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Conserved domains on  [gi|58331272|ref|NP_078893|]
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terminal uridylyltransferase 7 isoform 1 [Homo sapiens]

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 ...
 194-411 1.33e-120

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: 376.01  E-value: 1.33e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272    194 EQDGDLEGPVIDESVLSTKELLGLQQAEERLKRDCIDRLKRRPRNYPTAKYTCRLCDVLIESIAFAHKHIKEKRHKKNIK 273
Cdd:pfam19088    1 DQDEDEDGPVIDESNLTAEQQLGLRQAEERLKRDYIHRLKKRSPEYPNFQYLCKLCSVHIENIQGAHKHIKEKRHKKNIM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272    274 EKQEEELLTTLPPPTPSQINAVGIAIDKVVQEFGLHNENLEQRLEIKRIMENVFQHKLPDCSLRLYGSSCSRLGFKNSDV 353
Cdd:pfam19088   81 EKQEENELRALPPPSPAQLKALGAAVLEVAQEHGISDEDFEVRQEIVTRMEKIIQQHLPDCSLRLYGSCLTRFAFKTSDI 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 58331272    354 NIDIQFPAIMSQPDVLLLVQECLKNSDSFIDVDADFHARVPVVVCREKQSGLLCKVSA 411
Cdd:pfam19088  161 NIDVQFPSTMTQPDVLIQVLEILKNSESYSDVESDFHAKVPVVFCRDKQSGLMCKVSA 218
TUTF7_u4 pfam16631
Unstructured region 4 on terminal uridylyltransferase 7; TUTF7_u4 is the fourth natively ...
 1371-1450 1.88e-43

Unstructured region 4 on terminal uridylyltransferase 7; TUTF7_u4 is the fourth natively unstructured region found on a set of higher eukaryote Terminal uridylyltransferase 7 proteins. The function is not known. The region is rich in arginine and lysine.


:

Pssm-ID: 465208  Cd Length: 88  Bit Score: 152.70  E-value: 1.88e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272   1371 DQEDALNQRYPENKEKRSKEDKEIHNKYTEREVSTKEDKPIQCTPQKAKPMRAAADLGREKILRPPVEKWKRQDDKDLRE 1450
Cdd:pfam16631    9 DQEDTKNQRYPENKEKRSKEDKEIQNKYTEKEVSVKEGKLHPCTPQKAKPARAVVDTGREKSLRQSAEKWKRQDDRDLRE 88
TRF4 super family cl34961
DNA polymerase sigma [Replication, recombination and repair];
979-1310 8.21e-38

DNA polymerase sigma [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG5260:

Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 149.54  E-value: 8.21e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272  979 PEDFKRIQLEPLPPLTPK-----FLNILDQVCIQCYKDFSPTIIEDQAREHIRQNLESFIRQDFPGTKLSLFGSSKNGFG 1053
Cdd:COG5260   30 PLDAKKVSIQELLELSIDsvfneESDELTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVFGSTETGLA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272 1054 FKQSDLDVCMTINGLEtaeGLDCVRTIEELARVLRKHSGLRNILpITTAKVPIVKFFHLRSGLEVDISLYNTLALHNTRL 1133
Cdd:COG5260  110 LPKSDIDLCIISDPRG---YKETRNAGSLASHLFKKNLAKEVVV-VSTARVPIIKLVDPQSGLHCDISFNNTNGIVNAKL 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272 1134 LSAYSAIDPRVKYLCYTMKVFTKMCDIGDASRGSLSSYAYTLMVLYFLQQRNPPviPVLQEIYKGEKKPEIFVDGWNIYF 1213
Cdd:COG5260  186 IRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPF--LFFDNGLLSPLKYNKNIDNLGVLF 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272 1214 FDqidelptywsecgkntesvgqlwlgLLRFYTEEFDFKEHVISIRR-KSLLTTFKKQW----TSKYIVIEDPF-DLNHN 1287
Cdd:COG5260  264 DD-------------------------FFELYGKSFNYSLVVLSINSgDFYLPKYEKGWlkpsKPNSLSIQDPGtDRNND 318

                        330       340
                 ....*....|....*....|...
gi 58331272 1288 LGAGlSRKMtNFIMKAFINGRRV 1310
Cdd:COG5260  319 ISAV-SFNI-KDIKAAFIRAFEL 339
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
 550-599 2.36e-11

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: 60.28  E-value: 2.36e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 58331272    550 PVGQLWVELLRFYALEFNLADLVISIRVKELVSRELKDWPK------KRIAIEDPY 599
Cdd:pfam03828    1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEKGWLRnegrrpFLLCIEDPF 56
ZnF_C2HC smart00343
zinc finger;
1452-1468 2.49e-03

zinc finger;


:

Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 36.65  E-value: 2.49e-03
                            10
                    ....*....|....*..
gi 58331272    1452 RCFICGREGHIKKECPQ 1468
Cdd:smart00343    1 KCYNCGKEGHIARDCPS 17
ZnF_C2HC smart00343
zinc finger;
1346-1361 6.07e-03

zinc finger;


:

Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 35.50  E-value: 6.07e-03
                            10
                    ....*....|....*.
gi 58331272    1346 CCRICGKIGHFMKDCP 1361
Cdd:smart00343    1 KCYNCGKEGHIARDCP 16
 
Name Accession Description Interval E-value
TUTase pfam19088
TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase ...
 194-411 1.33e-120

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: 376.01  E-value: 1.33e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272    194 EQDGDLEGPVIDESVLSTKELLGLQQAEERLKRDCIDRLKRRPRNYPTAKYTCRLCDVLIESIAFAHKHIKEKRHKKNIK 273
Cdd:pfam19088    1 DQDEDEDGPVIDESNLTAEQQLGLRQAEERLKRDYIHRLKKRSPEYPNFQYLCKLCSVHIENIQGAHKHIKEKRHKKNIM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272    274 EKQEEELLTTLPPPTPSQINAVGIAIDKVVQEFGLHNENLEQRLEIKRIMENVFQHKLPDCSLRLYGSSCSRLGFKNSDV 353
Cdd:pfam19088   81 EKQEENELRALPPPSPAQLKALGAAVLEVAQEHGISDEDFEVRQEIVTRMEKIIQQHLPDCSLRLYGSCLTRFAFKTSDI 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 58331272    354 NIDIQFPAIMSQPDVLLLVQECLKNSDSFIDVDADFHARVPVVVCREKQSGLLCKVSA 411
Cdd:pfam19088  161 NIDVQFPSTMTQPDVLIQVLEILKNSESYSDVESDFHAKVPVVFCRDKQSGLMCKVSA 218
TUTF7_u4 pfam16631
Unstructured region 4 on terminal uridylyltransferase 7; TUTF7_u4 is the fourth natively ...
 1371-1450 1.88e-43

Unstructured region 4 on terminal uridylyltransferase 7; TUTF7_u4 is the fourth natively unstructured region found on a set of higher eukaryote Terminal uridylyltransferase 7 proteins. The function is not known. The region is rich in arginine and lysine.


Pssm-ID: 465208  Cd Length: 88  Bit Score: 152.70  E-value: 1.88e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272   1371 DQEDALNQRYPENKEKRSKEDKEIHNKYTEREVSTKEDKPIQCTPQKAKPMRAAADLGREKILRPPVEKWKRQDDKDLRE 1450
Cdd:pfam16631    9 DQEDTKNQRYPENKEKRSKEDKEIQNKYTEKEVSVKEGKLHPCTPQKAKPARAVVDTGREKSLRQSAEKWKRQDDRDLRE 88
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
979-1310 8.21e-38

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 149.54  E-value: 8.21e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272  979 PEDFKRIQLEPLPPLTPK-----FLNILDQVCIQCYKDFSPTIIEDQAREHIRQNLESFIRQDFPGTKLSLFGSSKNGFG 1053
Cdd:COG5260   30 PLDAKKVSIQELLELSIDsvfneESDELTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVFGSTETGLA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272 1054 FKQSDLDVCMTINGLEtaeGLDCVRTIEELARVLRKHSGLRNILpITTAKVPIVKFFHLRSGLEVDISLYNTLALHNTRL 1133
Cdd:COG5260  110 LPKSDIDLCIISDPRG---YKETRNAGSLASHLFKKNLAKEVVV-VSTARVPIIKLVDPQSGLHCDISFNNTNGIVNAKL 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272 1134 LSAYSAIDPRVKYLCYTMKVFTKMCDIGDASRGSLSSYAYTLMVLYFLQQRNPPviPVLQEIYKGEKKPEIFVDGWNIYF 1213
Cdd:COG5260  186 IRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPF--LFFDNGLLSPLKYNKNIDNLGVLF 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272 1214 FDqidelptywsecgkntesvgqlwlgLLRFYTEEFDFKEHVISIRR-KSLLTTFKKQW----TSKYIVIEDPF-DLNHN 1287
Cdd:COG5260  264 DD-------------------------FFELYGKSFNYSLVVLSINSgDFYLPKYEKGWlkpsKPNSLSIQDPGtDRNND 318

                        330       340
                 ....*....|....*....|...
gi 58331272 1288 LGAGlSRKMtNFIMKAFINGRRV 1310
Cdd:COG5260  319 ISAV-SFNI-KDIKAAFIRAFEL 339
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 1021-1138 5.29e-37

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: 135.38  E-value: 5.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272 1021 AREHIRQNLESFIRQDFPGTKLSLFGSSKNGFGFKQSDLDVCMTINGletaEGLDCVRTIEELARVLRKHSGLRNILPIT 1100
Cdd:cd05402    1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGPN----HRVDREDFLRKLAKLLKKSGEVVEVEPII 76

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 58331272 1101 TAKVPIVKFFHLRSGLEVDISLYNTLALHNTRLLSAYS 1138
Cdd:cd05402   77 NARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 315-427 8.82e-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: 111.88  E-value: 8.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272  315 QRLEIKRIMENVFQHKLPDCSLRLYGSSCSRLGFKNSDVNIDIQFPA-IMSQPDVLLLVQECLKNSDSFIDVDADFHARV 393
Cdd:cd05402    1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGPNhRVDREDFLRKLAKLLKKSGEVVEVEPIINARV 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 58331272  394 PVVVCREKQSGLLCKVSAGNENACLTTKHLTALG 427
Cdd:cd05402   81 PIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
301-478 1.38e-17

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 87.91  E-value: 1.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272  301 KVVQEFGLHNENLEQRLEIKRIMENVFQHKLPDCSLRLYGSSCSRLGFKNSDVNIDIQFPAIMSQPDV-LLLVQECLKNS 379
Cdd:COG5260   63 EFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVFGSTETGLALPKSDIDLCIISDPRGYKETRnAGSLASHLFKK 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272  380 DSFIDVDADFHARVPVVVCREKQSGLLCKVSAGNENACLTTKHLTALGKLEPKLVPLVIAFRYWAKLCSIDRPEEGGLPP 459
Cdd:COG5260  143 NLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVNAKLIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSS 222

                        170
                 ....*....|....*....
gi 58331272  460 YVFALMAIFFLQQRKEPLL 478
Cdd:COG5260  223 YTISCMVLSFLQMHPPFLF 241
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
 1233-1286 5.81e-15

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: 70.68  E-value: 5.81e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272   1233 SVGQLWLGLLRFYTEEFDFKEHVISIRRKSLLTTFKKQWT------SKYIVIEDPFDLNH 1286
Cdd:pfam03828    1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEKGWLrnegrrPFLLCIEDPFDLDN 60
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
 550-599 2.36e-11

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: 60.28  E-value: 2.36e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 58331272    550 PVGQLWVELLRFYALEFNLADLVISIRVKELVSRELKDWPK------KRIAIEDPY 599
Cdd:pfam03828    1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEKGWLRnegrrpFLLCIEDPF 56
ZnF_C2HC smart00343
zinc finger;
1452-1468 2.49e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 36.65  E-value: 2.49e-03
                            10
                    ....*....|....*..
gi 58331272    1452 RCFICGREGHIKKECPQ 1468
Cdd:smart00343    1 KCYNCGKEGHIARDCPS 17
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
 1451-1468 3.50e-03

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 36.35  E-value: 3.50e-03
                           10
                   ....*....|....*...
gi 58331272   1451 KRCFICGREGHIKKECPQ 1468
Cdd:pfam00098    1 GKCYNCGEPGHIARDCPK 18
ZnF_C2HC smart00343
zinc finger;
1346-1361 6.07e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 35.50  E-value: 6.07e-03
                            10
                    ....*....|....*.
gi 58331272    1346 CCRICGKIGHFMKDCP 1361
Cdd:smart00343    1 KCYNCGKEGHIARDCP 16
 
Name Accession Description Interval E-value
TUTase pfam19088
TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase ...
 194-411 1.33e-120

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: 376.01  E-value: 1.33e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272    194 EQDGDLEGPVIDESVLSTKELLGLQQAEERLKRDCIDRLKRRPRNYPTAKYTCRLCDVLIESIAFAHKHIKEKRHKKNIK 273
Cdd:pfam19088    1 DQDEDEDGPVIDESNLTAEQQLGLRQAEERLKRDYIHRLKKRSPEYPNFQYLCKLCSVHIENIQGAHKHIKEKRHKKNIM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272    274 EKQEEELLTTLPPPTPSQINAVGIAIDKVVQEFGLHNENLEQRLEIKRIMENVFQHKLPDCSLRLYGSSCSRLGFKNSDV 353
Cdd:pfam19088   81 EKQEENELRALPPPSPAQLKALGAAVLEVAQEHGISDEDFEVRQEIVTRMEKIIQQHLPDCSLRLYGSCLTRFAFKTSDI 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 58331272    354 NIDIQFPAIMSQPDVLLLVQECLKNSDSFIDVDADFHARVPVVVCREKQSGLLCKVSA 411
Cdd:pfam19088  161 NIDVQFPSTMTQPDVLIQVLEILKNSESYSDVESDFHAKVPVVFCRDKQSGLMCKVSA 218
TUTF7_u4 pfam16631
Unstructured region 4 on terminal uridylyltransferase 7; TUTF7_u4 is the fourth natively ...
 1371-1450 1.88e-43

Unstructured region 4 on terminal uridylyltransferase 7; TUTF7_u4 is the fourth natively unstructured region found on a set of higher eukaryote Terminal uridylyltransferase 7 proteins. The function is not known. The region is rich in arginine and lysine.


Pssm-ID: 465208  Cd Length: 88  Bit Score: 152.70  E-value: 1.88e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272   1371 DQEDALNQRYPENKEKRSKEDKEIHNKYTEREVSTKEDKPIQCTPQKAKPMRAAADLGREKILRPPVEKWKRQDDKDLRE 1450
Cdd:pfam16631    9 DQEDTKNQRYPENKEKRSKEDKEIQNKYTEKEVSVKEGKLHPCTPQKAKPARAVVDTGREKSLRQSAEKWKRQDDRDLRE 88
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
979-1310 8.21e-38

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 149.54  E-value: 8.21e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272  979 PEDFKRIQLEPLPPLTPK-----FLNILDQVCIQCYKDFSPTIIEDQAREHIRQNLESFIRQDFPGTKLSLFGSSKNGFG 1053
Cdd:COG5260   30 PLDAKKVSIQELLELSIDsvfneESDELTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVFGSTETGLA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272 1054 FKQSDLDVCMTINGLEtaeGLDCVRTIEELARVLRKHSGLRNILpITTAKVPIVKFFHLRSGLEVDISLYNTLALHNTRL 1133
Cdd:COG5260  110 LPKSDIDLCIISDPRG---YKETRNAGSLASHLFKKNLAKEVVV-VSTARVPIIKLVDPQSGLHCDISFNNTNGIVNAKL 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272 1134 LSAYSAIDPRVKYLCYTMKVFTKMCDIGDASRGSLSSYAYTLMVLYFLQQRNPPviPVLQEIYKGEKKPEIFVDGWNIYF 1213
Cdd:COG5260  186 IRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPF--LFFDNGLLSPLKYNKNIDNLGVLF 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272 1214 FDqidelptywsecgkntesvgqlwlgLLRFYTEEFDFKEHVISIRR-KSLLTTFKKQW----TSKYIVIEDPF-DLNHN 1287
Cdd:COG5260  264 DD-------------------------FFELYGKSFNYSLVVLSINSgDFYLPKYEKGWlkpsKPNSLSIQDPGtDRNND 318

                        330       340
                 ....*....|....*....|...
gi 58331272 1288 LGAGlSRKMtNFIMKAFINGRRV 1310
Cdd:COG5260  319 ISAV-SFNI-KDIKAAFIRAFEL 339
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 1021-1138 5.29e-37

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: 135.38  E-value: 5.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272 1021 AREHIRQNLESFIRQDFPGTKLSLFGSSKNGFGFKQSDLDVCMTINGletaEGLDCVRTIEELARVLRKHSGLRNILPIT 1100
Cdd:cd05402    1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGPN----HRVDREDFLRKLAKLLKKSGEVVEVEPII 76

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 58331272 1101 TAKVPIVKFFHLRSGLEVDISLYNTLALHNTRLLSAYS 1138
Cdd:cd05402   77 NARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 315-427 8.82e-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: 111.88  E-value: 8.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272  315 QRLEIKRIMENVFQHKLPDCSLRLYGSSCSRLGFKNSDVNIDIQFPA-IMSQPDVLLLVQECLKNSDSFIDVDADFHARV 393
Cdd:cd05402    1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGPNhRVDREDFLRKLAKLLKKSGEVVEVEPIINARV 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 58331272  394 PVVVCREKQSGLLCKVSAGNENACLTTKHLTALG 427
Cdd:cd05402   81 PIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
301-478 1.38e-17

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 87.91  E-value: 1.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272  301 KVVQEFGLHNENLEQRLEIKRIMENVFQHKLPDCSLRLYGSSCSRLGFKNSDVNIDIQFPAIMSQPDV-LLLVQECLKNS 379
Cdd:COG5260   63 EFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVFGSTETGLALPKSDIDLCIISDPRGYKETRnAGSLASHLFKK 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272  380 DSFIDVDADFHARVPVVVCREKQSGLLCKVSAGNENACLTTKHLTALGKLEPKLVPLVIAFRYWAKLCSIDRPEEGGLPP 459
Cdd:COG5260  143 NLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVNAKLIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSS 222

                        170
                 ....*....|....*....
gi 58331272  460 YVFALMAIFFLQQRKEPLL 478
Cdd:COG5260  223 YTISCMVLSFLQMHPPFLF 241
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
 1233-1286 5.81e-15

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: 70.68  E-value: 5.81e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272   1233 SVGQLWLGLLRFYTEEFDFKEHVISIRRKSLLTTFKKQWT------SKYIVIEDPFDLNH 1286
Cdd:pfam03828    1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEKGWLrnegrrPFLLCIEDPFDLDN 60
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
 550-599 2.36e-11

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: 60.28  E-value: 2.36e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 58331272    550 PVGQLWVELLRFYALEFNLADLVISIRVKELVSRELKDWPK------KRIAIEDPY 599
Cdd:pfam03828    1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEKGWLRnegrrpFLLCIEDPF 56
TUTase pfam19088
TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase ...
 975-1061 8.53e-05

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: 45.51  E-value: 8.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272    975 KKDCPEDFKRIQLEPLPPLTPKFLNILDQVCIQCYKDFSPTIIEDQAREHIRQNLESFIRQDFPGTKLSLFGSSKNGFGF 1054
Cdd:pfam19088   76 KKNIMEKQEENELRALPPPSPAQLKALGAAVLEVAQEHGISDEDFEVRQEIVTRMEKIIQQHLPDCSLRLYGSCLTRFAF 155


                   ....*..
gi 58331272   1055 KQSDLDV 1061
Cdd:pfam19088  156 KTSDINI 162
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 1029-1113 1.53e-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: 42.02  E-value: 1.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331272   1029 LESFIRQDFPGTKLSLFGSSKNGFGFKQSDLDVCMTING-LETAEGLDCVRTIEELARVLRKHSGLRNILPITTAKVPIV 1107
Cdd:pfam01909    4 LREILKELFPVAEVVLFGSYARGTALPGSDIDLLVVFPEpVEEERLLKLAKIIKELEELLGLEVDLVTREKIEFPLVKID 83


                   ....*.
gi 58331272   1108 KFFHLR 1113
Cdd:pfam01909   84 ILEERI 89
ZnF_C2HC smart00343
zinc finger;
1452-1468 2.49e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 36.65  E-value: 2.49e-03
                            10
                    ....*....|....*..
gi 58331272    1452 RCFICGREGHIKKECPQ 1468
Cdd:smart00343    1 KCYNCGKEGHIARDCPS 17
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
 1451-1468 3.50e-03

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 36.35  E-value: 3.50e-03
                           10
                   ....*....|....*...
gi 58331272   1451 KRCFICGREGHIKKECPQ 1468
Cdd:pfam00098    1 GKCYNCGEPGHIARDCPK 18
ZnF_C2HC smart00343
zinc finger;
1346-1361 6.07e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 35.50  E-value: 6.07e-03
                            10
                    ....*....|....*.
gi 58331272    1346 CCRICGKIGHFMKDCP 1361
Cdd:smart00343    1 KCYNCGKEGHIARDCP 16
 
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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