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Conserved domains on  [gi|2788412556|ref|XP_067172864|]
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terminal uridylyltransferase 7 isoform X4 [Apteryx mantelli]

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 ...
189-406 2.29e-126

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: 391.80  E-value: 2.29e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  189 DQDEEVDGPVIDESVLSAKELLGLQQAEERLKQDCIYRLKKRPRSYPSAKYTCKLCDVLIESVAFAHKHMKEKRHKKSIK 268
Cdd:pfam19088    1 DQDEDEDGPVIDESNLTAEQQLGLRQAEERLKRDYIHRLKKRSPEYPNFQYLCKLCSVHIENIQGAHKHIKEKRHKKNIM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  269 EKQEEQLLTTLPPPTPSQIQAIGVAIENVVLEFGLNNEDLEERLKIKTTMENLLHQKLPESSLRLYGSSCSRFGFKTSDI 348
Cdd:pfam19088   81 EKQEENELRALPPPSPAQLKALGAAVLEVAQEHGISDEDFEVRQEIVTRMEKIIQQHLPDCSLRLYGSCLTRFAFKTSDI 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2788412556  349 NIDIQFPANMAQPDVLLLVQESLKNSESFIEVDADFHARIPVVVCREKQSGLTCKVSA 406
Cdd:pfam19088  161 NIDVQFPSTMTQPDVLIQVLEILKNSESYSDVESDFHAKVPVVFCRDKQSGLMCKVSA 218
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
1026-1143 4.05e-36

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: 132.68  E-value: 4.05e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556 1026 AREHIRQNLENFIRQDFPGTKLNLFGSSKNGFGFKQSDLDICWTIDGletaESLDCIRIIEDLAKVLKKHSGLRNVLPIT 1105
Cdd:cd05402      1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGPN----HRVDREDFLRKLAKLLKKSGEVVEVEPII 76
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2788412556 1106 TAKVPIVKFFHVRSGLEVDISLYNTLALHNTRLLSSYA 1143
Cdd:cd05402     77 NARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TUTF7_u4 pfam16631
Unstructured region 4 on terminal uridylyltransferase 7; TUTF7_u4 is the fourth natively ...
1330-1416 4.48e-35

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: 128.82  E-value: 4.48e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556 1330 RRKLRRRHDYEDIKNQRYTEKEKRSKEE-KEIQNKTTERESSIKEGKLQLCTPQKSKLARATVDTGRDKTPRQSAEKWKR 1408
Cdd:pfam16631    1 RRKVRRRRDQEDTKNQRYPENKEKRSKEdKEIQNKYTEKEVSVKEGKLHPCTPQKAKPARAVVDTGREKSLRQSAEKWKR 80

                   ....*...
gi 2788412556 1409 LEDRDLRE 1416
Cdd:pfam16631   81 QDDRDLRE 88
TRF4 super family cl34961
DNA polymerase sigma [Replication, recombination and repair];
984-1277 6.84e-24

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: 107.17  E-value: 6.84e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  984 PEDFKKIELDPLPMLSPKFSF-----ILDQVCVQCYQDFAPNIVEDQAREHIRQNLENFIRQDFPGTKLNLFGSSKNGFG 1058
Cdd:COG5260     30 PLDAKKVSIQELLELSIDSVFneesdELTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVFGSTETGLA 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556 1059 FKQSDLDICWTIDGLETAESldciRIIEDLAKVLKKHSGLRNVLPITTAKVPIVKFFHVRSGLEVDISLYNTLALHNTRL 1138
Cdd:COG5260    110 LPKSDIDLCIISDPRGYKET----RNAGSLASHLFKKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVNAKL 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556 1139 LSSYAAIDPRVKYLCYTMKVFTKIYKEPK---------KPEILVDGW-----NVYFFDKIeELSVVWPEcgKNTESVGQL 1204
Cdd:COG5260    186 IRSYLKEDPRLRPLVLIIKHWLKRRALNDvatgtlssyTISCMVLSFlqmhpPFLFFDNG-LLSPLKYN--KNIDNLGVL 262
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788412556 1205 WLGLLRFYTEEFDFKEHVICIRR-KNLLTTFKKQW----TSKYIVIEDPF-DLNHNLGAGlSRKMtNFIMKAFINGRRV 1277
Cdd:COG5260    263 FDDFFELYGKSFNYSLVVLSINSgDFYLPKYEKGWlkpsKPNSLSIQDPGtDRNNDISAV-SFNI-KDIKAAFIRAFEL 339
TRF4 super family cl34961
DNA polymerase sigma [Replication, recombination and repair];
259-599 1.72e-22

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: 102.93  E-value: 1.72e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  259 KEKRHKKSIKEKQEEQLLTTLPPPTPSQIQAIGVAIENVVLEFGLNNEDLEERLKIKTTMENLLHQKLPESSLRLYGSSC 338
Cdd:COG5260     26 KERRPLDAKKVSIQELLELSIDSVFNEESDELTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVFGSTE 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  339 SRFGFKTSDINIDIQFPANMAQPDVLLLVQES-LKNSESFIEVDADFHARIPVVVCREKQSGLTCKVSAGNENACLTTNH 417
Cdd:COG5260    106 TGLALPKSDIDLCIISDPRGYKETRNAGSLAShLFKKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVNAKL 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  418 LATLGKLEPTVVPLVIAFRYWAKLCCVDRPEEGGLSPYVFALMVIFFLQQRKEPFLpvylgswiggfslnkltnfnlkev 497
Cdd:COG5260    186 IRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPFLF------------------------ 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  498 endavvwEHNPLDDsdssketslkkgkvPLVFDSGHQcsaPVGQLWVELLRFYALEFNLADLVISIR-----LKETVSRE 572
Cdd:COG5260    242 -------FDNGLLS--------------PLKYNKNID---NLGVLFDDFFELYGKSFNYSLVVLSINsgdfyLPKYEKGW 297
                          330       340
                   ....*....|....*....|....*..
gi 2788412556  573 LKDWPKKRIAVEDPysvkrNVARTLNS 599
Cdd:COG5260    298 LKPSKPNSLSIQDP-----GTDRNNDI 319
PTZ00368 super family cl31762
universal minicircle sequence binding protein (UMSBP); Provisional
1307-1451 1.16e-04

universal minicircle sequence binding protein (UMSBP); Provisional


The actual alignment was detected with superfamily member PTZ00368:

Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 44.03  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556 1307 LAPNDRCCRICGKIGHFMKDCPmrrklRRRHDYEDIKnqrytekekrskeekeiqnktteressikegklqlC--TPQKS 1384
Cdd:PTZ00368    48 GGRGERSCYNCGKTGHLSRECP-----EAPPGSGPRS-----------------------------------CynCGQTG 87
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788412556 1385 KLARatvdtgrDKTPRQSAEKWKRledrdlrekRCFICGREGHIKKECPQYKGATGSSKSEVLCGSP 1451
Cdd:PTZ00368    88 HISR-------ECPNRAKGGAARR---------ACYNCGGEGHISRDCPNAGKRPGGDKTCYNCGQT 138
 
Name Accession Description Interval E-value
TUTase pfam19088
TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase ...
189-406 2.29e-126

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: 391.80  E-value: 2.29e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  189 DQDEEVDGPVIDESVLSAKELLGLQQAEERLKQDCIYRLKKRPRSYPSAKYTCKLCDVLIESVAFAHKHMKEKRHKKSIK 268
Cdd:pfam19088    1 DQDEDEDGPVIDESNLTAEQQLGLRQAEERLKRDYIHRLKKRSPEYPNFQYLCKLCSVHIENIQGAHKHIKEKRHKKNIM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  269 EKQEEQLLTTLPPPTPSQIQAIGVAIENVVLEFGLNNEDLEERLKIKTTMENLLHQKLPESSLRLYGSSCSRFGFKTSDI 348
Cdd:pfam19088   81 EKQEENELRALPPPSPAQLKALGAAVLEVAQEHGISDEDFEVRQEIVTRMEKIIQQHLPDCSLRLYGSCLTRFAFKTSDI 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2788412556  349 NIDIQFPANMAQPDVLLLVQESLKNSESFIEVDADFHARIPVVVCREKQSGLTCKVSA 406
Cdd:pfam19088  161 NIDVQFPSTMTQPDVLIQVLEILKNSESYSDVESDFHAKVPVVFCRDKQSGLMCKVSA 218
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
1026-1143 4.05e-36

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: 132.68  E-value: 4.05e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556 1026 AREHIRQNLENFIRQDFPGTKLNLFGSSKNGFGFKQSDLDICWTIDGletaESLDCIRIIEDLAKVLKKHSGLRNVLPIT 1105
Cdd:cd05402      1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGPN----HRVDREDFLRKLAKLLKKSGEVVEVEPII 76
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2788412556 1106 TAKVPIVKFFHVRSGLEVDISLYNTLALHNTRLLSSYA 1143
Cdd:cd05402     77 NARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TUTF7_u4 pfam16631
Unstructured region 4 on terminal uridylyltransferase 7; TUTF7_u4 is the fourth natively ...
1330-1416 4.48e-35

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: 128.82  E-value: 4.48e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556 1330 RRKLRRRHDYEDIKNQRYTEKEKRSKEE-KEIQNKTTERESSIKEGKLQLCTPQKSKLARATVDTGRDKTPRQSAEKWKR 1408
Cdd:pfam16631    1 RRKVRRRRDQEDTKNQRYPENKEKRSKEdKEIQNKYTEKEVSVKEGKLHPCTPQKAKPARAVVDTGREKSLRQSAEKWKR 80

                   ....*...
gi 2788412556 1409 LEDRDLRE 1416
Cdd:pfam16631   81 QDDRDLRE 88
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
311-422 3.32e-25

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: 101.48  E-value: 3.32e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  311 RLKIKTTMENLLHQKLPESSLRLYGSSCSRFGFKTSDINIDIQFPAN-MAQPDVLLLVQESLKNSESFIEVDADFHARIP 389
Cdd:cd05402      2 REEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGPNHrVDREDFLRKLAKLLKKSGEVVEVEPIINARVP 81
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2788412556  390 VVVCREKQSGLTCKVSAGNENACLTTNHLATLG 422
Cdd:cd05402     82 IIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
984-1277 6.84e-24

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 107.17  E-value: 6.84e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  984 PEDFKKIELDPLPMLSPKFSF-----ILDQVCVQCYQDFAPNIVEDQAREHIRQNLENFIRQDFPGTKLNLFGSSKNGFG 1058
Cdd:COG5260     30 PLDAKKVSIQELLELSIDSVFneesdELTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVFGSTETGLA 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556 1059 FKQSDLDICWTIDGLETAESldciRIIEDLAKVLKKHSGLRNVLPITTAKVPIVKFFHVRSGLEVDISLYNTLALHNTRL 1138
Cdd:COG5260    110 LPKSDIDLCIISDPRGYKET----RNAGSLASHLFKKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVNAKL 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556 1139 LSSYAAIDPRVKYLCYTMKVFTKIYKEPK---------KPEILVDGW-----NVYFFDKIeELSVVWPEcgKNTESVGQL 1204
Cdd:COG5260    186 IRSYLKEDPRLRPLVLIIKHWLKRRALNDvatgtlssyTISCMVLSFlqmhpPFLFFDNG-LLSPLKYN--KNIDNLGVL 262
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788412556 1205 WLGLLRFYTEEFDFKEHVICIRR-KNLLTTFKKQW----TSKYIVIEDPF-DLNHNLGAGlSRKMtNFIMKAFINGRRV 1277
Cdd:COG5260    263 FDDFFELYGKSFNYSLVVLSINSgDFYLPKYEKGWlkpsKPNSLSIQDPGtDRNNDISAV-SFNI-KDIKAAFIRAFEL 339
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
259-599 1.72e-22

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 102.93  E-value: 1.72e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  259 KEKRHKKSIKEKQEEQLLTTLPPPTPSQIQAIGVAIENVVLEFGLNNEDLEERLKIKTTMENLLHQKLPESSLRLYGSSC 338
Cdd:COG5260     26 KERRPLDAKKVSIQELLELSIDSVFNEESDELTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVFGSTE 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  339 SRFGFKTSDINIDIQFPANMAQPDVLLLVQES-LKNSESFIEVDADFHARIPVVVCREKQSGLTCKVSAGNENACLTTNH 417
Cdd:COG5260    106 TGLALPKSDIDLCIISDPRGYKETRNAGSLAShLFKKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVNAKL 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  418 LATLGKLEPTVVPLVIAFRYWAKLCCVDRPEEGGLSPYVFALMVIFFLQQRKEPFLpvylgswiggfslnkltnfnlkev 497
Cdd:COG5260    186 IRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPFLF------------------------ 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  498 endavvwEHNPLDDsdssketslkkgkvPLVFDSGHQcsaPVGQLWVELLRFYALEFNLADLVISIR-----LKETVSRE 572
Cdd:COG5260    242 -------FDNGLLS--------------PLKYNKNID---NLGVLFDDFFELYGKSFNYSLVVLSINsgdfyLPKYEKGW 297
                          330       340
                   ....*....|....*....|....*..
gi 2788412556  573 LKDWPKKRIAVEDPysvkrNVARTLNS 599
Cdd:COG5260    298 LKPSKPNSLSIQDP-----GTDRNNDI 319
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
1200-1253 6.10e-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: 6.10e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556 1200 SVGQLWLGLLRFYTEEFDFKEHVICIRRKNLLTTFKKQWT------SKYIVIEDPFDLNH 1253
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 ...
538-587 1.43e-10

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: 57.97  E-value: 1.43e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2788412556  538 PVGQLWVELLRFYALEFNLADLVISIRLKETVSRELKDWPK------KRIAVEDPY 587
Cdd:pfam03828    1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEKGWLRnegrrpFLLCIEDPF 56
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
1307-1451 1.16e-04

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 44.03  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556 1307 LAPNDRCCRICGKIGHFMKDCPmrrklRRRHDYEDIKnqrytekekrskeekeiqnktteressikegklqlC--TPQKS 1384
Cdd:PTZ00368    48 GGRGERSCYNCGKTGHLSRECP-----EAPPGSGPRS-----------------------------------CynCGQTG 87
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788412556 1385 KLARatvdtgrDKTPRQSAEKWKRledrdlrekRCFICGREGHIKKECPQYKGATGSSKSEVLCGSP 1451
Cdd:PTZ00368    88 HISR-------ECPNRAKGGAARR---------ACYNCGGEGHISRDCPNAGKRPGGDKTCYNCGQT 138
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
1034-1104 4.34e-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: 40.86  E-value: 4.34e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788412556 1034 LENFIRQDFPGTKLNLFGSSKNGFGFKQSDLDICWTIDG-LETAESLDCIRIIEDLAKVLKKHSGLRNVLPI 1104
Cdd:pfam01909    4 LREILKELFPVAEVVLFGSYARGTALPGSDIDLLVVFPEpVEEERLLKLAKIIKELEELLGLEVDLVTREKI 75
ZnF_C2HC smart00343
zinc finger;
1418-1434 2.15e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 36.65  E-value: 2.15e-03
                            10
                    ....*....|....*..
gi 2788412556  1418 RCFICGREGHIKKECPQ 1434
Cdd:smart00343    1 KCYNCGKEGHIARDCPS 17
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
1417-1434 3.23e-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: 3.23e-03
                           10
                   ....*....|....*...
gi 2788412556 1417 KRCFICGREGHIKKECPQ 1434
Cdd:pfam00098    1 GKCYNCGEPGHIARDCPK 18
 
Name Accession Description Interval E-value
TUTase pfam19088
TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase ...
189-406 2.29e-126

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: 391.80  E-value: 2.29e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  189 DQDEEVDGPVIDESVLSAKELLGLQQAEERLKQDCIYRLKKRPRSYPSAKYTCKLCDVLIESVAFAHKHMKEKRHKKSIK 268
Cdd:pfam19088    1 DQDEDEDGPVIDESNLTAEQQLGLRQAEERLKRDYIHRLKKRSPEYPNFQYLCKLCSVHIENIQGAHKHIKEKRHKKNIM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  269 EKQEEQLLTTLPPPTPSQIQAIGVAIENVVLEFGLNNEDLEERLKIKTTMENLLHQKLPESSLRLYGSSCSRFGFKTSDI 348
Cdd:pfam19088   81 EKQEENELRALPPPSPAQLKALGAAVLEVAQEHGISDEDFEVRQEIVTRMEKIIQQHLPDCSLRLYGSCLTRFAFKTSDI 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2788412556  349 NIDIQFPANMAQPDVLLLVQESLKNSESFIEVDADFHARIPVVVCREKQSGLTCKVSA 406
Cdd:pfam19088  161 NIDVQFPSTMTQPDVLIQVLEILKNSESYSDVESDFHAKVPVVFCRDKQSGLMCKVSA 218
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
1026-1143 4.05e-36

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: 132.68  E-value: 4.05e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556 1026 AREHIRQNLENFIRQDFPGTKLNLFGSSKNGFGFKQSDLDICWTIDGletaESLDCIRIIEDLAKVLKKHSGLRNVLPIT 1105
Cdd:cd05402      1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGPN----HRVDREDFLRKLAKLLKKSGEVVEVEPII 76
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2788412556 1106 TAKVPIVKFFHVRSGLEVDISLYNTLALHNTRLLSSYA 1143
Cdd:cd05402     77 NARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TUTF7_u4 pfam16631
Unstructured region 4 on terminal uridylyltransferase 7; TUTF7_u4 is the fourth natively ...
1330-1416 4.48e-35

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: 128.82  E-value: 4.48e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556 1330 RRKLRRRHDYEDIKNQRYTEKEKRSKEE-KEIQNKTTERESSIKEGKLQLCTPQKSKLARATVDTGRDKTPRQSAEKWKR 1408
Cdd:pfam16631    1 RRKVRRRRDQEDTKNQRYPENKEKRSKEdKEIQNKYTEKEVSVKEGKLHPCTPQKAKPARAVVDTGREKSLRQSAEKWKR 80

                   ....*...
gi 2788412556 1409 LEDRDLRE 1416
Cdd:pfam16631   81 QDDRDLRE 88
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
311-422 3.32e-25

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: 101.48  E-value: 3.32e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  311 RLKIKTTMENLLHQKLPESSLRLYGSSCSRFGFKTSDINIDIQFPAN-MAQPDVLLLVQESLKNSESFIEVDADFHARIP 389
Cdd:cd05402      2 REEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGPNHrVDREDFLRKLAKLLKKSGEVVEVEPIINARVP 81
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2788412556  390 VVVCREKQSGLTCKVSAGNENACLTTNHLATLG 422
Cdd:cd05402     82 IIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
984-1277 6.84e-24

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 107.17  E-value: 6.84e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  984 PEDFKKIELDPLPMLSPKFSF-----ILDQVCVQCYQDFAPNIVEDQAREHIRQNLENFIRQDFPGTKLNLFGSSKNGFG 1058
Cdd:COG5260     30 PLDAKKVSIQELLELSIDSVFneesdELTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVFGSTETGLA 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556 1059 FKQSDLDICWTIDGLETAESldciRIIEDLAKVLKKHSGLRNVLPITTAKVPIVKFFHVRSGLEVDISLYNTLALHNTRL 1138
Cdd:COG5260    110 LPKSDIDLCIISDPRGYKET----RNAGSLASHLFKKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVNAKL 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556 1139 LSSYAAIDPRVKYLCYTMKVFTKIYKEPK---------KPEILVDGW-----NVYFFDKIeELSVVWPEcgKNTESVGQL 1204
Cdd:COG5260    186 IRSYLKEDPRLRPLVLIIKHWLKRRALNDvatgtlssyTISCMVLSFlqmhpPFLFFDNG-LLSPLKYN--KNIDNLGVL 262
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2788412556 1205 WLGLLRFYTEEFDFKEHVICIRR-KNLLTTFKKQW----TSKYIVIEDPF-DLNHNLGAGlSRKMtNFIMKAFINGRRV 1277
Cdd:COG5260    263 FDDFFELYGKSFNYSLVVLSINSgDFYLPKYEKGWlkpsKPNSLSIQDPGtDRNNDISAV-SFNI-KDIKAAFIRAFEL 339
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
259-599 1.72e-22

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 102.93  E-value: 1.72e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  259 KEKRHKKSIKEKQEEQLLTTLPPPTPSQIQAIGVAIENVVLEFGLNNEDLEERLKIKTTMENLLHQKLPESSLRLYGSSC 338
Cdd:COG5260     26 KERRPLDAKKVSIQELLELSIDSVFNEESDELTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVFGSTE 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  339 SRFGFKTSDINIDIQFPANMAQPDVLLLVQES-LKNSESFIEVDADFHARIPVVVCREKQSGLTCKVSAGNENACLTTNH 417
Cdd:COG5260    106 TGLALPKSDIDLCIISDPRGYKETRNAGSLAShLFKKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVNAKL 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  418 LATLGKLEPTVVPLVIAFRYWAKLCCVDRPEEGGLSPYVFALMVIFFLQQRKEPFLpvylgswiggfslnkltnfnlkev 497
Cdd:COG5260    186 IRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPFLF------------------------ 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  498 endavvwEHNPLDDsdssketslkkgkvPLVFDSGHQcsaPVGQLWVELLRFYALEFNLADLVISIR-----LKETVSRE 572
Cdd:COG5260    242 -------FDNGLLS--------------PLKYNKNID---NLGVLFDDFFELYGKSFNYSLVVLSINsgdfyLPKYEKGW 297
                          330       340
                   ....*....|....*....|....*..
gi 2788412556  573 LKDWPKKRIAVEDPysvkrNVARTLNS 599
Cdd:COG5260    298 LKPSKPNSLSIQDP-----GTDRNNDI 319
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
1200-1253 6.10e-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: 6.10e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556 1200 SVGQLWLGLLRFYTEEFDFKEHVICIRRKNLLTTFKKQWT------SKYIVIEDPFDLNH 1253
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 ...
538-587 1.43e-10

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: 57.97  E-value: 1.43e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2788412556  538 PVGQLWVELLRFYALEFNLADLVISIRLKETVSRELKDWPK------KRIAVEDPY 587
Cdd:pfam03828    1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEKGWLRnegrrpFLLCIEDPF 56
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
1307-1451 1.16e-04

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 44.03  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556 1307 LAPNDRCCRICGKIGHFMKDCPmrrklRRRHDYEDIKnqrytekekrskeekeiqnktteressikegklqlC--TPQKS 1384
Cdd:PTZ00368    48 GGRGERSCYNCGKTGHLSRECP-----EAPPGSGPRS-----------------------------------CynCGQTG 87
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788412556 1385 KLARatvdtgrDKTPRQSAEKWKRledrdlrekRCFICGREGHIKKECPQYKGATGSSKSEVLCGSP 1451
Cdd:PTZ00368    88 HISR-------ECPNRAKGGAARR---------ACYNCGGEGHISRDCPNAGKRPGGDKTCYNCGQT 138
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
1034-1104 4.34e-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: 40.86  E-value: 4.34e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2788412556 1034 LENFIRQDFPGTKLNLFGSSKNGFGFKQSDLDICWTIDG-LETAESLDCIRIIEDLAKVLKKHSGLRNVLPI 1104
Cdd:pfam01909    4 LREILKELFPVAEVVLFGSYARGTALPGSDIDLLVVFPEpVEEERLLKLAKIIKELEELLGLEVDLVTREKI 75
TUTase pfam19088
TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase ...
991-1126 1.22e-03

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: 42.04  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788412556  991 ELDPLPMLSPKFSFILDQVCVQCYQDFAPNIVEDQAREHIRQNLENFIRQDFPGTKLNLFGSSKNGFGFKQSDLDICWTI 1070
Cdd:pfam19088   87 ELRALPPPSPAQLKALGAAVLEVAQEHGISDEDFEVRQEIVTRMEKIIQQHLPDCSLRLYGSCLTRFAFKTSDINIDVQF 166
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2788412556 1071 DGLETAESLdCIRIIEdlakVLKKHSGLRNVLPITTAKVPIVKFFHVRSGLEVDIS 1126
Cdd:pfam19088  167 PSTMTQPDV-LIQVLE----ILKNSESYSDVESDFHAKVPVVFCRDKQSGLMCKVS 217
ZnF_C2HC smart00343
zinc finger;
1418-1434 2.15e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 36.65  E-value: 2.15e-03
                            10
                    ....*....|....*..
gi 2788412556  1418 RCFICGREGHIKKECPQ 1434
Cdd:smart00343    1 KCYNCGKEGHIARDCPS 17
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
1417-1434 3.23e-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: 3.23e-03
                           10
                   ....*....|....*...
gi 2788412556 1417 KRCFICGREGHIKKECPQ 1434
Cdd:pfam00098    1 GKCYNCGEPGHIARDCPK 18
ZnF_C2HC smart00343
zinc finger;
1313-1328 5.29e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 35.50  E-value: 5.29e-03
                            10
                    ....*....|....*.
gi 2788412556  1313 CCRICGKIGHFMKDCP 1328
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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