3'-terminal phosphate cyclase (RTC), insert domain; RNA cyclases are a family of ...
189-270 1.58e-18

RNA 3'-terminal phosphate cyclase (RTC), insert domain; RNA cyclases are a family of RNA-modifying enzymes that are conserved in all cellular organizms. They catalyze the ATP-dependent conversion of the 3'-phosphate to the 2',3'-cyclic phosphodiester at the end of RNA, in a reaction involving formation of the covalent AMP-cyclase intermediate. The structure of RTC demonstrates that RTCs are comprised two domain. The larger domain contains an insert domain of approximately 100 amino acids.


Pssm-ID: 461577 [Multi-domain]  Cd Length: 102  Bit Score: 79.52  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2500652    189 VEGISYVQNLDESIARRMRKKAVDLLNKekLLPNIKIE-------CSKGISTGAGIVLWNDT-----LGGSCLGEKGLRA 256
Cdd:pfam05189   9 IRGVAYVAGLPPHVAERMAEAAREVLNK--LLPDVYIYidvvvegRDSGKGPGSGIVLVAETttgciLGADALGERGVPA 86
                          90
                  ....*....|....
gi 2500652    257 EIVAERAVNELLKE 270
Cdd:pfam05189  87 EDVGEEAAEELLEE 100
 
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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