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Conserved domains on  [gi|1011726731|ref|WP_062570469|]
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endonuclease/exonuclease/phosphatase family protein [Pseudoalteromonas arabiensis]

Protein Classification

endonuclease/exonuclease/phosphatase family protein( domain architecture ID 11457186)

endonuclease/exonuclease/phosphatase (EEP) family protein is among a diverse set of enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins

CATH:  3.60.10.10
EC:  3.1.-.-
Gene Ontology:  GO:0046872|GO:0016787|GO:0003677
PubMed:  10838565
SCOP:  4002213

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
2-338 1.49e-39

Predicted extracellular nuclease [General function prediction only];


:

Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 142.85  E-value: 1.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731   2 IKHNQIKVATFNLYNYLAPPNAFYDFQR-IYSAQQWAKKQRWLADYLENQQPDIIGFQEVFS----IDALKQQVSEQGYP 76
Cdd:COG2374    64 PVGGDLRVATFNVENLFDTDDDDDDFGRgADTPEEYERKLAKIAAAIAALDADIVGLQEVENngsaLQDLVAALNLAGGT 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731  77 YFAVVDeptiIDEFIYRDPVVAIASR---FKIVAVAKVEYDTDYAAQMGLkgfcFSRDIVRATIDVPHIGIVDCYVLHFK 153
Cdd:COG2374   144 YAFVHP----PDGPDGDGIRVALLYRpdrVTLVGSATIADLPDSPGNPDR----FSRPPLAVTFELANGEPFTVIVNHFK 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731 154 SKRSmidneyddtsteqqnllkqlKDQVAGRWASSIQRGSEAAL---FLIEVinRRAQTNNPVIVMGDFNNELHDGVLNH 230
Cdd:COG2374   216 SKGS--------------------DDPGDGQGASEAKRTAQAEAlraFVDSL--LAADPDAPVIVLGDFNDYPFEDPLRA 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731 231 LIADNSrltenrqnsvyrshftlqdswqLYQRHVVTESDREATHYFGSSSSVFDYILLSREFDAGFHSSFFEVVDYHTYD 310
Cdd:COG2374   274 LLGAGG----------------------LTNLAEKLPAAERYSYVYDGNSGLLDHILVSPALAARVTGADIWHINADIYN 331
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1011726731 311 QHLINPQFAYDD---QSTDHGVVMITMALRS 338
Cdd:COG2374   332 DDFKPDFRTYADdpgRASDHDPVVVGLRLPP 362
 
Name Accession Description Interval E-value
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
2-338 1.49e-39

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 142.85  E-value: 1.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731   2 IKHNQIKVATFNLYNYLAPPNAFYDFQR-IYSAQQWAKKQRWLADYLENQQPDIIGFQEVFS----IDALKQQVSEQGYP 76
Cdd:COG2374    64 PVGGDLRVATFNVENLFDTDDDDDDFGRgADTPEEYERKLAKIAAAIAALDADIVGLQEVENngsaLQDLVAALNLAGGT 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731  77 YFAVVDeptiIDEFIYRDPVVAIASR---FKIVAVAKVEYDTDYAAQMGLkgfcFSRDIVRATIDVPHIGIVDCYVLHFK 153
Cdd:COG2374   144 YAFVHP----PDGPDGDGIRVALLYRpdrVTLVGSATIADLPDSPGNPDR----FSRPPLAVTFELANGEPFTVIVNHFK 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731 154 SKRSmidneyddtsteqqnllkqlKDQVAGRWASSIQRGSEAAL---FLIEVinRRAQTNNPVIVMGDFNNELHDGVLNH 230
Cdd:COG2374   216 SKGS--------------------DDPGDGQGASEAKRTAQAEAlraFVDSL--LAADPDAPVIVLGDFNDYPFEDPLRA 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731 231 LIADNSrltenrqnsvyrshftlqdswqLYQRHVVTESDREATHYFGSSSSVFDYILLSREFDAGFHSSFFEVVDYHTYD 310
Cdd:COG2374   274 LLGAGG----------------------LTNLAEKLPAAERYSYVYDGNSGLLDHILVSPALAARVTGADIWHINADIYN 331
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1011726731 311 QHLINPQFAYDD---QSTDHGVVMITMALRS 338
Cdd:COG2374   332 DDFKPDFRTYADdpgRASDHDPVVVGLRLPP 362
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
36-221 1.37e-09

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; 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: 197318 [Multi-domain]  Cd Length: 246  Bit Score: 57.69  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731  36 WAKKQRWLADYLENQQPDIIGFQEvFSIDALKQQVSEQ----GYPYFAVVDEPTIIDEFIyrdpvvAIASRFKIVAVAKV 111
Cdd:cd09084    14 WKDDPDKILDFIKKQDPDILCLQE-YYGSEGDKDDDLRlllkGYPYYYVVYKSDSGGTGL------AIFSKYPILNSGSI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731 112 EYDTDYAAqmglkgfcfsrdIVRATIDVPhiG-IVDCYVLHFkskRSMIDNEYDDTSTEQQNLLKQLKDQVAGRWASSIQ 190
Cdd:cd09084    87 DFPNTNNN------------AIFADIRVG--GdTIRVYNVHL---ESFRITPSDKELYKEEKKAKELSRNLLRKLAEAFK 149
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1011726731 191 RGSEAALFLIEVINRraqTNNPVIVMGDFNN 221
Cdd:cd09084   150 RRAAQADLLAADIAA---SPYPVIVCGDFND 177
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
10-220 1.35e-07

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: 51.07  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731  10 ATFNLYNYLAPpnafydfqriysAQQWAKKQRWLADYLENQQPDIIGFQEVFSIDALKQQVSEQGYPYFAvvdePTIIDE 89
Cdd:pfam03372   1 LTWNVNGGNAD------------AAGDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFL----SYGGPG 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731  90 FIYRDPVVAIASRFKIVAVAKVEYDTDYAAQMGLKGFCFSRDIVRATIDVPHIgivdcyvlhfkskrsmidneyddtste 169
Cdd:pfam03372  65 GGGGGGGVAILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAP--------------------------- 117
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1011726731 170 qqnllkqlkdqvagRWASSIQRGSEAALFLIEVINRRAQTNNPVIVMGDFN 220
Cdd:pfam03372 118 --------------HASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFN 154
 
Name Accession Description Interval E-value
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
2-338 1.49e-39

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 142.85  E-value: 1.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731   2 IKHNQIKVATFNLYNYLAPPNAFYDFQR-IYSAQQWAKKQRWLADYLENQQPDIIGFQEVFS----IDALKQQVSEQGYP 76
Cdd:COG2374    64 PVGGDLRVATFNVENLFDTDDDDDDFGRgADTPEEYERKLAKIAAAIAALDADIVGLQEVENngsaLQDLVAALNLAGGT 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731  77 YFAVVDeptiIDEFIYRDPVVAIASR---FKIVAVAKVEYDTDYAAQMGLkgfcFSRDIVRATIDVPHIGIVDCYVLHFK 153
Cdd:COG2374   144 YAFVHP----PDGPDGDGIRVALLYRpdrVTLVGSATIADLPDSPGNPDR----FSRPPLAVTFELANGEPFTVIVNHFK 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731 154 SKRSmidneyddtsteqqnllkqlKDQVAGRWASSIQRGSEAAL---FLIEVinRRAQTNNPVIVMGDFNNELHDGVLNH 230
Cdd:COG2374   216 SKGS--------------------DDPGDGQGASEAKRTAQAEAlraFVDSL--LAADPDAPVIVLGDFNDYPFEDPLRA 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731 231 LIADNSrltenrqnsvyrshftlqdswqLYQRHVVTESDREATHYFGSSSSVFDYILLSREFDAGFHSSFFEVVDYHTYD 310
Cdd:COG2374   274 LLGAGG----------------------LTNLAEKLPAAERYSYVYDGNSGLLDHILVSPALAARVTGADIWHINADIYN 331
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1011726731 311 QHLINPQFAYDD---QSTDHGVVMITMALRS 338
Cdd:COG2374   332 DDFKPDFRTYADdpgRASDHDPVVVGLRLPP 362
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
3-221 1.64e-10

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


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 59.15  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731   3 KHNQIKVATFNLYNYLAPPNAFyDFQRIysaqqwakkqrwlADYLENQQPDIIGFQEvfsidalkqqvseqgypyfavvd 82
Cdd:COG3568     4 AAATLRVMTYNIRYGLGTDGRA-DLERI-------------ARVIRALDPDVVALQE----------------------- 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731  83 eptiidefiyrdpvVAIASRFKIVAVAKVEYDTDYAAQmglkgfcfsRDIVRATIDVPHiGIVDCYVLHFKskrsmidne 162
Cdd:COG3568    47 --------------NAILSRYPIVSSGTFDLPDPGGEP---------RGALWADVDVPG-KPLRVVNTHLD--------- 93
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1011726731 163 yddtsteqqnllkqlkdqvagrWASSIQRGSEAALfLIEVINRRAqTNNPVIVMGDFNN 221
Cdd:COG3568    94 ----------------------LRSAAARRRQARA-LAELLAELP-AGAPVILAGDFND 128
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
36-221 1.37e-09

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; 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: 197318 [Multi-domain]  Cd Length: 246  Bit Score: 57.69  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731  36 WAKKQRWLADYLENQQPDIIGFQEvFSIDALKQQVSEQ----GYPYFAVVDEPTIIDEFIyrdpvvAIASRFKIVAVAKV 111
Cdd:cd09084    14 WKDDPDKILDFIKKQDPDILCLQE-YYGSEGDKDDDLRlllkGYPYYYVVYKSDSGGTGL------AIFSKYPILNSGSI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731 112 EYDTDYAAqmglkgfcfsrdIVRATIDVPhiG-IVDCYVLHFkskRSMIDNEYDDTSTEQQNLLKQLKDQVAGRWASSIQ 190
Cdd:cd09084    87 DFPNTNNN------------AIFADIRVG--GdTIRVYNVHL---ESFRITPSDKELYKEEKKAKELSRNLLRKLAEAFK 149
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1011726731 191 RGSEAALFLIEVINRraqTNNPVIVMGDFNN 221
Cdd:cd09084   150 RRAAQADLLAADIAA---SPYPVIVCGDFND 177
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
5-220 5.05e-08

Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily [General function prediction only];


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 53.46  E-value: 5.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731   5 NQIKVATFNLYNYLAPPNAfydfqriysaqqwakkqrwLADYLENQQPDIIGFQEVfsIDALKQQVS--EQGYPYFAVVD 82
Cdd:COG3021    93 PDLRVLTANVLFGNADAEA-------------------LAALVREEDPDVLVLQET--TPAWEEALAalEADYPYRVLCP 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731  83 EPTIIDefiyrdpvVAIASRFKIVAVAKVEYDTDYAAQmglkgfcfsrdiVRATIDVPHiGIVDCYVLHFKSKRsmidne 162
Cdd:COG3021   152 LDNAYG--------MALLSRLPLTEAEVVYLVGDDIPS------------IRATVELPG-GPVRLVAVHPAPPV------ 204
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1011726731 163 ydDTSTEQQNLLKQLKDQVAGRwassiqrgseaalflievinrraqtNNPVIVMGDFN 220
Cdd:COG3021   205 --GGSAERDAELAALAKAVAAL-------------------------DGPVIVAGDFN 235
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
9-312 7.42e-08

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: 52.48  E-value: 7.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731   9 VATFNLYNYLAPPNAFYdfqriysaqqWAKKQRWLAdylenqqPDIIGFQEVF----SIDALKQQVSEQGYPYFAVVDEP 84
Cdd:cd08372     1 VASYNVNGLNAATRASG----------IARWVRELD-------PDIVCLQEVKdsqySAVALNQLLPEGYHQYQSGPSRK 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731  85 TIidefiyrDPVVAIASRFKIVAVAKVEYDTDYaaqmglKGFCFSRDIVRATIDVpHIGIVDCYVLHFKSkrsmIDNEYD 164
Cdd:cd08372    64 EG-------YEGVAILSKTPKFKIVEKHQYKFG------EGDSGERRAVVVKFDV-HDKELCVVNAHLQA----GGTRAD 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731 165 DTSTEQQNLLKQLKdqvagrwassiqrgseaalflieviNRRAQTNNPVIVMGDFNNELHDGVLNHLIADNSRLTENRQN 244
Cdd:cd08372   126 VRDAQLKEVLEFLK-------------------------RLRQPNSAPVVICGDFNVRPSEVDSENPSSMLRLFVALNLV 180
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731 245 SVYRsHFTLQDSWQLYQRHVvtesdreathyfgssSSVFDYILLSREFDAGFHSS--FFEVVDYHTYDQH 312
Cdd:cd08372   181 DSFE-TLPHAYTFDTYMHNV---------------KSRLDYIFVSKSLLPSVKSSkiLSDAARARIPSDH 234
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
10-220 1.35e-07

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: 51.07  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731  10 ATFNLYNYLAPpnafydfqriysAQQWAKKQRWLADYLENQQPDIIGFQEVFSIDALKQQVSEQGYPYFAvvdePTIIDE 89
Cdd:pfam03372   1 LTWNVNGGNAD------------AAGDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFL----SYGGPG 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731  90 FIYRDPVVAIASRFKIVAVAKVEYDTDYAAQMGLKGFCFSRDIVRATIDVPHIgivdcyvlhfkskrsmidneyddtste 169
Cdd:pfam03372  65 GGGGGGGVAILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVPLVLTLAP--------------------------- 117
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1011726731 170 qqnllkqlkdqvagRWASSIQRGSEAALFLIEVINRRAQTNNPVIVMGDFN 220
Cdd:pfam03372 118 --------------HASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFN 154
RgfB-like cd09079
Streptococcus agalactiae RgfB, part of a putative two component signal transduction system, ...
35-230 6.05e-07

Streptococcus agalactiae RgfB, part of a putative two component signal transduction system, and related proteins; This family includes Streptococcus agalactiae RgfB (for regulator of fibrinogen binding) and related proteins. The function of RgfB is unknown. It is part of a putative two component signal transduction system designated rgfBDAC (the rgf locus was identified in a screen for mutants of Streptococcus agalactiae with altered binding to fibrinogen). RgfA,-C,and -D do not belong to this superfamily: rgfA encodes a putative response regulator, and rgfC, a putative histidine kinase. All four genes are co-transcribed, and may be involved in regulating expression of bacterial cell surface components. 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: 197313 [Multi-domain]  Cd Length: 259  Bit Score: 49.95  E-value: 6.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731  35 QWAKKQRwLADYLENQQPDIIGFQEVF-SIDALKQQVS---------------EQGYPYFAVVDEPTI-IDEFiyrDPVV 97
Cdd:cd09079    14 QKEKLER-LAKIIAEEDYDVIALQEVNqSIDAPVSQVPikednfalllyeklrELGATYYWTWILSHIgYDKY---DEGL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731  98 AIASRFKIVA-----VAKVEYDTDYAaqmglkgfcfSRDIVRATIDVPHiGIVDCYVLHFkskrsmidNEYDDTSTEQQN 172
Cdd:cd09079    90 AILSKRPIAEvedfyVSKSQDYTDYK----------SRKILGATIEING-QPIDVYSCHL--------GWWYDEEEPFAY 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1011726731 173 LLKQLkdqvagrwassiqrgseaalflievINRRAQTNNPVIVMGDFNNElhDGVLNH 230
Cdd:cd09079   151 EWSKL-------------------------EKALAEAGRPVLLMGDFNNP--AGSRGE 181
nSMase cd09078
Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological ...
7-140 1.86e-04

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: 42.71  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011726731   7 IKVATFNLYnYLAPPnafydfqrIYSAQQWAKKQRwlADYL--ENQQPDIIGFQEVFS---IDALKQQ-VSEQGYPYFAV 80
Cdd:cd09078     1 LKVLTYNVF-LLPPL--------LYNNGDDGQDER--LDLIpkALLQYDVVVLQEVFDaraRKRLLNGlKKEYPYQTDVV 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1011726731  81 VDEPTIIDEFIYrDPVVAIASRFKIVAVAKVEYD----TDYAAQmglKGFcfsrdiVRATIDVP 140
Cdd:cd09078    70 GRSPSGWSSKLV-DGGVVILSRYPIVEKDQYIFPngcgADCLAA---KGV------LYAKINKG 123
 
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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