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Conserved domains on  [gi|30682419|ref|NP_563894|]
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endonuclease/exonuclease/phosphatase family protein [Arabidopsis thaliana]

Protein Classification

zinc finger Ran-binding domain-containing protein( domain architecture ID 10650974)

zinc finger Ran-binding domain-containing protein; similar to human zinc finger Ran-binding domain-containing protein 2 (ZRANB2) which is a splice factor required for alternative splicing of TRA2B/SFRS10 transcripts and whose zinc finger domains bind single-stranded RNA, and to the zinc finger domain of human TAK1-binding protein 2 (TAB2) which binds Lys 63-linked polyubiquitin chains

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
 173-438 1.68e-91

Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related domains; Human TDP2, also known as TTRAP (TRAF/TNFR-associated factors, and tumor necrosis factor receptor/TNFR-associated protein), is a 5'-tyrosyl DNA phosphodiesterase. It is required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini, needed for subsequent DNA ligation, and hence repair of the break. TDP2 and 3'-tyrosyl DNA phosphodiesterase (TDP1) are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TTRAP has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation, and it may inhibit the activation of nuclear factor-kB. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


:

Pssm-ID: 197314 [Multi-domain]  Cd Length: 248  Bit Score: 276.92  E-value: 1.68e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 173 LKILSYNVWFREDLELNLRMRAIGHLIQLHSPHLICFQEVTPEIYDIFRKSNWW-KAYSCSVSVDVAVSRGYYCMLLSKL 251
Cdd:cd09080   1 LKVLTWNVDFLDDVNLAERMRAILKLLEELDPDVIFLQEVTPPFLAYLLSQPWVrKNYYFSEGPPSPAVDPYGVLILSKK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 252 GVKSFSSKsFGNSIMGRELSIAEVEVPGRKPLVFATSHLESPCPGPPkwdqmfsrERVEQAKEAIEILR---PNANVIFG 328
Cdd:cd09080  81 SLVVRRVP-FTSTRMGRNLLAAEINLGSGEPLRLATTHLESLKSHSS--------ERTAQLEEIAKKLKkppGAANVILG 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 329 GDMNWCDKLDGKFPLPDKWVDVWEVLKP-GDLGFTYDTKANPML-SGNRALQKRLDRILCRLDDYKLGGIEMVGKEAIPG 406
Cdd:cd09080 152 GDFNLRDKEDDTGGLPNGFVDAWEELGPpGEPGYTWDTQKNPMLrKGEAGPRKRFDRVLLRGSDLKPKSIELIGTEPIPG 231

                       250       260       270
                ....*....|....*....|....*....|..
gi 30682419 407 lsyvkekkvrgdikkLELPVLPSDHFGLLVTL 438
Cdd:cd09080 232 ---------------DEEGLFPSDHFGLLAEL 248
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 65-88 8.53e-04

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


:

Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 36.53  E-value: 8.53e-04
                           10        20
                   ....*....|....*....|....
gi 30682419     65 KWACKACTFLNTYKNSICDVCGTR 88
Cdd:smart00547   2 DWECPACTFLNFASRSKCFACGAP 25
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 18-43 9.69e-04

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


:

Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 36.53  E-value: 9.69e-04
                           10        20
                   ....*....|....*....|....*.
gi 30682419     18 SSWSCNKCTFLNSASQKlNCMICLAP 43
Cdd:smart00547   1 GDWECPACTFLNFASRS-KCFACGAP 25
 
Name Accession Description Interval E-value
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
 173-438 1.68e-91

Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related domains; Human TDP2, also known as TTRAP (TRAF/TNFR-associated factors, and tumor necrosis factor receptor/TNFR-associated protein), is a 5'-tyrosyl DNA phosphodiesterase. It is required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini, needed for subsequent DNA ligation, and hence repair of the break. TDP2 and 3'-tyrosyl DNA phosphodiesterase (TDP1) are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TTRAP has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation, and it may inhibit the activation of nuclear factor-kB. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197314 [Multi-domain]  Cd Length: 248  Bit Score: 276.92  E-value: 1.68e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 173 LKILSYNVWFREDLELNLRMRAIGHLIQLHSPHLICFQEVTPEIYDIFRKSNWW-KAYSCSVSVDVAVSRGYYCMLLSKL 251
Cdd:cd09080   1 LKVLTWNVDFLDDVNLAERMRAILKLLEELDPDVIFLQEVTPPFLAYLLSQPWVrKNYYFSEGPPSPAVDPYGVLILSKK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 252 GVKSFSSKsFGNSIMGRELSIAEVEVPGRKPLVFATSHLESPCPGPPkwdqmfsrERVEQAKEAIEILR---PNANVIFG 328
Cdd:cd09080  81 SLVVRRVP-FTSTRMGRNLLAAEINLGSGEPLRLATTHLESLKSHSS--------ERTAQLEEIAKKLKkppGAANVILG 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 329 GDMNWCDKLDGKFPLPDKWVDVWEVLKP-GDLGFTYDTKANPML-SGNRALQKRLDRILCRLDDYKLGGIEMVGKEAIPG 406
Cdd:cd09080 152 GDFNLRDKEDDTGGLPNGFVDAWEELGPpGEPGYTWDTQKNPMLrKGEAGPRKRFDRVLLRGSDLKPKSIELIGTEPIPG 231

                       250       260       270
                ....*....|....*....|....*....|..
gi 30682419 407 lsyvkekkvrgdikkLELPVLPSDHFGLLVTL 438
Cdd:cd09080 232 ---------------DEEGLFPSDHFGLLAEL 248
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 176-332 2.58e-14

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 71.10  E-value: 2.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419   176 LSYNVWF--REDLELNLRMRAIGHLIQLHSPHLICFQEVTPEIYDIFRKSNWWKAYSCSVSVDVAVSRGYYCMLLSKLGV 253
Cdd:pfam03372   1 LTWNVNGgnADAAGDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFLSYGGPGGGGGGGGVAILSRYPL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682419   254 KSFSSKSFGNSIMGRELSIAEVEVPGRKPLVFATSHLESPCPGPPKWDQmfsreRVEQAKEAIEILRPNANVIFGGDMN 332
Cdd:pfam03372  81 SSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQR-----ADLLLLLLALLAPRSEPVILAGDFN 154
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 173-332 3.69e-14

Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function prediction only];


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 69.94  E-value: 3.69e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 173 LKILSYNVWFREDLELNLRMRAIGHLIQLHSPHLICFQEVtpeiydifrksnwwkayscsvsvdvavsrgyycMLLSKLG 252
Cdd:COG3568   8 LRVMTYNIRYGLGTDGRADLERIARVIRALDPDVVALQEN---------------------------------AILSRYP 54

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 253 VKSFSSKSFGN-SIMGRELSIAEVEVPGRkPLVFATSHLESPCPgppkwdqmfsRERVEQAKEAIEILR---PNANVIFG 328
Cdd:COG3568  55 IVSSGTFDLPDpGGEPRGALWADVDVPGK-PLRVVNTHLDLRSA----------AARRRQARALAELLAelpAGAPVILA 123


                ....
gi 30682419 329 GDMN 332
Cdd:COG3568 124 GDFN 127
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 65-88 8.53e-04

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 36.53  E-value: 8.53e-04
                           10        20
                   ....*....|....*....|....
gi 30682419     65 KWACKACTFLNTYKNSICDVCGTR 88
Cdd:smart00547   2 DWECPACTFLNFASRSKCFACGAP 25
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 18-43 9.69e-04

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 36.53  E-value: 9.69e-04
                           10        20
                   ....*....|....*....|....*.
gi 30682419     18 SSWSCNKCTFLNSASQKlNCMICLAP 43
Cdd:smart00547   1 GDWECPACTFLNFASRS-KCFACGAP 25
 
Name Accession Description Interval E-value
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
 173-438 1.68e-91

Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related domains; Human TDP2, also known as TTRAP (TRAF/TNFR-associated factors, and tumor necrosis factor receptor/TNFR-associated protein), is a 5'-tyrosyl DNA phosphodiesterase. It is required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini, needed for subsequent DNA ligation, and hence repair of the break. TDP2 and 3'-tyrosyl DNA phosphodiesterase (TDP1) are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TTRAP has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation, and it may inhibit the activation of nuclear factor-kB. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197314 [Multi-domain]  Cd Length: 248  Bit Score: 276.92  E-value: 1.68e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 173 LKILSYNVWFREDLELNLRMRAIGHLIQLHSPHLICFQEVTPEIYDIFRKSNWW-KAYSCSVSVDVAVSRGYYCMLLSKL 251
Cdd:cd09080   1 LKVLTWNVDFLDDVNLAERMRAILKLLEELDPDVIFLQEVTPPFLAYLLSQPWVrKNYYFSEGPPSPAVDPYGVLILSKK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 252 GVKSFSSKsFGNSIMGRELSIAEVEVPGRKPLVFATSHLESPCPGPPkwdqmfsrERVEQAKEAIEILR---PNANVIFG 328
Cdd:cd09080  81 SLVVRRVP-FTSTRMGRNLLAAEINLGSGEPLRLATTHLESLKSHSS--------ERTAQLEEIAKKLKkppGAANVILG 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 329 GDMNWCDKLDGKFPLPDKWVDVWEVLKP-GDLGFTYDTKANPML-SGNRALQKRLDRILCRLDDYKLGGIEMVGKEAIPG 406
Cdd:cd09080 152 GDFNLRDKEDDTGGLPNGFVDAWEELGPpGEPGYTWDTQKNPMLrKGEAGPRKRFDRVLLRGSDLKPKSIELIGTEPIPG 231

                       250       260       270
                ....*....|....*....|....*....|..
gi 30682419 407 lsyvkekkvrgdikkLELPVLPSDHFGLLVTL 438
Cdd:cd09080 232 ---------------DEEGLFPSDHFGLLAEL 248
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 176-332 2.58e-14

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 71.10  E-value: 2.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419   176 LSYNVWF--REDLELNLRMRAIGHLIQLHSPHLICFQEVTPEIYDIFRKSNWWKAYSCSVSVDVAVSRGYYCMLLSKLGV 253
Cdd:pfam03372   1 LTWNVNGgnADAAGDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFLSYGGPGGGGGGGGVAILSRYPL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682419   254 KSFSSKSFGNSIMGRELSIAEVEVPGRKPLVFATSHLESPCPGPPKWDQmfsreRVEQAKEAIEILRPNANVIFGGDMN 332
Cdd:pfam03372  81 SSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQR-----ADLLLLLLALLAPRSEPVILAGDFN 154
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 173-332 3.69e-14

Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function prediction only];


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 69.94  E-value: 3.69e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 173 LKILSYNVWFREDLELNLRMRAIGHLIQLHSPHLICFQEVtpeiydifrksnwwkayscsvsvdvavsrgyycMLLSKLG 252
Cdd:COG3568   8 LRVMTYNIRYGLGTDGRADLERIARVIRALDPDVVALQEN---------------------------------AILSRYP 54

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 253 VKSFSSKSFGN-SIMGRELSIAEVEVPGRkPLVFATSHLESPCPgppkwdqmfsRERVEQAKEAIEILR---PNANVIFG 328
Cdd:COG3568  55 IVSSGTFDLPDpGGEPRGALWADVDVPGK-PLRVVNTHLDLRSA----------AARRRQARALAELLAelpAGAPVILA 123


                ....
gi 30682419 329 GDMN 332
Cdd:COG3568 124 GDFN 127
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 175-438 5.49e-12

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes the catalytic domain (exonuclease/endonuclease/phosphatase or EEP domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins.


Pssm-ID: 197306 [Multi-domain]  Cd Length: 241  Bit Score: 65.58  E-value: 5.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 175 ILSYNVwfrEDLELNLRMRAIGHLIQLHSPHLICFQEVTPEIYDIFRKSNWWKAYSCSVSVdVAVSRGYY--CMLLSK-- 250
Cdd:cd08372   1 VASYNV---NGLNAATRASGIARWVRELDPDIVCLQEVKDSQYSAVALNQLLPEGYHQYQS-GPSRKEGYegVAILSKtp 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 251 -LGVKSFSSKSFGNSIMG-RELSIAEVEVPGRKpLVFATSHLEspcpgppkWDQMFSRERVEQAKEAIEILR-----PNA 323
Cdd:cd08372  77 kFKIVEKHQYKFGEGDSGeRRAVVVKFDVHDKE-LCVVNAHLQ--------AGGTRADVRDAQLKEVLEFLKrlrqpNSA 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 324 NVIFGGDMN--------WCDKLDGKFPLPDKWVDVWEvlkpgDLGFTYDTKANPmlsgnRALQKRLDRILcrlddyklgg 395
Cdd:cd08372 148 PVVICGDFNvrpsevdsENPSSMLRLFVALNLVDSFE-----TLPHAYTFDTYM-----HNVKSRLDYIF---------- 207

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 30682419 396 iemVGKEAIPglsYVKEKKVRGDIKkleLPVLPSDHFGLLVTL 438
Cdd:cd08372 208 ---VSKSLLP---SVKSSKILSDAA---RARIPSDHYPIEVTL 241
nSMase cd09078
Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological ...
 173-438 3.97e-07

Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological membranes to ceramide and phosphorylcholine; Sphingomyelinases (SMase) are phosphodiesterases that catalyze the hydrolysis of sphingomyelin to ceramide and phosphorylcholine. Eukaryotic SMases have been classified according to their pH optima and are known as acid SMase, alkaline SMase, and neutral SMase (nSMase). Eukaryotic proteins in this family are nSMases, and are activated by a variety of stress-inducing agents such as cytokines or UV radiation. Ceramides and other metabolic derivatives, including sphingosine, are lipid "second messenger" molecules that participate in the regulation of stress-induced cellular responses, including cell death, adhesion, differentiation, and proliferation. Bacterial neutral SMases, which also belong to this domain family, are secreted proteins that act as membrane-damaging virulence factors. They promote colonization of the host tissue. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197312 [Multi-domain]  Cd Length: 280  Bit Score: 51.19  E-value: 3.97e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 173 LKILSYNVWFR-------EDLELNLRMRAIGHLIQlhSPHLICFQEV-TPEIYDIFRK-------------SNWWKAYSC 231
Cdd:cd09078   1 LKVLTYNVFLLppllynnGDDGQDERLDLIPKALL--QYDVVVLQEVfDARARKRLLNglkkeypyqtdvvGRSPSGWSS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 232 SVsvdvaVSRGyyCMLLSKL--------------GVKSFSSKSFgnsIMgrelsiAEVEVPGRKPL-VFATsHLESPcPG 296
Cdd:cd09078  79 KL-----VDGG--VVILSRYpivekdqyifpngcGADCLAAKGV---LY------AKINKGGTKVYhVFGT-HLQAS-DG 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 297 PPKWDQMfsreRVEQAKEAIEILR-----PNANVIFGGDMNwCDKLDGKFPLPDKW-----VDVWEVLKPGDLGFTYDTK 366
Cdd:cd09078 141 SCLDRAV----RQKQLDELRAFIEeknipDNEPVIIAGDFN-VDKRSSRDEYDDMLeqlhdYNAPEPITAGETPLTWDPG 215

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682419 367 ANPMLSGN--RALQKRLDRILCRLDDYKLGGIE-MVGKEAIPGLSYVKEKKVRGDikklelpvlpSDHFGLLVTL 438
Cdd:cd09078 216 TNLLAKYNypGGGGERLDYILYSNDHLQPSSWSnEVEVPKSPTWSVTNGYTFADL----------SDHYPVSATF 280
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
173-332 4.76e-04

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 42.32  E-value: 4.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 173 LKILSYNV-WF--------------REDLELNLRMRAIGHLIQLHSPHLICFQEVtpE---------IYDIFRKSNWWKA 228
Cdd:COG2374  69 LRVATFNVeNLfdtddddddfgrgaDTPEEYERKLAKIAAAIAALDADIVGLQEV--EnngsalqdlVAALNLAGGTYAF 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 229 YSCSVSVDvavSRGYYCMLLSK------LGVKS---FSSKSFGNSIMGRELSIAEVEVPGRKPLVFATSHLESPCPGPPK 299
Cdd:COG2374 147 VHPPDGPD---GDGIRVALLYRpdrvtlVGSATiadLPDSPGNPDRFSRPPLAVTFELANGEPFTVIVNHFKSKGSDDPG 223

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30682419 300 WDQMFSRE-RVEQAKEAIEIL------RPNANVIFGGDMN 332
Cdd:COG2374 224 DGQGASEAkRTAQAEALRAFVdsllaaDPDAPVIVLGDFN 263
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 65-88 8.53e-04

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 36.53  E-value: 8.53e-04
                           10        20
                   ....*....|....*....|....
gi 30682419     65 KWACKACTFLNTYKNSICDVCGTR 88
Cdd:smart00547   2 DWECPACTFLNFASRSKCFACGAP 25
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 18-43 9.69e-04

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 36.53  E-value: 9.69e-04
                           10        20
                   ....*....|....*....|....*.
gi 30682419     18 SSWSCNKCTFLNSASQKlNCMICLAP 43
Cdd:smart00547   1 GDWECPACTFLNFASRS-KCFACGAP 25
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
 281-385 3.55e-03

Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a membrane-associated nuclease related to Deoxyribonuclease 1 (DNase1 or DNase I, EC 3.1.21.1). The in vivo role of MnuA is as yet undetermined. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197338 [Multi-domain]  Cd Length: 266  Bit Score: 38.92  E-value: 3.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682419 281 KPLVFATSHLESPCPGPPKWDQmfsrERVEQAKEAIEILR------PNANVIFGGDMNwcdkldgkfpLPDKwVDVWEVL 354
Cdd:cd10283 124 FDFTLVNVHLKSGGSSKSGQGA----KRVAEAQALAEYLKeladedPDDDVILLGDFN----------IPAD-EDAFKAL 188

                        90       100       110
                ....*....|....*....|....*....|..
gi 30682419 355 KpgDLGFTYDTKANPMLSG-NRALQKRLDRIL 385
Cdd:cd10283 189 T--KAGFKSLLPDSTNLSTsFKGYANSYDNIF 218
 
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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