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Conserved domains on  [gi|568928870|ref|XP_006503046|]
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terminal uridylyltransferase 4 isoform X11 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TUTase pfam19088
TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase ...
 274-491 2.75e-135

TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase enzymes. Terminal uridyltransferases (TUTases) execute 3' RNA uridylation across protists, fungi, metazoan and plant species.


:

Pssm-ID: 465974  Cd Length: 218  Bit Score: 406.44  E-value: 2.75e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870   274 EMDYLENATVIDESALTPEQRLGLKQAEERLERDHIFRLEKRSPEYTNCRYLCKLCLIHIENIQGAHKHIKEKRHKKNIL 353
Cdd:pfam19088    1 DQDEDEDGPVIDESNLTAEQQLGLRQAEERLKRDYIHRLKKRSPEYPNFQYLCKLCSVHIENIQGAHKHIKEKRHKKNIM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870   354 EKQEESELRSLPSPSSAHLAALSVAVVELAKEQGITDDDLRIRQDIVEEMSKVIMTFLPECSLRLYGSSLTKFALKSSDV 433
Cdd:pfam19088   81 EKQEENELRALPPPSPAQLKALGAAVLEVAQEHGISDEDFEVRQEIVTRMEKIIQQHLPDCSLRLYGSCLTRFAFKTSDI 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568928870   434 NIDIKFPPKMNHPDLLIQVLGILKKSALYIDVESDFHAKVPVVVCKDRKSALLCRVSA 491
Cdd:pfam19088  161 NIDVQFPSTMTQPDVLIQVLEILKNSESYSDVESDFHAKVPVVFCRDKQSGLMCKVSA 218
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
 648-697 6.15e-13

Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown to have polynucleotide adenylyltransferase activity. Proteins in this family have been located to both the nucleus and the cytoplasm.


:

Pssm-ID: 427532  Cd Length: 60  Bit Score: 64.52  E-value: 6.15e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568928870   648 PLGQLWLELLKFYTLDFALEEYVICVRIQDILTRENKNWPKR------RIAIEDPF 697
Cdd:pfam03828    1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEKGWLRNegrrpfLLCIEDPF 56
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 988-1038 4.79e-11

Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.


:

Pssm-ID: 143392 [Multi-domain]  Cd Length: 114  Bit Score: 60.65  E-value: 4.79e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568928870  988 NREQILIGLEKFIQKEYdEKARLCLFGSSKNGFGFRDSDLDICMTLEGHEN 1038
Cdd:cd05402     1 KREEVLDRLQELIKEWF-PGAKLYPFGSYVTGLGLPGSDIDLCLLGPNHRV 50
rad2 super family cl36701
DNA excision repair protein (rad2); All proteins in this family for which functions are known ...
 2-366 1.43e-03

DNA excision repair protein (rad2); All proteins in this family for which functions are known are flap endonucleases that generate the 3' incision next to DNA damage as part of nucleotide excision repair. This family is related to many other flap endonuclease families including the fen1 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


The actual alignment was detected with superfamily member TIGR00600:

Pssm-ID: 273166 [Multi-domain]  Cd Length: 1034  Bit Score: 42.58  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870     2 EEPKTSKNENHEPKKNIICEESKAVKIIS----NQTLKPRNDKSEIGTSSLNRNSSKKTK----------------QNDI 61
Cdd:TIGR00600  367 DSDESEWERQELKRNNVAFVDDGSLSPRTlqaiGQALDDDEDKKVSASSDDQASPSKKTKmllisrievedddldyLDQG 446

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870    62 CIEKTEAKSCKVNAASVPGPKDLGLVHRDQSHCKMKKLPNSPMKAQKGSSQTKLEKTPS--LQTKAEKVPKSPNLPVKAE 139
Cdd:TIGR00600  447 EGIPLMAALQLSSVNSKPEAVASTKIAREVTSSGHEAVPKAVQSLLLGATNDSPIPSEFtiLDRKSELSIERTVKPVSSE 526

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870   140 KAPCTTAEAT----TEKALNSQRKEENTPTSqmkLQKTPRSPLEPENVPSLLLKEnvKQTESQQTGKKLTSSFVSMDkrk 215
Cdd:TIGR00600  527 FGLPSQREDKlaipTEGTQNLQGISDHPEQF---EFQNELSPLETKNNESNLSSD--AETEGSPNPEMPSWSSVTVP--- 598

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870   216 SEALQG-EKSALENSSLSQKQQ---TQTDNIADSDDSASGIEDTADDLSKMKSEESNKENSS-EMDYL---ENATVIDES 287
Cdd:TIGR00600  599 SEALDNyETTNPSNAKEVRNFAetgIQTTNVGESADLLLISNPMEVEPMESEKEESESDGSFiEVDSVsstLELQVPSKS 678

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870   288 ALTPEQRLGLKQAEERLERDH---IFRLEKRSPEytncrylcklclihIENIQGAHKHIKEKRHKKNILEKQEESELRSL 364
Cdd:TIGR00600  679 QPTDESEENAENKVASIEGEHrkeIEDLLFDESE--------------EDNIVGMIEEEKDADDFKNEWQDISLEELEAL 744


                   ..
gi 568928870   365 PS 366
Cdd:TIGR00600  745 EA 746
 
Name Accession Description Interval E-value
TUTase pfam19088
TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase ...
 274-491 2.75e-135

TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase enzymes. Terminal uridyltransferases (TUTases) execute 3' RNA uridylation across protists, fungi, metazoan and plant species.


Pssm-ID: 465974  Cd Length: 218  Bit Score: 406.44  E-value: 2.75e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870   274 EMDYLENATVIDESALTPEQRLGLKQAEERLERDHIFRLEKRSPEYTNCRYLCKLCLIHIENIQGAHKHIKEKRHKKNIL 353
Cdd:pfam19088    1 DQDEDEDGPVIDESNLTAEQQLGLRQAEERLKRDYIHRLKKRSPEYPNFQYLCKLCSVHIENIQGAHKHIKEKRHKKNIM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870   354 EKQEESELRSLPSPSSAHLAALSVAVVELAKEQGITDDDLRIRQDIVEEMSKVIMTFLPECSLRLYGSSLTKFALKSSDV 433
Cdd:pfam19088   81 EKQEENELRALPPPSPAQLKALGAAVLEVAQEHGISDEDFEVRQEIVTRMEKIIQQHLPDCSLRLYGSCLTRFAFKTSDI 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568928870   434 NIDIKFPPKMNHPDLLIQVLGILKKSALYIDVESDFHAKVPVVVCKDRKSALLCRVSA 491
Cdd:pfam19088  161 NIDVQFPSTMTQPDVLIQVLEILKNSESYSDVESDFHAKVPVVFCRDKQSGLMCKVSA 218
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 395-507 1.45e-29

Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.


Pssm-ID: 143392 [Multi-domain]  Cd Length: 114  Bit Score: 113.81  E-value: 1.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870  395 IRQDIVEEMSKVIMTFLPECSLRLYGSSLTKFALKSSDVNIDIKFPP-KMNHPDLLIQVLGILKKSALYIDVESDFHAKV 473
Cdd:cd05402     1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGPNhRVDREDFLRKLAKLLKKSGEVVEVEPIINARV 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 568928870  474 PVVVCKDRKSALLCRVSAGNDMACLTTDLLAALG 507
Cdd:cd05402    81 PIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
341-558 3.20e-24

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 107.55  E-value: 3.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870  341 KHIKEKRHKKNILEKQEEselRSLPSPSSAHLAALSVAVVELAKEQGITDDDLRIRQDIVEEMSKVIMTFLPECSLRLYG 420
Cdd:COG5260    26 KERRPLDAKKVSIQELLE---LSIDSVFNEESDELTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVFG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870  421 SSLTKFALKSSDVNIDIKFPPKMNHPDLLIQVLGI-LKKSALYIDVESDFHAKVPVVVCKDRKSALLCRVSAGNDMACLT 499
Cdd:COG5260   103 STETGLALPKSDIDLCIISDPRGYKETRNAGSLAShLFKKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVN 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568928870  500 TDLLAALGKVEPVFTPLVLAFRYWAKLCYIDSQTDGGIPSYCFALMVMFFLQQRKPPLL 558
Cdd:COG5260   183 AKLIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPFLF 241
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
 648-697 6.15e-13

Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown to have polynucleotide adenylyltransferase activity. Proteins in this family have been located to both the nucleus and the cytoplasm.


Pssm-ID: 427532  Cd Length: 60  Bit Score: 64.52  E-value: 6.15e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568928870   648 PLGQLWLELLKFYTLDFALEEYVICVRIQDILTRENKNWPKR------RIAIEDPF 697
Cdd:pfam03828    1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEKGWLRNegrrpfLLCIEDPF 56
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 988-1038 4.79e-11

Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.


Pssm-ID: 143392 [Multi-domain]  Cd Length: 114  Bit Score: 60.65  E-value: 4.79e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568928870  988 NREQILIGLEKFIQKEYdEKARLCLFGSSKNGFGFRDSDLDICMTLEGHEN 1038
Cdd:cd05402     1 KREEVLDRLQELIKEWF-PGAKLYPFGSYVTGLGLPGSDIDLCLLGPNHRV 50
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 996-1041 1.73e-04

Nucleotidyltransferase domain; Members of this family belong to a large family of nucleotidyltransferases. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTase in-activates antibiotics by catalysing the addition of a nucleotidyl group onto the drug.


Pssm-ID: 396474  Cd Length: 91  Bit Score: 41.25  E-value: 1.73e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568928870   996 LEKFIQ--KEYDEKARLCLFGSSKNGFGFRDSDLDICMTLEGHENAEI 1041
Cdd:pfam01909    1 LRKLREilKELFPVAEVVLFGSYARGTALPGSDIDLLVVFPEPVEEER 48
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
946-1040 2.03e-04

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 45.15  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870  946 PEDFRKIDLKPLPP--MTNRFREILDLVCKRC---FDELSPPCSEQHNREQILIGLEKFIQKEYDEkARLCLFGSSKNGF 1020
Cdd:COG5260    30 PLDAKKVSIQELLElsIDSVFNEESDELTSELlefYDYIAPSDEELKRRKALLEKLRTLLKKEFPD-ADLKVFGSTETGL 108

                          90       100
                  ....*....|....*....|
gi 568928870 1021 GFRDSDLDICMTLEGHENAE 1040
Cdd:COG5260   109 ALPKSDIDLCIISDPRGYKE 128
rad2 TIGR00600
DNA excision repair protein (rad2); All proteins in this family for which functions are known ...
 2-366 1.43e-03

DNA excision repair protein (rad2); All proteins in this family for which functions are known are flap endonucleases that generate the 3' incision next to DNA damage as part of nucleotide excision repair. This family is related to many other flap endonuclease families including the fen1 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273166 [Multi-domain]  Cd Length: 1034  Bit Score: 42.58  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870     2 EEPKTSKNENHEPKKNIICEESKAVKIIS----NQTLKPRNDKSEIGTSSLNRNSSKKTK----------------QNDI 61
Cdd:TIGR00600  367 DSDESEWERQELKRNNVAFVDDGSLSPRTlqaiGQALDDDEDKKVSASSDDQASPSKKTKmllisrievedddldyLDQG 446

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870    62 CIEKTEAKSCKVNAASVPGPKDLGLVHRDQSHCKMKKLPNSPMKAQKGSSQTKLEKTPS--LQTKAEKVPKSPNLPVKAE 139
Cdd:TIGR00600  447 EGIPLMAALQLSSVNSKPEAVASTKIAREVTSSGHEAVPKAVQSLLLGATNDSPIPSEFtiLDRKSELSIERTVKPVSSE 526

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870   140 KAPCTTAEAT----TEKALNSQRKEENTPTSqmkLQKTPRSPLEPENVPSLLLKEnvKQTESQQTGKKLTSSFVSMDkrk 215
Cdd:TIGR00600  527 FGLPSQREDKlaipTEGTQNLQGISDHPEQF---EFQNELSPLETKNNESNLSSD--AETEGSPNPEMPSWSSVTVP--- 598

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870   216 SEALQG-EKSALENSSLSQKQQ---TQTDNIADSDDSASGIEDTADDLSKMKSEESNKENSS-EMDYL---ENATVIDES 287
Cdd:TIGR00600  599 SEALDNyETTNPSNAKEVRNFAetgIQTTNVGESADLLLISNPMEVEPMESEKEESESDGSFiEVDSVsstLELQVPSKS 678

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870   288 ALTPEQRLGLKQAEERLERDH---IFRLEKRSPEytncrylcklclihIENIQGAHKHIKEKRHKKNILEKQEESELRSL 364
Cdd:TIGR00600  679 QPTDESEENAENKVASIEGEHrkeIEDLLFDESE--------------EDNIVGMIEEEKDADDFKNEWQDISLEELEAL 744


                   ..
gi 568928870   365 PS 366
Cdd:TIGR00600  745 EA 746
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
101-207 2.16e-03

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 41.57  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870   101 NSPMKAQKGSSQTKLEKTPSLQTKAEKVPKSPnlPVKAEKAPCTTAEATTEKALNSQRKEENTPTSQMKLQ-KTPRSPLE 179
Cdd:pfam05539  199 PATQGHQTATANQRLSSTEPVGTQGTTTSSNP--EPQTEPPPSQRGPSGSPQHPPSTTSQDQSTTGDGQEHtQRRKTPPA 276

                           90       100
                   ....*....|....*....|....*...
gi 568928870   180 PENVPSLLLKENVKQTESQQTGKKLTSS 207
Cdd:pfam05539  277 TSNRRSPHSTATPPPTTKRQETGRPTPR 304
 
Name Accession Description Interval E-value
TUTase pfam19088
TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase ...
 274-491 2.75e-135

TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase enzymes. Terminal uridyltransferases (TUTases) execute 3' RNA uridylation across protists, fungi, metazoan and plant species.


Pssm-ID: 465974  Cd Length: 218  Bit Score: 406.44  E-value: 2.75e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870   274 EMDYLENATVIDESALTPEQRLGLKQAEERLERDHIFRLEKRSPEYTNCRYLCKLCLIHIENIQGAHKHIKEKRHKKNIL 353
Cdd:pfam19088    1 DQDEDEDGPVIDESNLTAEQQLGLRQAEERLKRDYIHRLKKRSPEYPNFQYLCKLCSVHIENIQGAHKHIKEKRHKKNIM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870   354 EKQEESELRSLPSPSSAHLAALSVAVVELAKEQGITDDDLRIRQDIVEEMSKVIMTFLPECSLRLYGSSLTKFALKSSDV 433
Cdd:pfam19088   81 EKQEENELRALPPPSPAQLKALGAAVLEVAQEHGISDEDFEVRQEIVTRMEKIIQQHLPDCSLRLYGSCLTRFAFKTSDI 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568928870   434 NIDIKFPPKMNHPDLLIQVLGILKKSALYIDVESDFHAKVPVVVCKDRKSALLCRVSA 491
Cdd:pfam19088  161 NIDVQFPSTMTQPDVLIQVLEILKNSESYSDVESDFHAKVPVVFCRDKQSGLMCKVSA 218
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 395-507 1.45e-29

Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.


Pssm-ID: 143392 [Multi-domain]  Cd Length: 114  Bit Score: 113.81  E-value: 1.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870  395 IRQDIVEEMSKVIMTFLPECSLRLYGSSLTKFALKSSDVNIDIKFPP-KMNHPDLLIQVLGILKKSALYIDVESDFHAKV 473
Cdd:cd05402     1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGPNhRVDREDFLRKLAKLLKKSGEVVEVEPIINARV 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 568928870  474 PVVVCKDRKSALLCRVSAGNDMACLTTDLLAALG 507
Cdd:cd05402    81 PIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
341-558 3.20e-24

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 107.55  E-value: 3.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870  341 KHIKEKRHKKNILEKQEEselRSLPSPSSAHLAALSVAVVELAKEQGITDDDLRIRQDIVEEMSKVIMTFLPECSLRLYG 420
Cdd:COG5260    26 KERRPLDAKKVSIQELLE---LSIDSVFNEESDELTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVFG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870  421 SSLTKFALKSSDVNIDIKFPPKMNHPDLLIQVLGI-LKKSALYIDVESDFHAKVPVVVCKDRKSALLCRVSAGNDMACLT 499
Cdd:COG5260   103 STETGLALPKSDIDLCIISDPRGYKETRNAGSLAShLFKKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVN 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568928870  500 TDLLAALGKVEPVFTPLVLAFRYWAKLCYIDSQTDGGIPSYCFALMVMFFLQQRKPPLL 558
Cdd:COG5260   183 AKLIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPFLF 241
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
 648-697 6.15e-13

Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown to have polynucleotide adenylyltransferase activity. Proteins in this family have been located to both the nucleus and the cytoplasm.


Pssm-ID: 427532  Cd Length: 60  Bit Score: 64.52  E-value: 6.15e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568928870   648 PLGQLWLELLKFYTLDFALEEYVICVRIQDILTRENKNWPKR------RIAIEDPF 697
Cdd:pfam03828    1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEKGWLRNegrrpfLLCIEDPF 56
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 988-1038 4.79e-11

Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.


Pssm-ID: 143392 [Multi-domain]  Cd Length: 114  Bit Score: 60.65  E-value: 4.79e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568928870  988 NREQILIGLEKFIQKEYdEKARLCLFGSSKNGFGFRDSDLDICMTLEGHEN 1038
Cdd:cd05402     1 KREEVLDRLQELIKEWF-PGAKLYPFGSYVTGLGLPGSDIDLCLLGPNHRV 50
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 996-1041 1.73e-04

Nucleotidyltransferase domain; Members of this family belong to a large family of nucleotidyltransferases. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTase in-activates antibiotics by catalysing the addition of a nucleotidyl group onto the drug.


Pssm-ID: 396474  Cd Length: 91  Bit Score: 41.25  E-value: 1.73e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568928870   996 LEKFIQ--KEYDEKARLCLFGSSKNGFGFRDSDLDICMTLEGHENAEI 1041
Cdd:pfam01909    1 LRKLREilKELFPVAEVVLFGSYARGTALPGSDIDLLVVFPEPVEEER 48
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
946-1040 2.03e-04

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 45.15  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870  946 PEDFRKIDLKPLPP--MTNRFREILDLVCKRC---FDELSPPCSEQHNREQILIGLEKFIQKEYDEkARLCLFGSSKNGF 1020
Cdd:COG5260    30 PLDAKKVSIQELLElsIDSVFNEESDELTSELlefYDYIAPSDEELKRRKALLEKLRTLLKKEFPD-ADLKVFGSTETGL 108

                          90       100
                  ....*....|....*....|
gi 568928870 1021 GFRDSDLDICMTLEGHENAE 1040
Cdd:COG5260   109 ALPKSDIDLCIISDPRGYKE 128
rad2 TIGR00600
DNA excision repair protein (rad2); All proteins in this family for which functions are known ...
 2-366 1.43e-03

DNA excision repair protein (rad2); All proteins in this family for which functions are known are flap endonucleases that generate the 3' incision next to DNA damage as part of nucleotide excision repair. This family is related to many other flap endonuclease families including the fen1 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273166 [Multi-domain]  Cd Length: 1034  Bit Score: 42.58  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870     2 EEPKTSKNENHEPKKNIICEESKAVKIIS----NQTLKPRNDKSEIGTSSLNRNSSKKTK----------------QNDI 61
Cdd:TIGR00600  367 DSDESEWERQELKRNNVAFVDDGSLSPRTlqaiGQALDDDEDKKVSASSDDQASPSKKTKmllisrievedddldyLDQG 446

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870    62 CIEKTEAKSCKVNAASVPGPKDLGLVHRDQSHCKMKKLPNSPMKAQKGSSQTKLEKTPS--LQTKAEKVPKSPNLPVKAE 139
Cdd:TIGR00600  447 EGIPLMAALQLSSVNSKPEAVASTKIAREVTSSGHEAVPKAVQSLLLGATNDSPIPSEFtiLDRKSELSIERTVKPVSSE 526

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870   140 KAPCTTAEAT----TEKALNSQRKEENTPTSqmkLQKTPRSPLEPENVPSLLLKEnvKQTESQQTGKKLTSSFVSMDkrk 215
Cdd:TIGR00600  527 FGLPSQREDKlaipTEGTQNLQGISDHPEQF---EFQNELSPLETKNNESNLSSD--AETEGSPNPEMPSWSSVTVP--- 598

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870   216 SEALQG-EKSALENSSLSQKQQ---TQTDNIADSDDSASGIEDTADDLSKMKSEESNKENSS-EMDYL---ENATVIDES 287
Cdd:TIGR00600  599 SEALDNyETTNPSNAKEVRNFAetgIQTTNVGESADLLLISNPMEVEPMESEKEESESDGSFiEVDSVsstLELQVPSKS 678

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870   288 ALTPEQRLGLKQAEERLERDH---IFRLEKRSPEytncrylcklclihIENIQGAHKHIKEKRHKKNILEKQEESELRSL 364
Cdd:TIGR00600  679 QPTDESEENAENKVASIEGEHrkeIEDLLFDESE--------------EDNIVGMIEEEKDADDFKNEWQDISLEELEAL 744


                   ..
gi 568928870   365 PS 366
Cdd:TIGR00600  745 EA 746
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
101-207 2.16e-03

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 41.57  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928870   101 NSPMKAQKGSSQTKLEKTPSLQTKAEKVPKSPnlPVKAEKAPCTTAEATTEKALNSQRKEENTPTSQMKLQ-KTPRSPLE 179
Cdd:pfam05539  199 PATQGHQTATANQRLSSTEPVGTQGTTTSSNP--EPQTEPPPSQRGPSGSPQHPPSTTSQDQSTTGDGQEHtQRRKTPPA 276

                           90       100
                   ....*....|....*....|....*...
gi 568928870   180 PENVPSLLLKENVKQTESQQTGKKLTSS 207
Cdd:pfam05539  277 TSNRRSPHSTATPPPTTKRQETGRPTPR 304
 
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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