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Conserved domains on  [gi|1057866489|ref|NP_001317276|]
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double-strand break repair protein MRE11 isoform 3 [Homo sapiens]

Protein Classification

double-strand break repair protein MRE11( domain architecture ID 1903556)

double-strand break repair protein MRE11 is a component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
mre11 super family cl44331
DNA repair protein (mre11); All proteins in this family for which functions are known are ...
10-402 7.61e-174

DNA repair protein (mre11); All proteins in this family for which functions are known are subunits of a nuclease complex made up of multiple proteins including MRE11 and RAD50 homologs. The functions of this nuclease complex include recombinational repair and non-homolgous end joining. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). The proteins in this family are distantly related to proteins in the SbcCD complex of bacteria. [DNA metabolism, DNA replication, recombination, and repair]


The actual alignment was detected with superfamily member TIGR00583:

Pssm-ID: 273153 [Multi-domain]  Cd Length: 405  Bit Score: 502.83  E-value: 7.61e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  10 ENTFKILVATDIHLGFMEKDAVRGNDTFVTLDEILRLAQENEVDFILLGGDLFHENKPSRKTLHTCLELLRKYCMGDRPV 89
Cdd:TIGR00583   1 EDTIRILVSTDNHVGYGENDPVRGDDSWNTFEEVLQIAKEQDVDMILLGGDLFHENKPSRKSLYQVLRSLRLYCLGDKPC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  90 QFEILSDQSVNFGFSKFPWVNYQDGNLNISIPVFSIHGNHDDPTGADALCALDILSCAGFVNHFGRSMSVEKIDISPVLL 169
Cdd:TIGR00583  81 ELEFLSDASVVFNQSAFGNVNYEDPNINVAIPVFSIHGNHDDPSGDGLLCALDLLHATGLVNYFGKVPEIDNIIVSPILL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 170 QKGSTKIALYGLGSIPDERLYRMFVNKKVTMLRPKEDENSWFNLFVIHQNRSKHGSTNFIPEQFLDDFIDLVIWGHEHEC 249
Cdd:TIGR00583 161 QKGETKLALYGISNVRDERLVRTFKDNKVSFLRPNAGAEDWFNLLVLHQNHAAHTSTSFLPESFIPDFFDLVIWGHEHEC 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 250 KIAPTKNEQQLFYISQPGSSVVTSLSPGEAVKKHVGLLRIKGRKMNMHKIPLHTVRQFFMEDIVLANHPDIFNPDNPKVT 329
Cdd:TIGR00583 241 LPDPVYNPSDGFYVLQPGSTVATSLTPGEALPKHVFILNIKGRKFASKPIPLQTVRPFVMKEILLDKVPGSRPILKTDNK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 330 QAIQSFCLEKIEEMLE--NAE-RERLGNSH-----QPEKPLVRLRVDYSG---GFEPFSVLRFSQKFVDRVANPKDIIHF 398
Cdd:TIGR00583 321 KETDKRLIDEVEEMINeaNAEwKAKRADGEgdeprEPPLPLIRLKVDYTGpwlNYQVENPKRFSNRFVGRVANANDVVQF 400

                  ....
gi 1057866489 399 FRHR 402
Cdd:TIGR00583 401 YKNN 404
 
Name Accession Description Interval E-value
mre11 TIGR00583
DNA repair protein (mre11); All proteins in this family for which functions are known are ...
10-402 7.61e-174

DNA repair protein (mre11); All proteins in this family for which functions are known are subunits of a nuclease complex made up of multiple proteins including MRE11 and RAD50 homologs. The functions of this nuclease complex include recombinational repair and non-homolgous end joining. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). The proteins in this family are distantly related to proteins in the SbcCD complex of bacteria. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273153 [Multi-domain]  Cd Length: 405  Bit Score: 502.83  E-value: 7.61e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  10 ENTFKILVATDIHLGFMEKDAVRGNDTFVTLDEILRLAQENEVDFILLGGDLFHENKPSRKTLHTCLELLRKYCMGDRPV 89
Cdd:TIGR00583   1 EDTIRILVSTDNHVGYGENDPVRGDDSWNTFEEVLQIAKEQDVDMILLGGDLFHENKPSRKSLYQVLRSLRLYCLGDKPC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  90 QFEILSDQSVNFGFSKFPWVNYQDGNLNISIPVFSIHGNHDDPTGADALCALDILSCAGFVNHFGRSMSVEKIDISPVLL 169
Cdd:TIGR00583  81 ELEFLSDASVVFNQSAFGNVNYEDPNINVAIPVFSIHGNHDDPSGDGLLCALDLLHATGLVNYFGKVPEIDNIIVSPILL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 170 QKGSTKIALYGLGSIPDERLYRMFVNKKVTMLRPKEDENSWFNLFVIHQNRSKHGSTNFIPEQFLDDFIDLVIWGHEHEC 249
Cdd:TIGR00583 161 QKGETKLALYGISNVRDERLVRTFKDNKVSFLRPNAGAEDWFNLLVLHQNHAAHTSTSFLPESFIPDFFDLVIWGHEHEC 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 250 KIAPTKNEQQLFYISQPGSSVVTSLSPGEAVKKHVGLLRIKGRKMNMHKIPLHTVRQFFMEDIVLANHPDIFNPDNPKVT 329
Cdd:TIGR00583 241 LPDPVYNPSDGFYVLQPGSTVATSLTPGEALPKHVFILNIKGRKFASKPIPLQTVRPFVMKEILLDKVPGSRPILKTDNK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 330 QAIQSFCLEKIEEMLE--NAE-RERLGNSH-----QPEKPLVRLRVDYSG---GFEPFSVLRFSQKFVDRVANPKDIIHF 398
Cdd:TIGR00583 321 KETDKRLIDEVEEMINeaNAEwKAKRADGEgdeprEPPLPLIRLKVDYTGpwlNYQVENPKRFSNRFVGRVANANDVVQF 400

                  ....
gi 1057866489 399 FRHR 402
Cdd:TIGR00583 401 YKNN 404
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
14-275 8.41e-64

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: 209.82  E-value: 8.41e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  14 KILVATDIHLGFMEKDAV-RGNDTFVTLDEILRLAQENEVDFILLGGDLFHENKPSRKTLHTCLELLRKYCmgdrpvqfe 92
Cdd:cd00840     1 RFLHTADWHLGYPLYGLSrREEDFFKAFEEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLRRLC--------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  93 ilsdqsvnfgfskfpwvnyqdgnlNISIPVFSIHGNHDDPTGadalcaldilscagfvnhfgrsmsvekidispvllqkg 172
Cdd:cd00840    72 ------------------------EAGIPVFVIAGNHDSPAR-------------------------------------- 89
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 173 stkIALYGLGSIPDERLYRMFVNKKvtmLRPKEDENSWFNLFVIHQNRSKHGSTN----FIPEQFLDDFIDLVIWGHEHE 248
Cdd:cd00840    90 ---VAIYGLPYLRDERLERLFEDLE---LRPRLLKPDWFNILLLHQGVDGAGPSDserpIVPEDLLPDGFDYVALGHIHK 163
                         250       260
                  ....*....|....*....|....*..
gi 1057866489 249 CKIaptkNEQQLFYISQPGSSVVTSLS 275
Cdd:cd00840   164 PQI----IEGGGPPIVYPGSPEPTSFS 186
Mre11_DNA_bind pfam04152
Mre11 DNA-binding presumed domain; The Mre11 complex is a multi-subunit nuclease that is ...
294-461 5.89e-63

Mre11 DNA-binding presumed domain; The Mre11 complex is a multi-subunit nuclease that is composed of Mre11, Rad50 and Nbs1/Xrs2, and is involved in checkpoint signalling and DNA replication. Mre11 has an intrinsic DNA-binding activity that is stimulated by Rad50 on its own or in combination with Nbs1.


Pssm-ID: 461198  Cd Length: 175  Bit Score: 207.45  E-value: 5.89e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 294 MNMHKIPLHTVRQFFMEDIVLANHPDIFNPDnPKVTQAIQSFCLEKIEEMLENAERERL--------GNSHQPEKPLVRL 365
Cdd:pfam04152   1 FKLEPIPLKTVRPFVMDEIVLSEVAEIKPPD-PDDKEEVTKFLREKVEELIEEAKEEWLereaddeeGEPEQPPLPLIRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 366 RVDYSGGFEPFSVLRFSQKFVDRVANPKDIIHFFRHREQKEKTGEEINFGK----LITKPSEGTTLRVEDLVKQYFQTAe 441
Cdd:pfam04152  80 RVEYTGGFEVENPQRFGQRFVGRVANPNDVVQFYRKKKARRKKKKDKAADGedeeLLDEPEKLDELRVEDLVKEYLAAQ- 158
                         170       180
                  ....*....|....*....|
gi 1057866489 442 knvQLSLLTERGMGEAVQEF 461
Cdd:pfam04152 159 ---QLTLLPENGLGEAVEQF 175
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
13-308 1.59e-21

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 94.59  E-value: 1.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  13 FKILVATDIHLGFMEKDAVRGNDTFVTLDEILRLAQENEVDFILLGGDLFHENKPSRKTLHTCLELLRKycmgdrpvqfe 92
Cdd:COG0420     1 MRFLHTADWHLGKPLHGASRREDQLAALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRR----------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  93 iLSDQsvnfgfskfpwvnyqdgnlniSIPVFSIHGNHDDPTGADAlcALDILSCAGFvnHFgrsmsVEKIDISPVLLQKG 172
Cdd:COG0420    70 -LSEA---------------------GIPVVLIAGNHDSPSRLSA--GSPLLENLGV--HV-----FGSVEPEPVELEDG 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 173 sTKIALYGLGSIPDERLYRMfvNKKVTMLRPKEDENsWFNLFVIHQ--NRSKHGSTNFI----PEQFLDDFIDLVIWGHE 246
Cdd:COG0420   119 -LGVAVYGLPYLRPSDEEAL--RDLLERLPRALDPG-GPNILLLHGfvAGASGSRDIYVapvpLSALPAAGFDYVALGHI 194
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1057866489 247 HECKIAPtkNEQQLFYisqPGSSVvtSLSPGEAVKKHVGLLRI-KGRKMNMHKIPLHTVRQFF 308
Cdd:COG0420   195 HRPQVLG--GDPRIRY---SGSPE--PRSFSEAGGKGVLLVELdAGGLVSVEFVPLPATRRFL 250
 
Name Accession Description Interval E-value
mre11 TIGR00583
DNA repair protein (mre11); All proteins in this family for which functions are known are ...
10-402 7.61e-174

DNA repair protein (mre11); All proteins in this family for which functions are known are subunits of a nuclease complex made up of multiple proteins including MRE11 and RAD50 homologs. The functions of this nuclease complex include recombinational repair and non-homolgous end joining. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). The proteins in this family are distantly related to proteins in the SbcCD complex of bacteria. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273153 [Multi-domain]  Cd Length: 405  Bit Score: 502.83  E-value: 7.61e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  10 ENTFKILVATDIHLGFMEKDAVRGNDTFVTLDEILRLAQENEVDFILLGGDLFHENKPSRKTLHTCLELLRKYCMGDRPV 89
Cdd:TIGR00583   1 EDTIRILVSTDNHVGYGENDPVRGDDSWNTFEEVLQIAKEQDVDMILLGGDLFHENKPSRKSLYQVLRSLRLYCLGDKPC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  90 QFEILSDQSVNFGFSKFPWVNYQDGNLNISIPVFSIHGNHDDPTGADALCALDILSCAGFVNHFGRSMSVEKIDISPVLL 169
Cdd:TIGR00583  81 ELEFLSDASVVFNQSAFGNVNYEDPNINVAIPVFSIHGNHDDPSGDGLLCALDLLHATGLVNYFGKVPEIDNIIVSPILL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 170 QKGSTKIALYGLGSIPDERLYRMFVNKKVTMLRPKEDENSWFNLFVIHQNRSKHGSTNFIPEQFLDDFIDLVIWGHEHEC 249
Cdd:TIGR00583 161 QKGETKLALYGISNVRDERLVRTFKDNKVSFLRPNAGAEDWFNLLVLHQNHAAHTSTSFLPESFIPDFFDLVIWGHEHEC 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 250 KIAPTKNEQQLFYISQPGSSVVTSLSPGEAVKKHVGLLRIKGRKMNMHKIPLHTVRQFFMEDIVLANHPDIFNPDNPKVT 329
Cdd:TIGR00583 241 LPDPVYNPSDGFYVLQPGSTVATSLTPGEALPKHVFILNIKGRKFASKPIPLQTVRPFVMKEILLDKVPGSRPILKTDNK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 330 QAIQSFCLEKIEEMLE--NAE-RERLGNSH-----QPEKPLVRLRVDYSG---GFEPFSVLRFSQKFVDRVANPKDIIHF 398
Cdd:TIGR00583 321 KETDKRLIDEVEEMINeaNAEwKAKRADGEgdeprEPPLPLIRLKVDYTGpwlNYQVENPKRFSNRFVGRVANANDVVQF 400

                  ....
gi 1057866489 399 FRHR 402
Cdd:TIGR00583 401 YKNN 404
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
14-275 8.41e-64

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: 209.82  E-value: 8.41e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  14 KILVATDIHLGFMEKDAV-RGNDTFVTLDEILRLAQENEVDFILLGGDLFHENKPSRKTLHTCLELLRKYCmgdrpvqfe 92
Cdd:cd00840     1 RFLHTADWHLGYPLYGLSrREEDFFKAFEEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLRRLC--------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  93 ilsdqsvnfgfskfpwvnyqdgnlNISIPVFSIHGNHDDPTGadalcaldilscagfvnhfgrsmsvekidispvllqkg 172
Cdd:cd00840    72 ------------------------EAGIPVFVIAGNHDSPAR-------------------------------------- 89
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 173 stkIALYGLGSIPDERLYRMFVNKKvtmLRPKEDENSWFNLFVIHQNRSKHGSTN----FIPEQFLDDFIDLVIWGHEHE 248
Cdd:cd00840    90 ---VAIYGLPYLRDERLERLFEDLE---LRPRLLKPDWFNILLLHQGVDGAGPSDserpIVPEDLLPDGFDYVALGHIHK 163
                         250       260
                  ....*....|....*....|....*..
gi 1057866489 249 CKIaptkNEQQLFYISQPGSSVVTSLS 275
Cdd:cd00840   164 PQI----IEGGGPPIVYPGSPEPTSFS 186
Mre11_DNA_bind pfam04152
Mre11 DNA-binding presumed domain; The Mre11 complex is a multi-subunit nuclease that is ...
294-461 5.89e-63

Mre11 DNA-binding presumed domain; The Mre11 complex is a multi-subunit nuclease that is composed of Mre11, Rad50 and Nbs1/Xrs2, and is involved in checkpoint signalling and DNA replication. Mre11 has an intrinsic DNA-binding activity that is stimulated by Rad50 on its own or in combination with Nbs1.


Pssm-ID: 461198  Cd Length: 175  Bit Score: 207.45  E-value: 5.89e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 294 MNMHKIPLHTVRQFFMEDIVLANHPDIFNPDnPKVTQAIQSFCLEKIEEMLENAERERL--------GNSHQPEKPLVRL 365
Cdd:pfam04152   1 FKLEPIPLKTVRPFVMDEIVLSEVAEIKPPD-PDDKEEVTKFLREKVEELIEEAKEEWLereaddeeGEPEQPPLPLIRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 366 RVDYSGGFEPFSVLRFSQKFVDRVANPKDIIHFFRHREQKEKTGEEINFGK----LITKPSEGTTLRVEDLVKQYFQTAe 441
Cdd:pfam04152  80 RVEYTGGFEVENPQRFGQRFVGRVANPNDVVQFYRKKKARRKKKKDKAADGedeeLLDEPEKLDELRVEDLVKEYLAAQ- 158
                         170       180
                  ....*....|....*....|
gi 1057866489 442 knvQLSLLTERGMGEAVQEF 461
Cdd:pfam04152 159 ---QLTLLPENGLGEAVEQF 175
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
13-308 1.59e-21

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 94.59  E-value: 1.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  13 FKILVATDIHLGFMEKDAVRGNDTFVTLDEILRLAQENEVDFILLGGDLFHENKPSRKTLHTCLELLRKycmgdrpvqfe 92
Cdd:COG0420     1 MRFLHTADWHLGKPLHGASRREDQLAALDRLVDLAIEEKVDAVLIAGDLFDSANPSPEAVRLLAEALRR----------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  93 iLSDQsvnfgfskfpwvnyqdgnlniSIPVFSIHGNHDDPTGADAlcALDILSCAGFvnHFgrsmsVEKIDISPVLLQKG 172
Cdd:COG0420    70 -LSEA---------------------GIPVVLIAGNHDSPSRLSA--GSPLLENLGV--HV-----FGSVEPEPVELEDG 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 173 sTKIALYGLGSIPDERLYRMfvNKKVTMLRPKEDENsWFNLFVIHQ--NRSKHGSTNFI----PEQFLDDFIDLVIWGHE 246
Cdd:COG0420   119 -LGVAVYGLPYLRPSDEEAL--RDLLERLPRALDPG-GPNILLLHGfvAGASGSRDIYVapvpLSALPAAGFDYVALGHI 194
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1057866489 247 HECKIAPtkNEQQLFYisqPGSSVvtSLSPGEAVKKHVGLLRI-KGRKMNMHKIPLHTVRQFF 308
Cdd:COG0420   195 HRPQVLG--GDPRIRY---SGSPE--PRSFSEAGGKGVLLVELdAGGLVSVEFVPLPATRRFL 250
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
13-277 2.85e-08

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 55.08  E-value: 2.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  13 FKILVATDIHLGfmekdAVRGNDTFVTLDEILRLAQENEVDFILLGGDLFHENKPSrktlhtclellrkycmgdrpvQFE 92
Cdd:COG1409     1 FRFAHISDLHLG-----APDGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPE---------------------EYA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  93 ILSDQsvnfgFSKFPwvnyqdgnlnisIPVFSIHGNHDDPTGADALcaldilscagFVNHFGRSMSVEK---IDISPVLL 169
Cdd:COG1409    55 AAREI-----LARLG------------VPVYVVPGNHDIRAAMAEA----------YREYFGDLPPGGLyysFDYGGVRF 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 170 qkgstkIAL------YGLGSIPDERLYRMfvnkkVTMLRPKEDEnswFNLFVIHQN-RSKHGSTNFIP----EQFLDDF- 237
Cdd:COG1409   108 ------IGLdsnvpgRSSGELGPEQLAWL-----EEELAAAPAK---PVIVFLHHPpYSTGSGSDRIGlrnaEELLALLa 173
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1057866489 238 ---IDLVIWGHEHECKIAPTKNeqqLFYISQPGSSVVTSLSPG 277
Cdd:COG1409   174 rygVDLVLSGHVHRYERTRRDG---VPYIVAGSTGGQVRLPPG 213
MPP_YkuE_C cd07385
Bacillus subtilis YkuE and related proteins, C-terminal metallophosphatase domain; YkuE is an ...
13-247 1.55e-07

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: 52.67  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  13 FKILVATDIHLGfmekdavrGNDTFVTLDEILRLAQENEVDFILLGGDLFHENKPSRKTLHTCLELLRkycmgdrpvqfe 92
Cdd:cd07385     2 LRIVQLSDIHLG--------PFVGRTRLQKVVRKVNELNPDLIVITGDLVDGDVSVLRLLASPLSKLK------------ 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  93 ilsdqsvnfgfSKFpwvnyqdgnlnisiPVFSIHGNHDDPTGADALcaldilscagFVNHFgrsmsvEKIDISP-----V 167
Cdd:cd07385    62 -----------APL--------------GVYFVLGNHDYYSGDVEV----------WIAAL------EKAGITVlrnesV 100
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 168 LLQKGSTKIALYGLGSIPDERlYRMFVNKKVtmlrpKEDENSWFNLFVIHQnrskhgstnfiPEQFLD---DFIDLVIWG 244
Cdd:cd07385   101 ELSRDGATIGLAGSGVDDIGG-HGEDLEKAL-----KGLDENDPVILLAHN-----------PDAAEEaqrPGVDLVLSG 163

                  ...
gi 1057866489 245 HEH 247
Cdd:cd07385   164 HTH 166
YaeI COG1408
Predicted phosphohydrolase, MPP superfamily [General function prediction only];
13-247 3.20e-07

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


Pssm-ID: 441018 [Multi-domain]  Cd Length: 268  Bit Score: 52.49  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  13 FKILVATDIHLG-FMEKDAVRgndtfvtldEILRLAQENEVDFILLGGDLFHEnkpSRKTLHTCLELLRKycmgdrpvqf 91
Cdd:COG1408    43 LRIVQLSDLHLGpFIGGERLE---------RLVEKINALKPDLVVLTGDLVDG---SVAELEALLELLKK---------- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  92 eilsdqsvnfgfskfpwvnyqdgnLNISIPVFSIHGNHDDPTGADALcaLDILSCAGFVNHFGRSmsvekidispVLLQK 171
Cdd:COG1408   101 ------------------------LKAPLGVYAVLGNHDYYAGLEEL--RAALEEAGVRVLRNEA----------VTLER 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1057866489 172 GSTKIALYGLGsipDERLYRMFVNKKVTMLRPKEDenswFNLFVIHQnrskhgstnfiP---EQFLDDFIDLVIWGHEH 247
Cdd:COG1408   145 GGDRLNLAGVD---DPHAGRFPDLEKALAGVPPDA----PRILLAHN-----------PdvfDEAAAAGVDLQLSGHTH 205
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
14-293 3.99e-07

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 51.17  E-value: 3.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  14 KILVATDIHLGFMEkdavrgndtfvtLDEILRLAQENEVDFILLGGDLfhenkpsrkTLHTCLELLRKYcmgdrpvqFEI 93
Cdd:COG2129     1 KILAVSDLHGNFDL------------LEKLLELARAEDADLVILAGDL---------TDFGTAEEAREV--------LEE 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  94 LSDqsvnfgfskfpwvnyqdgnlnISIPVFSIHGNHDDPTgadalcALDILSCAGFVNHFGRSMSVEKIDIspvllqkgs 173
Cdd:COG2129    52 LAA---------------------LGVPVLAVPGNHDDPE------VLDALEESGVHNLHGRVVEIGGLRI--------- 95
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489 174 tkialYGLGSI---PDERLYRMF---VNKKVTMLRPKEdenswFNLFVIH-----------QNRSKHGSTNFipEQFLDD 236
Cdd:COG2129    96 -----AGLGGSrptPFGTPYEYTeeeIEERLAKLREKD-----VDILLTHappygttldrvEDGPHVGSKAL--RELIEE 163
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1057866489 237 F-IDLVIWGHEHECkiaptkneqqlFYISQPGSSVVtsLSPGEAVKKHVGLLRIKGRK 293
Cdd:COG2129   164 FqPKLVLHGHIHES-----------RGVDKIGGTRV--VNPGSLAEGYYALIDLEDRS 208
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
13-131 1.76e-06

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: 47.21  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057866489  13 FKILVATDIHLGfmekdavrgnDTFVTLDEILR-LAQENEVDFILLGGDLFHENKPSrktlHTCLELLRKycmgdrpvqf 91
Cdd:pfam00149   1 MRILVIGDLHLP----------GQLDDLLELLKkLLEEGKPDLVLHAGDLVDRGPPS----EEVLELLER---------- 56
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1057866489  92 eilsdqsvnfgfskfpwvnyqdgnLNISIPVFSIHGNHDD 131
Cdd:pfam00149  57 ------------------------LIKYVPVYLVRGNHDF 72
 
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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