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Conserved domains on  [gi|1311712405|ref|WP_101217593|]
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MULTISPECIES: ExeM/NucH family extracellular endonuclease [Pseudoalteromonas]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ExeM_NucH_DNase NF033681
ExeM/NucH family extracellular endonuclease;
233-774 0e+00

ExeM/NucH family extracellular endonuclease;


:

Pssm-ID: 468139 [Multi-domain]  Cd Length: 545  Bit Score: 800.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 233 EGIVTADFqdDDQLKGFFVSSLAADIDANPLTSEGVFVYFADI--DVNVGDHVRVQGTVEEYFDATQIGSVSQVAVCGTG 310
Cdd:NF033681    2 EGVVTAVP--TGGLNGFYLQTPGTDGDGNPATSDGLFVYTGAAvtDVAVGDRVRVTGTVSEYYGLTQLSAVSAVEVCGTG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 311 LAAAATKITLPLADTTDLEAFEGMLVTLEQPLVVTNNFGLGRYGEVELAT-ERLYQGTQVALPG-DAANAVETENLLKKI 388
Cdd:NF033681   80 AAVTPTPLTLPVDEALRLERYEGMLVRLPQDLTVTDNYNLGRYGELVLSAgGRLLQPTQVAAPGsAEAAALAAANAARRI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 389 LLDDGSTGQNLDPTAYPtPGLSAENTLRTGDTVNTVTGALAYSFSLYRIHPT---VAPSFIATNARENAPELnAEADLRV 465
Cdd:NF033681  160 VLDDGSTAQNPGPVPYY-PGLSADNTLRVGDTVTGLTGVLDYRFGAYRLQPTngaTAPDFVPANPRPAAPAL-VGGDLRV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 466 ASFNVLNYFNGDGQGGG--FPTARGADSEAEFTRQEAKIVSAISAIQADVVGLMEIENDGFGEFSAIASLVDALNDADSA 543
Cdd:NF033681  238 ASFNVLNYFNGDGFGGPadFPTNRGADTAAEFERQQAKIVAAINALDADVVGLMEIENNGYGRDSAIADLVDALNAAAGG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 544 NNYAFVD-FNVGQIGTDAITTALIYRANKVEEVGTAAITTEAPFDFSNRAPIAQSFKSLETDEVFTVAVSHLKSKSCGSA 622
Cdd:NF033681  318 GTYAYVPsPGTDPLGTDAIRVALIYRPAKVTPVGDAAILDDPAFDGSNRPPLAQTFRPKGGGETFTVVVNHFKSKGSGCA 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 623 SGNNaDSGDGQGCWNEIRTEGANAFANWLDSKPTGVDDEDTILVGDMNAYAMEDPIRAFADKGYKNVVAEIDGDTlGYSY 702
Cdd:NF033681  398 SGDD-DQGDGQGCWNATRVAAAQALADWLATLPTGVGDGDVLLLGDLNAYAKEDPIRVLTDAGYTNLVARFHGDD-AYSY 475
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1311712405 703 SFSGRAGSLDHAVATQSLLSKIVAATDWHINADEPISLDYNVEFKSEgqqSSLYSESAYRASDHDPVIIDIK 774
Cdd:NF033681  476 VFGGESGSLDHALASPSLAAKVVGATDWHINADEPTALDYNTEYKGA---ADLYAPDPYRSSDHDPVIVGLD 544
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
18-126 2.75e-14

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


:

Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 69.76  E-value: 2.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405  18 APASADLIISEYIEGSS--NNKAIELYNNAPTSIVLDGYTLGLYSNGSDTVGNSIaltgELAANTTYVIANSGAIEDILS 95
Cdd:pfam00932   1 SSATGDVVISEVVYDGSggNDEFIELYNTGSKAVDLSGWKLQDASGGTYTFPNGT----TLAPGQTVVVWTGSGTNSATA 76
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1311712405  96 ISDTTSTVTFYNGDDALVLTK-DGIVVDSFGQ 126
Cdd:pfam00932  77 GYWGPSNAVWNNGGDAVALYDaNGELVDSVGY 108
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
793-887 1.81e-08

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 52.70  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 793 VFAVDENSAIGTIIGTLDFSDPNADESPVVKF-ITSDNDS--VSINNQ-GQLIVAGEIDYEFENRITLTVQAQDSVGN-L 867
Cdd:cd11304     3 EVSVPENAPPGTVVLTVSATDPDSGENGEVTYsIVSGNEDglFSIDPStGEITTAKPLDREEQSSYTLTVTATDGGGPpL 82
                          90       100
                  ....*....|....*....|
gi 1311712405 868 SNVEKVAVKVNnlrsdDDND 887
Cdd:cd11304    83 SSTATVTITVL-----DVND 97
 
Name Accession Description Interval E-value
ExeM_NucH_DNase NF033681
ExeM/NucH family extracellular endonuclease;
233-774 0e+00

ExeM/NucH family extracellular endonuclease;


Pssm-ID: 468139 [Multi-domain]  Cd Length: 545  Bit Score: 800.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 233 EGIVTADFqdDDQLKGFFVSSLAADIDANPLTSEGVFVYFADI--DVNVGDHVRVQGTVEEYFDATQIGSVSQVAVCGTG 310
Cdd:NF033681    2 EGVVTAVP--TGGLNGFYLQTPGTDGDGNPATSDGLFVYTGAAvtDVAVGDRVRVTGTVSEYYGLTQLSAVSAVEVCGTG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 311 LAAAATKITLPLADTTDLEAFEGMLVTLEQPLVVTNNFGLGRYGEVELAT-ERLYQGTQVALPG-DAANAVETENLLKKI 388
Cdd:NF033681   80 AAVTPTPLTLPVDEALRLERYEGMLVRLPQDLTVTDNYNLGRYGELVLSAgGRLLQPTQVAAPGsAEAAALAAANAARRI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 389 LLDDGSTGQNLDPTAYPtPGLSAENTLRTGDTVNTVTGALAYSFSLYRIHPT---VAPSFIATNARENAPELnAEADLRV 465
Cdd:NF033681  160 VLDDGSTAQNPGPVPYY-PGLSADNTLRVGDTVTGLTGVLDYRFGAYRLQPTngaTAPDFVPANPRPAAPAL-VGGDLRV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 466 ASFNVLNYFNGDGQGGG--FPTARGADSEAEFTRQEAKIVSAISAIQADVVGLMEIENDGFGEFSAIASLVDALNDADSA 543
Cdd:NF033681  238 ASFNVLNYFNGDGFGGPadFPTNRGADTAAEFERQQAKIVAAINALDADVVGLMEIENNGYGRDSAIADLVDALNAAAGG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 544 NNYAFVD-FNVGQIGTDAITTALIYRANKVEEVGTAAITTEAPFDFSNRAPIAQSFKSLETDEVFTVAVSHLKSKSCGSA 622
Cdd:NF033681  318 GTYAYVPsPGTDPLGTDAIRVALIYRPAKVTPVGDAAILDDPAFDGSNRPPLAQTFRPKGGGETFTVVVNHFKSKGSGCA 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 623 SGNNaDSGDGQGCWNEIRTEGANAFANWLDSKPTGVDDEDTILVGDMNAYAMEDPIRAFADKGYKNVVAEIDGDTlGYSY 702
Cdd:NF033681  398 SGDD-DQGDGQGCWNATRVAAAQALADWLATLPTGVGDGDVLLLGDLNAYAKEDPIRVLTDAGYTNLVARFHGDD-AYSY 475
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1311712405 703 SFSGRAGSLDHAVATQSLLSKIVAATDWHINADEPISLDYNVEFKSEgqqSSLYSESAYRASDHDPVIIDIK 774
Cdd:NF033681  476 VFGGESGSLDHALASPSLAAKVVGATDWHINADEPTALDYNTEYKGA---ADLYAPDPYRSSDHDPVIVGLD 544
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
423-774 7.14e-92

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 295.01  E-value: 7.14e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 423 TVTGALaysFSLYRIhptvaPSFIATNARENAPelnAEADLRVASFNVLNYFNGDGQGGGFptARGADSEAEFTRQEAKI 502
Cdd:COG2374    40 GLTGVL---FGNYRQ-----PTETFVNPRPEAP---VGGDLRVATFNVENLFDTDDDDDDF--GRGADTPEEYERKLAKI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 503 VSAISAIQADVVGLMEIENDGfgefSAIASLVDALNDAdsANNYAFVDFNVGQIGtDAITTALIYRANKVEEVGTAAI-- 580
Cdd:COG2374   107 AAAIAALDADIVGLQEVENNG----SALQDLVAALNLA--GGTYAFVHPPDGPDG-DGIRVALLYRPDRVTLVGSATIad 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 581 TTEAPF--DFSNRAPIAQSFKsLETDEVFTVAVSHLKSKSCGsasgnnaDSGDGQGCWNEIRTEGANAFANWLDSKPTGV 658
Cdd:COG2374   180 LPDSPGnpDRFSRPPLAVTFE-LANGEPFTVIVNHFKSKGSD-------DPGDGQGASEAKRTAQAEALRAFVDSLLAAD 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 659 DDEDTILVGDMNAYAMEDPIRAF-ADKGYKNVVAEIDGDTlGYSYSFSGRAGSLDHAVATQSLLSKIVAATDWHINADep 737
Cdd:COG2374   252 PDAPVIVLGDFNDYPFEDPLRALlGAGGLTNLAEKLPAAE-RYSYVYDGNSGLLDHILVSPALAARVTGADIWHINAD-- 328
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1311712405 738 islDYNVEFKSEGqqsSLYSESAYRASDHDPVIIDIK 774
Cdd:COG2374   329 ---IYNDDFKPDF---RTYADDPGRASDHDPVVVGLR 359
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
463-773 1.33e-52

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: 184.91  E-value: 1.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 463 LRVASFNVLNYFNGDGQgggfptargadseaEFTRQEAKIVSAISAiqaDVVGLMEIENDGfGEFSAIASLVDALNDADS 542
Cdd:cd10283     1 LRIASWNILNFGNSKGK--------------EKNPAIAEIISAFDL---DLIALQEVMDNG-GGLDALAKLVNELNKPGG 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 543 ANNYAFVDFNVGQIGtDAITTALIYRANKVEEVGTAAITTEAPFDFSNRAPIAQSFKSLETDEVFTVAVSHLKSKScGSA 622
Cdd:cd10283    63 TWKYIVSDKTGGSSG-DKERYAFLYKSSKVRKVGKAVLEKDSNTDGFARPPYAAKFKSGGTGFDFTLVNVHLKSGG-SSK 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 623 SGNNADsgdgqgcwneiRTEGANAFANWLDSKPTGVDDEDTILVGDMNAYAMEDPIRAFADKGYKNVVAeidgDTLGYSY 702
Cdd:cd10283   141 SGQGAK-----------RVAEAQALAEYLKELADEDPDDDVILLGDFNIPADEDAFKALTKAGFKSLLP----DSTNLST 205
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1311712405 703 SFSGRAGSLDHAVATQSLLSKIVAA--TDWHINADEPISLDYNvefksegqqsslYSESAYRASDHDPVIIDI 773
Cdd:cd10283   206 SFKGYANSYDNIFVSGNLKEKFSNSgvFDFNILVDEAGEEDLD------------YSKWRKQISDHDPVWVEF 266
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
18-126 2.75e-14

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 69.76  E-value: 2.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405  18 APASADLIISEYIEGSS--NNKAIELYNNAPTSIVLDGYTLGLYSNGSDTVGNSIaltgELAANTTYVIANSGAIEDILS 95
Cdd:pfam00932   1 SSATGDVVISEVVYDGSggNDEFIELYNTGSKAVDLSGWKLQDASGGTYTFPNGT----TLAPGQTVVVWTGSGTNSATA 76
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1311712405  96 ISDTTSTVTFYNGDDALVLTK-DGIVVDSFGQ 126
Cdd:pfam00932  77 GYWGPSNAVWNNGGDAVALYDaNGELVDSVGY 108
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
793-887 1.81e-08

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 52.70  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 793 VFAVDENSAIGTIIGTLDFSDPNADESPVVKF-ITSDNDS--VSINNQ-GQLIVAGEIDYEFENRITLTVQAQDSVGN-L 867
Cdd:cd11304     3 EVSVPENAPPGTVVLTVSATDPDSGENGEVTYsIVSGNEDglFSIDPStGEITTAKPLDREEQSSYTLTVTATDGGGPpL 82
                          90       100
                  ....*....|....*....|
gi 1311712405 868 SNVEKVAVKVNnlrsdDDND 887
Cdd:cd11304    83 SSTATVTITVL-----DVND 97
Cadherin pfam00028
Cadherin domain;
792-877 3.23e-05

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 43.44  E-value: 3.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 792 QVFAVDENSAIGTIIGTLDFSDPN-ADESPVVKFITSDN--DSVSINNQ-GQLIVAGEIDYEFENRITLTVQAQDSVG-N 866
Cdd:pfam00028   1 YSASVPENAPVGTEVLTVTATDPDlGPNGRIFYSILGGGpgGNFRIDPDtGDISTTKPLDRESIGEYELTVEATDSGGpP 80
                          90
                  ....*....|.
gi 1311712405 867 LSNVEKVAVKV 877
Cdd:pfam00028  81 LSSTATVTITV 91
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
812-887 6.33e-03

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 36.56  E-value: 6.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405  812 SDPNADESPVVKF-ITSDNDS--VSIN-NQGQLIVAGEIDYEFENRITLTVQAQDSVG-NLSNVEKVAVKVNnlrsdDDN 886
Cdd:smart00112   3 TDADSGENGKVTYsILSGNDDglFSIDpETGEITTTKPLDREEQPEYTLTVEATDGGGpPLSSTATVTITVL-----DVN 77

                   .
gi 1311712405  887 D 887
Cdd:smart00112  78 D 78
 
Name Accession Description Interval E-value
ExeM_NucH_DNase NF033681
ExeM/NucH family extracellular endonuclease;
233-774 0e+00

ExeM/NucH family extracellular endonuclease;


Pssm-ID: 468139 [Multi-domain]  Cd Length: 545  Bit Score: 800.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 233 EGIVTADFqdDDQLKGFFVSSLAADIDANPLTSEGVFVYFADI--DVNVGDHVRVQGTVEEYFDATQIGSVSQVAVCGTG 310
Cdd:NF033681    2 EGVVTAVP--TGGLNGFYLQTPGTDGDGNPATSDGLFVYTGAAvtDVAVGDRVRVTGTVSEYYGLTQLSAVSAVEVCGTG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 311 LAAAATKITLPLADTTDLEAFEGMLVTLEQPLVVTNNFGLGRYGEVELAT-ERLYQGTQVALPG-DAANAVETENLLKKI 388
Cdd:NF033681   80 AAVTPTPLTLPVDEALRLERYEGMLVRLPQDLTVTDNYNLGRYGELVLSAgGRLLQPTQVAAPGsAEAAALAAANAARRI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 389 LLDDGSTGQNLDPTAYPtPGLSAENTLRTGDTVNTVTGALAYSFSLYRIHPT---VAPSFIATNARENAPELnAEADLRV 465
Cdd:NF033681  160 VLDDGSTAQNPGPVPYY-PGLSADNTLRVGDTVTGLTGVLDYRFGAYRLQPTngaTAPDFVPANPRPAAPAL-VGGDLRV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 466 ASFNVLNYFNGDGQGGG--FPTARGADSEAEFTRQEAKIVSAISAIQADVVGLMEIENDGFGEFSAIASLVDALNDADSA 543
Cdd:NF033681  238 ASFNVLNYFNGDGFGGPadFPTNRGADTAAEFERQQAKIVAAINALDADVVGLMEIENNGYGRDSAIADLVDALNAAAGG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 544 NNYAFVD-FNVGQIGTDAITTALIYRANKVEEVGTAAITTEAPFDFSNRAPIAQSFKSLETDEVFTVAVSHLKSKSCGSA 622
Cdd:NF033681  318 GTYAYVPsPGTDPLGTDAIRVALIYRPAKVTPVGDAAILDDPAFDGSNRPPLAQTFRPKGGGETFTVVVNHFKSKGSGCA 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 623 SGNNaDSGDGQGCWNEIRTEGANAFANWLDSKPTGVDDEDTILVGDMNAYAMEDPIRAFADKGYKNVVAEIDGDTlGYSY 702
Cdd:NF033681  398 SGDD-DQGDGQGCWNATRVAAAQALADWLATLPTGVGDGDVLLLGDLNAYAKEDPIRVLTDAGYTNLVARFHGDD-AYSY 475
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1311712405 703 SFSGRAGSLDHAVATQSLLSKIVAATDWHINADEPISLDYNVEFKSEgqqSSLYSESAYRASDHDPVIIDIK 774
Cdd:NF033681  476 VFGGESGSLDHALASPSLAAKVVGATDWHINADEPTALDYNTEYKGA---ADLYAPDPYRSSDHDPVIVGLD 544
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
423-774 7.14e-92

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 295.01  E-value: 7.14e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 423 TVTGALaysFSLYRIhptvaPSFIATNARENAPelnAEADLRVASFNVLNYFNGDGQGGGFptARGADSEAEFTRQEAKI 502
Cdd:COG2374    40 GLTGVL---FGNYRQ-----PTETFVNPRPEAP---VGGDLRVATFNVENLFDTDDDDDDF--GRGADTPEEYERKLAKI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 503 VSAISAIQADVVGLMEIENDGfgefSAIASLVDALNDAdsANNYAFVDFNVGQIGtDAITTALIYRANKVEEVGTAAI-- 580
Cdd:COG2374   107 AAAIAALDADIVGLQEVENNG----SALQDLVAALNLA--GGTYAFVHPPDGPDG-DGIRVALLYRPDRVTLVGSATIad 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 581 TTEAPF--DFSNRAPIAQSFKsLETDEVFTVAVSHLKSKSCGsasgnnaDSGDGQGCWNEIRTEGANAFANWLDSKPTGV 658
Cdd:COG2374   180 LPDSPGnpDRFSRPPLAVTFE-LANGEPFTVIVNHFKSKGSD-------DPGDGQGASEAKRTAQAEALRAFVDSLLAAD 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 659 DDEDTILVGDMNAYAMEDPIRAF-ADKGYKNVVAEIDGDTlGYSYSFSGRAGSLDHAVATQSLLSKIVAATDWHINADep 737
Cdd:COG2374   252 PDAPVIVLGDFNDYPFEDPLRALlGAGGLTNLAEKLPAAE-RYSYVYDGNSGLLDHILVSPALAARVTGADIWHINAD-- 328
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1311712405 738 islDYNVEFKSEGqqsSLYSESAYRASDHDPVIIDIK 774
Cdd:COG2374   329 ---IYNDDFKPDF---RTYADDPGRASDHDPVVVGLR 359
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
463-773 1.33e-52

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: 184.91  E-value: 1.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 463 LRVASFNVLNYFNGDGQgggfptargadseaEFTRQEAKIVSAISAiqaDVVGLMEIENDGfGEFSAIASLVDALNDADS 542
Cdd:cd10283     1 LRIASWNILNFGNSKGK--------------EKNPAIAEIISAFDL---DLIALQEVMDNG-GGLDALAKLVNELNKPGG 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 543 ANNYAFVDFNVGQIGtDAITTALIYRANKVEEVGTAAITTEAPFDFSNRAPIAQSFKSLETDEVFTVAVSHLKSKScGSA 622
Cdd:cd10283    63 TWKYIVSDKTGGSSG-DKERYAFLYKSSKVRKVGKAVLEKDSNTDGFARPPYAAKFKSGGTGFDFTLVNVHLKSGG-SSK 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 623 SGNNADsgdgqgcwneiRTEGANAFANWLDSKPTGVDDEDTILVGDMNAYAMEDPIRAFADKGYKNVVAeidgDTLGYSY 702
Cdd:cd10283   141 SGQGAK-----------RVAEAQALAEYLKELADEDPDDDVILLGDFNIPADEDAFKALTKAGFKSLLP----DSTNLST 205
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1311712405 703 SFSGRAGSLDHAVATQSLLSKIVAA--TDWHINADEPISLDYNvefksegqqsslYSESAYRASDHDPVIIDI 773
Cdd:cd10283   206 SFKGYANSYDNIFVSGNLKEKFSNSgvFDFNILVDEAGEEDLD------------YSKWRKQISDHDPVWVEF 266
YhcR_OBF_like cd04486
YhcR_OBF_like: A subfamily of OB-fold domains similar to the OB folds of Bacillus subtilis ...
233-310 6.87e-23

YhcR_OBF_like: A subfamily of OB-fold domains similar to the OB folds of Bacillus subtilis YhcR. YhcR is a sugar-nonspecific nuclease, which is active in the presence of Ca2+ and Mn2+. It cleaves RNA endonucleolytically, producing 3'-monophosphate nucleosides. YhcR appears to be the major Ca2+ activated nuclease of B. subtilis. YhcR may be localized in the cell wall.


Pssm-ID: 239932 [Multi-domain]  Cd Length: 78  Bit Score: 93.09  E-value: 6.87e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1311712405 233 EGIVTADFQDDdQLKGFFVSSLAADidANPLTSEGVFVYFADI-DVNVGDHVRVQGTVEEYFDATQIGSVSQVAVCGTG 310
Cdd:cd04486     3 EGVVTAVFSGG-GLGGFYIQDEDGD--GDPATSEGIFVYTGSGaDVAVGDLVRVTGTVTEYYGLTQLTAVSAIEVLGSG 78
LTD pfam00932
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ...
18-126 2.75e-14

Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.


Pssm-ID: 460003 [Multi-domain]  Cd Length: 108  Bit Score: 69.76  E-value: 2.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405  18 APASADLIISEYIEGSS--NNKAIELYNNAPTSIVLDGYTLGLYSNGSDTVGNSIaltgELAANTTYVIANSGAIEDILS 95
Cdd:pfam00932   1 SSATGDVVISEVVYDGSggNDEFIELYNTGSKAVDLSGWKLQDASGGTYTFPNGT----TLAPGQTVVVWTGSGTNSATA 76
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1311712405  96 ISDTTSTVTFYNGDDALVLTK-DGIVVDSFGQ 126
Cdd:pfam00932  77 GYWGPSNAVWNNGGDAVALYDaNGELVDSVGY 108
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
793-887 1.81e-08

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 52.70  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 793 VFAVDENSAIGTIIGTLDFSDPNADESPVVKF-ITSDNDS--VSINNQ-GQLIVAGEIDYEFENRITLTVQAQDSVGN-L 867
Cdd:cd11304     3 EVSVPENAPPGTVVLTVSATDPDSGENGEVTYsIVSGNEDglFSIDPStGEITTAKPLDREEQSSYTLTVTATDGGGPpL 82
                          90       100
                  ....*....|....*....|
gi 1311712405 868 SNVEKVAVKVNnlrsdDDND 887
Cdd:cd11304    83 SSTATVTITVL-----DVND 97
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
464-773 8.81e-07

Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, 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: 197317 [Multi-domain]  Cd Length: 252  Bit Score: 51.06  E-value: 8.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 464 RVASFNVLNYFNGDGqgggfptargADSEAEftRQEAkIVSAISAIQADVVGLMEIendgfgefsaiasLVDALNDADSA 543
Cdd:cd09083     1 RVMTFNIRYDNPSDG----------ENSWEN--RKDL-VAELIKFYDPDIIGTQEA-------------LPHQLADLEEL 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 544 -NNYAFVDFnvgqiGTDA-----ITTALIYRANKVE--EVGT----------------AA---ITTEApfdfsnrapiaq 596
Cdd:cd09083    55 lPEYDWIGV-----GRDDgkekgEFSAIFYRKDRFEllDSGTfwlsetpdvvgskgwdAAlprICTWA------------ 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 597 SFKSLETDEVFTVAVSHLkskscgsasgnnadsgDGQGcwNEIRTEGANAFANWLDSKPtgvDDEDTILVGDMNAYAMED 676
Cdd:cd09083   118 RFKDKKTGKEFYVFNTHL----------------DHVG--EEAREESAKLILERIKEIA---GDLPVILTGDFNAEPDSE 176
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 677 PIRAFADKGYK--NVVAEIDGDTLGYSY-SFSGRAGS--LDHAvatqsLLSKIVAATDWHINADepisldynvefksegq 751
Cdd:cd09083   177 PYKTLTSGGLKdaRDTAATTDGGPEGTFhGFKGPPGGsrIDYI-----FVSPGVKVLSYEILTD---------------- 235
                         330       340
                  ....*....|....*....|..
gi 1311712405 752 qsslySESAYRASDHDPVIIDI 773
Cdd:cd09083   236 -----RYDGRYPSDHFPVVADL 252
Deadenylase_nocturnin cd09096
C-terminal deadenylase domain of nocturnin and related domains; This subfamily contains the ...
564-682 2.03e-06

C-terminal deadenylase domain of nocturnin and related domains; This subfamily contains the C-terminal catalytic domain of the deadenylase, nocturnin, and related domains. Nocturnin is a poly(A)-specific 3' exonuclease that specifically degrades the 3' poly(A) tail of RNA in a process known as deadenylation. This nuclease activity is manganese dependent. Nocturnin is expressed in the cytoplasm of Xenopus laevis retinal photoreceptor cells in a rhythmic fashion, and it has been proposed that it participates in posttranscriptional regulation of the circadian clock or its outputs, and that the mRNA target(s) of this deadenylase are circadian clock-related. In mouse, the nocturnin gene, mNoc, is expressed in a circadian pattern in a range of tissues including retina, spleen, heart, kidney, and liver. It is highly expressed in bone-marrow stromal cells, adipocytes and hepatocytes. In mammals, nocturnin plays a role in regulating mesenchymal stem-cell lineage allocation, perhaps through regulating PPAR-gamma (peroxisome proliferator-activated receptor-gamma) nuclear translocation. 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: 197330 [Multi-domain]  Cd Length: 280  Bit Score: 50.50  E-value: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 564 ALIYRANKVEEVGTAAITTEAPFDFSNRAPIAQSFKSLETDEVFTVAVSHLKSKscgsasgnnadsgdgQGcWNEIRTEG 643
Cdd:cd09096    94 ALFFRKDRFELVNTEKIRLSAMTLKTNQVAIACTLRCKETGREICLAVTHLKAR---------------TG-WERLRSEQ 157
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1311712405 644 ANAFANWLDSKpTGVDDEDTILVGDMNAYAMEDPIRAFA 682
Cdd:cd09096   158 GKDLLQNLQSF-IEGAKIPLIICGDFNAEPTEPVYKTFS 195
Cadherin pfam00028
Cadherin domain;
792-877 3.23e-05

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 43.44  E-value: 3.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405 792 QVFAVDENSAIGTIIGTLDFSDPN-ADESPVVKFITSDN--DSVSINNQ-GQLIVAGEIDYEFENRITLTVQAQDSVG-N 866
Cdd:pfam00028   1 YSASVPENAPVGTEVLTVTATDPDlGPNGRIFYSILGGGpgGNFRIDPDtGDISTTKPLDRESIGEYELTVEATDSGGpP 80
                          90
                  ....*....|.
gi 1311712405 867 LSNVEKVAVKV 877
Cdd:pfam00028  81 LSSTATVTITV 91
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
812-887 6.33e-03

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 36.56  E-value: 6.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1311712405  812 SDPNADESPVVKF-ITSDNDS--VSIN-NQGQLIVAGEIDYEFENRITLTVQAQDSVG-NLSNVEKVAVKVNnlrsdDDN 886
Cdd:smart00112   3 TDADSGENGKVTYsILSGNDDglFSIDpETGEITTTKPLDREEQPEYTLTVEATDGGGpPLSSTATVTITVL-----DVN 77

                   .
gi 1311712405  887 D 887
Cdd:smart00112  78 D 78
 
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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