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Conserved domains on  [gi|446687804|ref|WP_000765150|]
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MULTISPECIES: exonuclease SbcCD subunit D [Bacillus]

Protein Classification

exonuclease SbcCD subunit D( domain architecture ID 11417993)

exonuclease SbcCD subunit D is a component of SbcCD, which is involved in double-strand DNA break detection and repair by homologous recombination and non-homologous end joining of damaged DNA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
1-275 7.42e-79

DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];


:

Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 242.90  E-value: 7.42e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804   1 MKLFHTADWHLGKLVHGVYMTEDQKIVLDQFVQAVEEEKPDAVIIAGDLYDRAIPPTEAVDLLNDVLQKIViDLQTPVIA 80
Cdd:COG0420    1 MRFLHTADWHLGKPLHGASRREDQLAALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRLS-EAGIPVVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804  81 VAGNHDSPDRIHFGSSLMKKQGLHIAGqfQFPYEPVVLNDEYGeVHFHLIPYADPSIvrhvlknedvrshDDAMRIFMNE 160
Cdd:COG0420   80 IAGNHDSPSRLSAGSPLLENLGVHVFG--SVEPEPVELEDGLG-VAVYGLPYLRPSD-------------EEALRDLLER 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804 161 LSETMDKEARHVFVGHAFVTSSGEaeentsdaERPLSIggaEYVNSHYF--DKFHYTALGHLHQAHFVR-NETIRYSGSP 237
Cdd:COG0420  144 LPRALDPGGPNILLLHGFVAGASG--------SRDIYV---APVPLSALpaAGFDYVALGHIHRPQVLGgDPRIRYSGSP 212

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 446687804 238 LAYSISEEkHKKGYYIVELNETGEVAIEKRLLSPRRKM 275
Cdd:COG0420  213 EPRSFSEA-GGKGVLLVELDAGGLVSVEFVPLPATRRF 249
SbcD_C pfam12320
Type 5 capsule protein repressor C-terminal domain; This domain is found in bacteria and ...
 271-357 7.32e-10

Type 5 capsule protein repressor C-terminal domain; This domain is found in bacteria and archaea. This domain is about 90 amino acids in length. This domain is found associated with pfam00149. SbcD works in complex with SbdC (SbcDC) which is a transcription regulator. It down-regulates transcription of arl and mgr to inhibit type 5 capsule protein production. It acts as part of the SOS pathway of bacteria.


:

Pssm-ID: 463533  Cd Length: 100  Bit Score: 55.77  E-value: 7.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804  271 PRRKMRTVEAKIDELLQHPV--------SEDYVFVKLLDENPVLQPMEKIRSVYPNA----MHVERAMQRRELTDTNEVT 338
Cdd:pfam12320   1 PLRDLRRIKGSLEELLAALAyleeepadREDYLEVELTDEEPIPDLMERLREAYPNIpvelLRIRRTREERQAEEEEEAA 80

                          90
                  ....*....|....*....
gi 446687804  339 VSRHKTDDLSLLKAFYKEM 357
Cdd:pfam12320  81 EDLEELSPLELFERFYEEQ 99
 
Name Accession Description Interval E-value
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
1-275 7.42e-79

DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 242.90  E-value: 7.42e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804   1 MKLFHTADWHLGKLVHGVYMTEDQKIVLDQFVQAVEEEKPDAVIIAGDLYDRAIPPTEAVDLLNDVLQKIViDLQTPVIA 80
Cdd:COG0420    1 MRFLHTADWHLGKPLHGASRREDQLAALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRLS-EAGIPVVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804  81 VAGNHDSPDRIHFGSSLMKKQGLHIAGqfQFPYEPVVLNDEYGeVHFHLIPYADPSIvrhvlknedvrshDDAMRIFMNE 160
Cdd:COG0420   80 IAGNHDSPSRLSAGSPLLENLGVHVFG--SVEPEPVELEDGLG-VAVYGLPYLRPSD-------------EEALRDLLER 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804 161 LSETMDKEARHVFVGHAFVTSSGEaeentsdaERPLSIggaEYVNSHYF--DKFHYTALGHLHQAHFVR-NETIRYSGSP 237
Cdd:COG0420  144 LPRALDPGGPNILLLHGFVAGASG--------SRDIYV---APVPLSALpaAGFDYVALGHIHRPQVLGgDPRIRYSGSP 212

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 446687804 238 LAYSISEEkHKKGYYIVELNETGEVAIEKRLLSPRRKM 275
Cdd:COG0420  213 EPRSFSEA-GGKGVLLVELDAGGLVSVEFVPLPATRRF 249
sbcd TIGR00619
exonuclease SbcD; All proteins in this family for which functions are known are ...
 1-250 4.77e-44

exonuclease SbcD; All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273178 [Multi-domain]  Cd Length: 253  Bit Score: 152.96  E-value: 4.77e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804    1 MKLFHTADWHLGKLVHGVYMTEDQKIVLDQFVQAVEEEKPDAVIIAGDLYDRAIPPTEAVDLLNDVLQKIVIDLQTPVIA 80
Cdd:TIGR00619   1 MRILHTSDWHLGKTLEGVSRLAEQKAFLDDLLEFAKAEQVDALLVAGDVFDTANPPAEAQELFNAFFVNLSDTGIRPIVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804   81 VAGNHDSPDRIHFGSSLMKKQGLHIAGqfqFP-YEPVVLNDEYGEVHFHLIPYADPSIVRHVL--------KNEDVRSH- 150
Cdd:TIGR00619  81 ISGNHDSAQRLSAAKKLLAELGVFVVG---SPgHDPQILLLKDGTNGEGLCVGLFLLPREAILtragldgfGLELLLAHt 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804  151 DDAMRIFMNELSETMDKEARHVFVGHAFVTSSGEaeentSDAERPLSIGGAEYVNSHYFDKFHYTALGHLHQAHFVR-NE 229
Cdd:TIGR00619 158 DVKLRQAAEALKLRLDQDLPKILLAHLFTAGATK-----SDAERRIYIGTLYAFPLQNFPEADYIALGHIHIHKISKgRE 232

                         250       260
                  ....*....|....*....|.
gi 446687804  230 TIRYSGSPLAYSISEEKHKKG 250
Cdd:TIGR00619 233 RVRYSGSPFPLSFDEAGKDKY 253
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 2-243 8.47e-38

Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277319 [Multi-domain]  Cd Length: 186  Bit Score: 134.70  E-value: 8.47e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804   2 KLFHTADWHLGKLVHG-VYMTEDQKIVLDQFVQAVEEEKPDAVIIAGDLYDRAIPPTEAVDLLNDVLQKIViDLQTPVIA 80
Cdd:cd00840    1 RFLHTADWHLGYPLYGlSRREEDFFKAFEEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLRRLC-EAGIPVFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804  81 VAGNHDSPDRihfgsslmkkqglhiagqfqfpyepvvlndeygeVHFHLIPYADPSIVRHVLKNEDVRSHDDamrifmne 160
Cdd:cd00840   80 IAGNHDSPAR----------------------------------VAIYGLPYLRDERLERLFEDLELRPRLL-------- 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804 161 lsetmDKEARHVFVGHAFVTSSGEaeentSDAERPLSIGGAEyvnshyFDKFHYTALGHLH--QAHFVRNETIRYSGSPL 238
Cdd:cd00840  118 -----KPDWFNILLLHQGVDGAGP-----SDSERPIVPEDLL------PDGFDYVALGHIHkpQIIEGGGPPIVYPGSPE 181


                 ....*
gi 446687804 239 AYSIS 243
Cdd:cd00840  182 PTSFS 186
PRK10966 PRK10966
exonuclease subunit SbcD; Provisional
 1-265 5.78e-25

exonuclease subunit SbcD; Provisional


Pssm-ID: 182871 [Multi-domain]  Cd Length: 407  Bit Score: 105.02  E-value: 5.78e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804   1 MKLFHTADWHLGKLVHGVYMTEDQKIVLDQFVQAVEEEKPDAVIIAGDLYDRAIPPTEAVDLLNDvlqkIVIDLQ---TP 77
Cdd:PRK10966   1 MRILHTSDWHLGQNFYSKSRAAEHQAFLDWLLEQVQEHQVDAIIVAGDIFDTGSPPSYARELYNR----FVVNLQqtgCQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804  78 VIAVAGNHDSPDRIHFGSSLMKKQGLH-IAGQFQFP-YEPVVLNDEYGEVHFHL--IPYADPsivRHVLKNEDVRSHDDA 153
Cdd:PRK10966  77 LVVLAGNHDSVATLNESRDLLAFLNTTvIASASDDLgHQVIILPRRDGTPGAVLcaIPFLRP---RDVITSQAGQSGIEK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804 154 M------------RIF--MNELSETMDKEARHVFVGHafVTSSGEAeenTSDAERPLSIGGAEYVNSHYFDKFHYTALGH 219
Cdd:PRK10966 154 QqalqaaiadhyqQLYqlACELRDELGQPLPIIATGH--LTTVGAS---KSDSVRDIYIGTLDAFPAQAFPPADYIALGH 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 446687804 220 LHQAHFV-RNETIRYSGSPLAYSISEEKHKKGYYIVELNETGEVAIE 265
Cdd:PRK10966 229 IHRAQKVgGTEHIRYSGSPIPLSFDELGKSKSVHLVEFDQGKLQSVT 275
SbcD_C pfam12320
Type 5 capsule protein repressor C-terminal domain; This domain is found in bacteria and ...
 271-357 7.32e-10

Type 5 capsule protein repressor C-terminal domain; This domain is found in bacteria and archaea. This domain is about 90 amino acids in length. This domain is found associated with pfam00149. SbcD works in complex with SbdC (SbcDC) which is a transcription regulator. It down-regulates transcription of arl and mgr to inhibit type 5 capsule protein production. It acts as part of the SOS pathway of bacteria.


Pssm-ID: 463533  Cd Length: 100  Bit Score: 55.77  E-value: 7.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804  271 PRRKMRTVEAKIDELLQHPV--------SEDYVFVKLLDENPVLQPMEKIRSVYPNA----MHVERAMQRRELTDTNEVT 338
Cdd:pfam12320   1 PLRDLRRIKGSLEELLAALAyleeepadREDYLEVELTDEEPIPDLMERLREAYPNIpvelLRIRRTREERQAEEEEEAA 80

                          90
                  ....*....|....*....
gi 446687804  339 VSRHKTDDLSLLKAFYKEM 357
Cdd:pfam12320  81 EDLEELSPLELFERFYEEQ 99
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-117 1.13e-08

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 52.60  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804    1 MKLFHTADWHLgklvhgvymtEDQKIVLDQFVQAV-EEEKPDAVIIAGDLYDRAIPPTEAVDLLNDVLQKIvidlqtPVI 79
Cdd:pfam00149   1 MRILVIGDLHL----------PGQLDDLLELLKKLlEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYV------PVY 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 446687804   80 AVAGNHDSP--DRIHFGSSLMKKQGLHIAGQFQFPYEPVV 117
Cdd:pfam00149  65 LVRGNHDFDygECLRLYPYLGLLARPWKRFLEVFNFLPLA 104
 
Name Accession Description Interval E-value
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
1-275 7.42e-79

DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 242.90  E-value: 7.42e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804   1 MKLFHTADWHLGKLVHGVYMTEDQKIVLDQFVQAVEEEKPDAVIIAGDLYDRAIPPTEAVDLLNDVLQKIViDLQTPVIA 80
Cdd:COG0420    1 MRFLHTADWHLGKPLHGASRREDQLAALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRRLS-EAGIPVVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804  81 VAGNHDSPDRIHFGSSLMKKQGLHIAGqfQFPYEPVVLNDEYGeVHFHLIPYADPSIvrhvlknedvrshDDAMRIFMNE 160
Cdd:COG0420   80 IAGNHDSPSRLSAGSPLLENLGVHVFG--SVEPEPVELEDGLG-VAVYGLPYLRPSD-------------EEALRDLLER 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804 161 LSETMDKEARHVFVGHAFVTSSGEaeentsdaERPLSIggaEYVNSHYF--DKFHYTALGHLHQAHFVR-NETIRYSGSP 237
Cdd:COG0420  144 LPRALDPGGPNILLLHGFVAGASG--------SRDIYV---APVPLSALpaAGFDYVALGHIHRPQVLGgDPRIRYSGSP 212

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 446687804 238 LAYSISEEkHKKGYYIVELNETGEVAIEKRLLSPRRKM 275
Cdd:COG0420  213 EPRSFSEA-GGKGVLLVELDAGGLVSVEFVPLPATRRF 249
sbcd TIGR00619
exonuclease SbcD; All proteins in this family for which functions are known are ...
 1-250 4.77e-44

exonuclease SbcD; All proteins in this family for which functions are known are double-stranded DNA exonuclease (as part of a complex with SbcC homologs). This complex functions in the initiation of recombination and recombinational repair and is particularly important in regulating the stability of DNA sections that can form secondary structures. This family is likely homologous to the MRE11 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273178 [Multi-domain]  Cd Length: 253  Bit Score: 152.96  E-value: 4.77e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804    1 MKLFHTADWHLGKLVHGVYMTEDQKIVLDQFVQAVEEEKPDAVIIAGDLYDRAIPPTEAVDLLNDVLQKIVIDLQTPVIA 80
Cdd:TIGR00619   1 MRILHTSDWHLGKTLEGVSRLAEQKAFLDDLLEFAKAEQVDALLVAGDVFDTANPPAEAQELFNAFFVNLSDTGIRPIVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804   81 VAGNHDSPDRIHFGSSLMKKQGLHIAGqfqFP-YEPVVLNDEYGEVHFHLIPYADPSIVRHVL--------KNEDVRSH- 150
Cdd:TIGR00619  81 ISGNHDSAQRLSAAKKLLAELGVFVVG---SPgHDPQILLLKDGTNGEGLCVGLFLLPREAILtragldgfGLELLLAHt 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804  151 DDAMRIFMNELSETMDKEARHVFVGHAFVTSSGEaeentSDAERPLSIGGAEYVNSHYFDKFHYTALGHLHQAHFVR-NE 229
Cdd:TIGR00619 158 DVKLRQAAEALKLRLDQDLPKILLAHLFTAGATK-----SDAERRIYIGTLYAFPLQNFPEADYIALGHIHIHKISKgRE 232

                         250       260
                  ....*....|....*....|.
gi 446687804  230 TIRYSGSPLAYSISEEKHKKG 250
Cdd:TIGR00619 233 RVRYSGSPFPLSFDEAGKDKY 253
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 2-243 8.47e-38

Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277319 [Multi-domain]  Cd Length: 186  Bit Score: 134.70  E-value: 8.47e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804   2 KLFHTADWHLGKLVHG-VYMTEDQKIVLDQFVQAVEEEKPDAVIIAGDLYDRAIPPTEAVDLLNDVLQKIViDLQTPVIA 80
Cdd:cd00840    1 RFLHTADWHLGYPLYGlSRREEDFFKAFEEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLRRLC-EAGIPVFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804  81 VAGNHDSPDRihfgsslmkkqglhiagqfqfpyepvvlndeygeVHFHLIPYADPSIVRHVLKNEDVRSHDDamrifmne 160
Cdd:cd00840   80 IAGNHDSPAR----------------------------------VAIYGLPYLRDERLERLFEDLELRPRLL-------- 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804 161 lsetmDKEARHVFVGHAFVTSSGEaeentSDAERPLSIGGAEyvnshyFDKFHYTALGHLH--QAHFVRNETIRYSGSPL 238
Cdd:cd00840  118 -----KPDWFNILLLHQGVDGAGP-----SDSERPIVPEDLL------PDGFDYVALGHIHkpQIIEGGGPPIVYPGSPE 181


                 ....*
gi 446687804 239 AYSIS 243
Cdd:cd00840  182 PTSFS 186
PRK10966 PRK10966
exonuclease subunit SbcD; Provisional
 1-265 5.78e-25

exonuclease subunit SbcD; Provisional


Pssm-ID: 182871 [Multi-domain]  Cd Length: 407  Bit Score: 105.02  E-value: 5.78e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804   1 MKLFHTADWHLGKLVHGVYMTEDQKIVLDQFVQAVEEEKPDAVIIAGDLYDRAIPPTEAVDLLNDvlqkIVIDLQ---TP 77
Cdd:PRK10966   1 MRILHTSDWHLGQNFYSKSRAAEHQAFLDWLLEQVQEHQVDAIIVAGDIFDTGSPPSYARELYNR----FVVNLQqtgCQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804  78 VIAVAGNHDSPDRIHFGSSLMKKQGLH-IAGQFQFP-YEPVVLNDEYGEVHFHL--IPYADPsivRHVLKNEDVRSHDDA 153
Cdd:PRK10966  77 LVVLAGNHDSVATLNESRDLLAFLNTTvIASASDDLgHQVIILPRRDGTPGAVLcaIPFLRP---RDVITSQAGQSGIEK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804 154 M------------RIF--MNELSETMDKEARHVFVGHafVTSSGEAeenTSDAERPLSIGGAEYVNSHYFDKFHYTALGH 219
Cdd:PRK10966 154 QqalqaaiadhyqQLYqlACELRDELGQPLPIIATGH--LTTVGAS---KSDSVRDIYIGTLDAFPAQAFPPADYIALGH 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 446687804 220 LHQAHFV-RNETIRYSGSPLAYSISEEKHKKGYYIVELNETGEVAIE 265
Cdd:PRK10966 229 IHRAQKVgGTEHIRYSGSPIPLSFDELGKSKSVHLVEFDQGKLQSVT 275
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
1-260 4.79e-11

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 62.02  E-value: 4.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804   1 MKLFHTADWHLGKlvhgvYMTEDQKIVLDQFVQAVEEEKPDAVIIAGDLYDRAIPptEAVDLLNDVLQkiviDLQTPVIA 80
Cdd:COG1409    1 FRFAHISDLHLGA-----PDGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEP--EEYAAAREILA----RLGVPVYV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804  81 VAGNHDspDRIHFGSSLMKKQGLHIAGQFQFPYepvvlndEYGEVHFHLIpyaDPSIVRHVlkneDVRSHDDAMRIFMNE 160
Cdd:COG1409   70 VPGNHD--IRAAMAEAYREYFGDLPPGGLYYSF-------DYGGVRFIGL---DSNVPGRS----SGELGPEQLAWLEEE 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804 161 LSETmdKEARHVFVGH--AFVTSSGEAEENTSDAERPLSIggaeyvnshyFDKFHYTAL--GHLHQAHFVRNETIRYSGS 236
Cdd:COG1409  134 LAAA--PAKPVIVFLHhpPYSTGSGSDRIGLRNAEELLAL----------LARYGVDLVlsGHVHRYERTRRDGVPYIVA 201

                        250       260
                 ....*....|....*....|....
gi 446687804 237 PLAYSISEEKHkkGYYIVELNETG 260
Cdd:COG1409  202 GSTGGQVRLPP--GYRVIEVDGDG 223
SbcD_C pfam12320
Type 5 capsule protein repressor C-terminal domain; This domain is found in bacteria and ...
 271-357 7.32e-10

Type 5 capsule protein repressor C-terminal domain; This domain is found in bacteria and archaea. This domain is about 90 amino acids in length. This domain is found associated with pfam00149. SbcD works in complex with SbdC (SbcDC) which is a transcription regulator. It down-regulates transcription of arl and mgr to inhibit type 5 capsule protein production. It acts as part of the SOS pathway of bacteria.


Pssm-ID: 463533  Cd Length: 100  Bit Score: 55.77  E-value: 7.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804  271 PRRKMRTVEAKIDELLQHPV--------SEDYVFVKLLDENPVLQPMEKIRSVYPNA----MHVERAMQRRELTDTNEVT 338
Cdd:pfam12320   1 PLRDLRRIKGSLEELLAALAyleeepadREDYLEVELTDEEPIPDLMERLREAYPNIpvelLRIRRTREERQAEEEEEAA 80

                          90
                  ....*....|....*....
gi 446687804  339 VSRHKTDDLSLLKAFYKEM 357
Cdd:pfam12320  81 EDLEELSPLELFERFYEEQ 99
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-117 1.13e-08

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 52.60  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804    1 MKLFHTADWHLgklvhgvymtEDQKIVLDQFVQAV-EEEKPDAVIIAGDLYDRAIPPTEAVDLLNDVLQKIvidlqtPVI 79
Cdd:pfam00149   1 MRILVIGDLHL----------PGQLDDLLELLKKLlEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYV------PVY 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 446687804   80 AVAGNHDSP--DRIHFGSSLMKKQGLHIAGQFQFPYEPVV 117
Cdd:pfam00149  65 LVRGNHDFDygECLRLYPYLGLLARPWKRFLEVFNFLPLA 104
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
1-86 1.94e-08

Predicted phosphohydrolase, MPP superfamily [General function prediction only];


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 54.80  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804   1 MKLFHTADWHLGKLVHGVYmtedqkivLDQFVQAVEEEKPDAVIIAGDLYDRAIPPTEAV-DLLNDVLQKIvidlqtPVI 79
Cdd:COG1408   43 LRIVQLSDLHLGPFIGGER--------LERLVEKINALKPDLVVLTGDLVDGSVAELEALlELLKKLKAPL------GVY 108


                 ....*..
gi 446687804  80 AVAGNHD 86
Cdd:COG1408  109 AVLGNHD 115
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
 2-105 2.14e-08

Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an uncharacterized Bacillus subtilis protein with a C-terminal metallophosphatase domain and an N-terminal twin-arginine (RR) motif. An RR-signal peptide derived from the Bacillus subtilis YkuE protein can direct Tat-dependent secretion of agarase in Streptomyces lividans. This is an indication that YkuE is transported by the Bacillus subtilis Tat (Twin-arginine translocation) pathway machinery. YkuE belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277331 [Multi-domain]  Cd Length: 224  Bit Score: 54.21  E-value: 2.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804   2 KLFHTADWHLGKLVHgvymtedqKIVLDQFVQAVEEEKPDAVIIAGDLYDRAIPP-TEAVDLLNDVLQKIvidlqtPVIA 80
Cdd:cd07385    3 RIVQLSDIHLGPFVG--------RTRLQKVVRKVNELNPDLIVITGDLVDGDVSVlRLLASPLSKLKAPL------GVYF 68

                         90       100
                 ....*....|....*....|....*...
gi 446687804  81 VAGNHD---SPDRIHFgsSLMKKQGLHI 105
Cdd:cd07385   69 VLGNHDyysGDVEVWI--AALEKAGITV 94
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
28-92 2.45e-07

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 50.78  E-value: 2.45e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446687804  28 LDQFVQAVEEEKPDAVIIAGDLYDRAiPPTEAVDLLndvlqKIVIDLQTPVIAVAGNHDSPDRIH 92
Cdd:COG2129   15 LEKLLELARAEDADLVILAGDLTDFG-TAEEAREVL-----EELAALGVPVLAVPGNHDDPEVLD 73
MPP_PF1019 cd07391
Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family ...
 7-87 1.33e-05

Pyrococcus furiosus PF1019 and related proteins, metallophosphatase domain; This family includes bacterial and archeal proteins homologous to PF1019, an uncharacterized Pyrococcus furiosus protein. The domain present in members of this family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277337  Cd Length: 175  Bit Score: 44.99  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804   7 ADWHLGK----LVHGVYMTEDQKI-VLDQFVQAVEEEKPDAVIIAGDLYDR--AIPPTEAVDLLNDVLQKIVIDlqtpVI 79
Cdd:cd07391    4 ADLHLGYeeelRRQGINLPRRQKErLLERLDRLLEELGPDRLVILGDLKHSfgRVSRQERREVPFFRLLAKDVD----VI 79


                 ....*...
gi 446687804  80 AVAGNHDS 87
Cdd:cd07391   80 LIRGNHDG 87
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
28-88 1.63e-05

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 44.91  E-value: 1.63e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446687804  28 LDQFVQAVEEEKPDAVIIAGDLYDRAIPPTEAVDLLNDVlqkividlqtPVIAVAGNHDSP 88
Cdd:COG0622   15 LEAVLEDLEREGVDLIVHLGDLVGYGPDPPEVLDLLREL----------PIVAVRGNHDGA 65
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 5-89 2.79e-05

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 44.96  E-value: 2.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804   5 HTADWHLGKLVHGVYMTEDQKIVLDQFVQAVEEEK--PDAVIIAGDLYDRAIPptEAVDLLNDVLQKividLQTPVIAVA 82
Cdd:cd07402    3 QISDTHLFAPGEGALLGVDTAARLAAAVAQVNALHprPDLVVVTGDLSDDGSP--ESYERLRELLAP----LPAPVYWIP 76


                 ....*..
gi 446687804  83 GNHDSPD 89
Cdd:cd07402   77 GNHDDRA 83
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 32-86 8.33e-05

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 41.87  E-value: 8.33e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446687804  32 VQAVEEEKPDAVIIAGDLYDRAIPPTEAVDLLndvlqKIVIDLQTPVIAVAGNHD 86
Cdd:cd00838   19 AALAKAEKPDLVICLGDLVDYGPDPEEVELKA-----LRLLLAGIPVYVVPGNHD 68
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 30-144 2.96e-04

Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277345 [Multi-domain]  Cd Length: 138  Bit Score: 40.74  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804  30 QFVQAVEEEKPDAVIIAGDLYDRAIPP--TEAVDLLnDVLQKIvidlqtPVIAVAGNHDSpdrihfgsslmkkqglhiag 107
Cdd:cd07400   21 NLLDEINALKPDLVVVTGDLTQRARPAefEEAREFL-DALEPE------PVVVVPGNHDA-------------------- 73

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446687804 108 qfqfpyepVVLndeygeVHFHLIPYADPSIVRHVLKN 144
Cdd:cd07400   74 --------IVA------LHHPLLPPPDTGRERNVLLD 96
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 33-93 4.73e-04

Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; DCR2 phosphatase (Dosage-dependent Cell Cycle Regulator 2) functions together with DCR1 (Gid8) in a common pathway to accelerate initiation of DNA replication in Saccharomyces cerevisiae. Genetic analysis suggests that DCR1 functions upstream of DCR2. DCR2 interacts with and dephosphorylates Sic1, an inhibitor of mitotic cyclin/cyclin-dependent kinase complexes, which may serve to trigger the initiation of cell division. DCR2 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277329 [Multi-domain]  Cd Length: 202  Bit Score: 41.12  E-value: 4.73e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446687804  33 QAVEEEKPDAVIIAGDL-YDRAIPPTEAVDLLNDVLqKIVIDLQTPVIAVAGNHDSPDRIHF 93
Cdd:cd07383   36 SVLDEEKPDLVVLTGDLiTGENTADDNATSYLDKAV-SPLVERGIPWAATFGNHDGYDWIDP 96
MPP_CSTP1 cd07395
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ...
 23-174 1.10e-03

Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete S-transactivated protein 1) is an uncharacterized Homo sapiens protein with a metallophosphatase domain, that is transactivated by the complete S protein of hepatitis B virus. CSTP1 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277340 [Multi-domain]  Cd Length: 263  Bit Score: 40.38  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804  23 DQKIVL-DQFVQAVEE--EKPDAVIIAGDLYDraIPPTEA-----VDLLNDVLQKIviDLQTPVIAVAGNHD-----SPD 89
Cdd:cd07395   31 DKEIELtEQAVQAINKlnPKPKFVVVCGDLVH--AMPGEEfreqqVSDLKDVLSKL--DPDIPLVCVCGNHDvgntpTPE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804  90 RI-----HFGSSLMkkqGLHIAGQFQfpyepVVLNDEYgevhfhlipYADPSIVRHVLKNEDVrshddamrIFMNELSET 164
Cdd:cd07395  107 TIqryrdDFGDDYF---SFWVGGVFF-----IVLNSQL---------FKDPSKVPELASAQDQ--------WLEEQLQIA 161

                        170
                 ....*....|
gi 446687804 165 MDKEARHVFV 174
Cdd:cd07395  162 RESDAKHVVV 171
47 PHA02546
endonuclease subunit; Provisional
 1-253 5.04e-03

endonuclease subunit; Provisional


Pssm-ID: 222867 [Multi-domain]  Cd Length: 340  Bit Score: 38.44  E-value: 5.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804   1 MKLFHTADWHLGKLVHGVYMTEDQKIVLDQFVQAVEEEKPDAVIIAGDLYD--RAIPPT---EAVDLLNDVLQKIVIDLQ 75
Cdd:PHA02546   1 MKILLIGDQHLGVRKDDPWFQNYQLKFIKQAIEYSKAHGITTWIQLGDTFDvrKAITQNtmnFVREKIFDLLKEAGITLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804  76 TPViavaGNHDspdrIHFGSSLMKKQGLHIAGQfqfpYEPVVLNDE-----YGEVHFHLIPYadpsivrhvlKNEDVRSh 150
Cdd:PHA02546  81 VLV----GNHD----MYYKNTIRPNAPTELLGQ----YDNITVIDEpttvdFDGCSIDLIPW----------ICKENTE- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446687804 151 ddamRIFmnELSETMDKEarhVFVGHaFVTSSGEAEENtSDAERPLSIGgaeyvnshYFDKFHYTALGHLHQAHFVRNet 230
Cdd:PHA02546 138 ----EIL--EFIKNSKSE---YCVGH-WELNGFYFYKG-MKSDHGLDPD--------FLKKYKQVWSGHFHTISEKGN-- 196

                        250       260
                 ....*....|....*....|...
gi 446687804 231 IRYSGSPLAYSISEEKHKKGYYI 253
Cdd:PHA02546 197 VTYIGTPYTLTAGDENDPRGFWV 219
 
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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