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Conserved domains on  [gi|515498086|ref|WP_016931340|]
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MULTISPECIES: 3'-5' exoribonuclease YhaM [Staphylococcus]

Protein Classification

3'-5' exoribonuclease YhaM( domain architecture ID 11486651)

3'-5' exoribonuclease YhaM is involved in trimming of a few nucleotides and targeting transcript ends generated either by transcription termination or by endonucleolytic activity

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13480 PRK13480
3'-5' exoribonuclease YhaM; Provisional
1-313 0e+00

3'-5' exoribonuclease YhaM; Provisional


:

Pssm-ID: 237394 [Multi-domain]  Cd Length: 314  Bit Score: 638.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086   1 MRNVEKLNPGDSVENFFLIHRATQGVTAQGKDYMTLFLQDKSGDIEAKLWTVSKEDMQILKPETIVWVKGDVINYRGRKQ 80
Cdd:PRK13480   2 MKGIEELEVGEQVDHFLLIKSATKGVASNGKPFLTLILQDKSGDIEAKLWDVSPEDEATYVPETIVHVKGDIINYRGRKQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086  81 MKVNQFRLAKPEDGFKTQDFVAGAPLSPDEIQENISHYILDIENANLQRITRHLLKKYQDKFFTYPAASSHHHNFASGLS 160
Cdd:PRK13480  82 LKVNQIRLATEEDGVKISDFVEKAPLSKEEMQEEITQYIFEMENPNIQRITRHLLKKYQEEFLDYPAATKNHHEFVSGLA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086 161 YHVLTMLEIAKSLCNIYPLLNRSLLYSSIILHDLGKVRELSGPVATTYTVEGNLLGHISIASDEVAEAAKELGIDGEEVM 240
Cdd:PRK13480 162 YHVVSMLRLAKSICDLYPSLNKDLLYAGIILHDLGKVIELSGPVSTTYTLEGNLLGHISIMVNEIAKAADELQIDGEEVL 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515498086 241 LLRHMILAHHGKMEFGSPKLPHLKEAEILFFIDNIDAKMNMFEKAFKKTDKGQFTERIFGMENRQFYNPEKLD 313
Cdd:PRK13480 242 ILQHMVLSHHGKAEWGSPKPPLVKEAEILHYIDNIDAKMNMMDRALKKTKPGEFTERVFALDNRSFYKPTFLD 314
 
Name Accession Description Interval E-value
PRK13480 PRK13480
3'-5' exoribonuclease YhaM; Provisional
1-313 0e+00

3'-5' exoribonuclease YhaM; Provisional


Pssm-ID: 237394 [Multi-domain]  Cd Length: 314  Bit Score: 638.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086   1 MRNVEKLNPGDSVENFFLIHRATQGVTAQGKDYMTLFLQDKSGDIEAKLWTVSKEDMQILKPETIVWVKGDVINYRGRKQ 80
Cdd:PRK13480   2 MKGIEELEVGEQVDHFLLIKSATKGVASNGKPFLTLILQDKSGDIEAKLWDVSPEDEATYVPETIVHVKGDIINYRGRKQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086  81 MKVNQFRLAKPEDGFKTQDFVAGAPLSPDEIQENISHYILDIENANLQRITRHLLKKYQDKFFTYPAASSHHHNFASGLS 160
Cdd:PRK13480  82 LKVNQIRLATEEDGVKISDFVEKAPLSKEEMQEEITQYIFEMENPNIQRITRHLLKKYQEEFLDYPAATKNHHEFVSGLA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086 161 YHVLTMLEIAKSLCNIYPLLNRSLLYSSIILHDLGKVRELSGPVATTYTVEGNLLGHISIASDEVAEAAKELGIDGEEVM 240
Cdd:PRK13480 162 YHVVSMLRLAKSICDLYPSLNKDLLYAGIILHDLGKVIELSGPVSTTYTLEGNLLGHISIMVNEIAKAADELQIDGEEVL 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515498086 241 LLRHMILAHHGKMEFGSPKLPHLKEAEILFFIDNIDAKMNMFEKAFKKTDKGQFTERIFGMENRQFYNPEKLD 313
Cdd:PRK13480 242 ILQHMVLSHHGKAEWGSPKPPLVKEAEILHYIDNIDAKMNMMDRALKKTKPGEFTERVFALDNRSFYKPTFLD 314
YhaM COG3481
3'-5' exoribonuclease YhaM, can participate in 23S rRNA maturation, HD superfamily ...
1-309 6.12e-150

3'-5' exoribonuclease YhaM, can participate in 23S rRNA maturation, HD superfamily [Translation, ribosomal structure and biogenesis]; 3'-5' exoribonuclease YhaM, can participate in 23S rRNA maturation, HD superfamily is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 442704 [Multi-domain]  Cd Length: 316  Bit Score: 423.06  E-value: 6.12e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086   1 MRNVEKLNPGDSVENFFLIHRATQGVTAQGKDYMTLFLQDKSGDIEAKLWTVSKEDMQILKPETIVWVKGDVINYRGRKQ 80
Cdd:COG3481    4 RKFIKDLKPGEEVDGFFLIKSKELRTTKNGKPYLSLTLQDKTGTIEAKIWDASEEDIEEFQPGDVVKVRGKVQEYQGRLQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086  81 MKVNQFRLAKPEDgFKTQDFVAGAPLSPDEIQENISHYILDIENANLQRITRHLL-KKYQDKFFTYPAASSHHHNFASGL 159
Cdd:COG3481   84 LKITRIRLADEEE-VDPSDFLPSSPKDIEEMYEELLELIDSIENPYLKRLLRAILdKEFRERFLTAPAAKSNHHAYIGGL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086 160 SYHVLTMLEIAKSLCNIYPLLNRSLLYSSIILHDLGKVRELSGPVATTYTVEGNLLGHISIASDEVAEAAKELG-IDGEE 238
Cdd:COG3481  163 LEHTLSVARLAKALADLYPELNRDLLIAGAILHDIGKVRELSGPPGTEYTDEGQLLGHIVLGVEMIEEAAAELGdFPEEL 242
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498086 239 VMLLRHMILAHHGKMEFGSPKLPHLKEAEILFFIDNIDAKMNMFEKAFKKTDK-GQFTERIFGMENRqFYNP 309
Cdd:COG3481  243 LLLLKHMILSHHGELEWGSPKRPKTPEAEILHYADNLDAKMNMFERALEKVEPgGEWTEYIRALDRR-FYKP 313
YhaM_OBF_like cd04492
YhaM_OBF_like: A subfamily of OB folds similar to that found in Bacillus subtilis YhaM and ...
14-94 1.55e-28

YhaM_OBF_like: A subfamily of OB folds similar to that found in Bacillus subtilis YhaM and Staphylococcus aureus cmp-binding factor-1 (SaCBF1). Both these proteins are 3'-to-5'exoribonucleases. YhaM requires Mn2+ or Co2+ for activity and is inactive in the presence of Mg2+. YhaM also has a Mn2+ dependent 3'-to-5'single-stranded DNA exonuclease activity. SaCBF is also a double-stranded DNA binding protein, binding specifically to cmp, the replication enhancer found in S. aureus plasmid pT181. Proteins in this group combine an N-terminal OB fold with a C-terminal HD domain. The HD domain is found in metal-dependent phosphohydrolases.


Pssm-ID: 239938 [Multi-domain]  Cd Length: 83  Bit Score: 104.98  E-value: 1.55e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086  14 ENFFLIHRATQGVTAQGKDYMTLFLQDKSGDIEAKLWTVSKEDMQILKPETIVWVKGDVINYRGRKQMKVNQFRLAKPED 93
Cdd:cd04492    1 DGFFLIKSKELRTAKNGKPYLALTLQDKTGEIEAKLWDASEEDEEKFKPGDIVHVKGRVEEYRGRLQLKIQRIRLVTEED 80

                 .
gi 515498086  94 G 94
Cdd:cd04492   81 G 81
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
150-277 3.40e-11

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 59.62  E-value: 3.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086   150 SHHHNFasglsYHVLTMLEIAKSLCNIYPLLNRSLLYSSIILHDLGKVRELSGPVATTytveGNLLGHISIAsdevAEAA 229
Cdd:smart00471   1 SDYHVF-----EHSLRVAQLAAALAEELGLLDIELLLLAALLHDIGKPGTPDSFLVKT----SVLEDHHFIG----AEIL 67
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 515498086   230 KELGIDGEEVMLLRHMILAHHGkMEFGSPKLPHLKEAEILFFIDNIDA 277
Cdd:smart00471  68 LEEEEPRILEEILRTAILSHHE-RPDGLRGEPITLEARIVKVADRLDA 114
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
161-277 7.85e-11

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 58.40  E-value: 7.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086  161 YHVLTMLEIAKSLCNIYPLLNRSLLYSSIILHDLGKvrelsGPVATTYTVEGNLLGHISIASDEVAEAAKELGidgeeVM 240
Cdd:pfam01966   3 EHSLRVALLARELAEELGELDRELLLLAALLHDIGK-----GPFGDEKPEFEIFLGHAVVGAEILRELEKRLG-----LE 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 515498086  241 LLRHMILAHHGKMEFGSPKLPHLKEAEILFFIDNIDA 277
Cdd:pfam01966  73 DVLKLILEHHESWEGAGYPEEISLEARIVKLADRLDA 109
cas3_HD TIGR01596
CRISPR-associated endonuclease Cas3-HD; CRISPR/Cas systems are widespread, mobile systems for ...
159-252 3.19e-04

CRISPR-associated endonuclease Cas3-HD; CRISPR/Cas systems are widespread, mobile systems for host defense against invasive elements such as phage. In these systems, Cas3 designates one of the core proteins shared widely by multiple types of CRISPR/Cas system. This model represents an HD-like endonuclease that occurs either separately or as the N-terminal region of Cas3, the helicase-containing CRISPR-associated protein.


Pssm-ID: 273711 [Multi-domain]  Cd Length: 176  Bit Score: 40.65  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086  159 LSYHVLTMLEIAKSLCNIYPLLN-------RSLLYSSIILHDLGKVRE-----LSGPvatTYTVEGNLLGHiSIASDEVA 226
Cdd:TIGR01596   1 LKEHLLDVAAVAEALPALRPRLAeklglelRELLKLAGLLHDLGKASPafqkkLRKA---EERGDRGEVRH-STLSAALL 76
                          90       100
                  ....*....|....*....|....*..
gi 515498086  227 -EAAKELGIDGEEVMLLRHMILAHHGK 252
Cdd:TIGR01596  77 yDLLEELGLEEELALLLALAIAGHHGG 103
 
Name Accession Description Interval E-value
PRK13480 PRK13480
3'-5' exoribonuclease YhaM; Provisional
1-313 0e+00

3'-5' exoribonuclease YhaM; Provisional


Pssm-ID: 237394 [Multi-domain]  Cd Length: 314  Bit Score: 638.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086   1 MRNVEKLNPGDSVENFFLIHRATQGVTAQGKDYMTLFLQDKSGDIEAKLWTVSKEDMQILKPETIVWVKGDVINYRGRKQ 80
Cdd:PRK13480   2 MKGIEELEVGEQVDHFLLIKSATKGVASNGKPFLTLILQDKSGDIEAKLWDVSPEDEATYVPETIVHVKGDIINYRGRKQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086  81 MKVNQFRLAKPEDGFKTQDFVAGAPLSPDEIQENISHYILDIENANLQRITRHLLKKYQDKFFTYPAASSHHHNFASGLS 160
Cdd:PRK13480  82 LKVNQIRLATEEDGVKISDFVEKAPLSKEEMQEEITQYIFEMENPNIQRITRHLLKKYQEEFLDYPAATKNHHEFVSGLA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086 161 YHVLTMLEIAKSLCNIYPLLNRSLLYSSIILHDLGKVRELSGPVATTYTVEGNLLGHISIASDEVAEAAKELGIDGEEVM 240
Cdd:PRK13480 162 YHVVSMLRLAKSICDLYPSLNKDLLYAGIILHDLGKVIELSGPVSTTYTLEGNLLGHISIMVNEIAKAADELQIDGEEVL 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515498086 241 LLRHMILAHHGKMEFGSPKLPHLKEAEILFFIDNIDAKMNMFEKAFKKTDKGQFTERIFGMENRQFYNPEKLD 313
Cdd:PRK13480 242 ILQHMVLSHHGKAEWGSPKPPLVKEAEILHYIDNIDAKMNMMDRALKKTKPGEFTERVFALDNRSFYKPTFLD 314
YhaM COG3481
3'-5' exoribonuclease YhaM, can participate in 23S rRNA maturation, HD superfamily ...
1-309 6.12e-150

3'-5' exoribonuclease YhaM, can participate in 23S rRNA maturation, HD superfamily [Translation, ribosomal structure and biogenesis]; 3'-5' exoribonuclease YhaM, can participate in 23S rRNA maturation, HD superfamily is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 442704 [Multi-domain]  Cd Length: 316  Bit Score: 423.06  E-value: 6.12e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086   1 MRNVEKLNPGDSVENFFLIHRATQGVTAQGKDYMTLFLQDKSGDIEAKLWTVSKEDMQILKPETIVWVKGDVINYRGRKQ 80
Cdd:COG3481    4 RKFIKDLKPGEEVDGFFLIKSKELRTTKNGKPYLSLTLQDKTGTIEAKIWDASEEDIEEFQPGDVVKVRGKVQEYQGRLQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086  81 MKVNQFRLAKPEDgFKTQDFVAGAPLSPDEIQENISHYILDIENANLQRITRHLL-KKYQDKFFTYPAASSHHHNFASGL 159
Cdd:COG3481   84 LKITRIRLADEEE-VDPSDFLPSSPKDIEEMYEELLELIDSIENPYLKRLLRAILdKEFRERFLTAPAAKSNHHAYIGGL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086 160 SYHVLTMLEIAKSLCNIYPLLNRSLLYSSIILHDLGKVRELSGPVATTYTVEGNLLGHISIASDEVAEAAKELG-IDGEE 238
Cdd:COG3481  163 LEHTLSVARLAKALADLYPELNRDLLIAGAILHDIGKVRELSGPPGTEYTDEGQLLGHIVLGVEMIEEAAAELGdFPEEL 242
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498086 239 VMLLRHMILAHHGKMEFGSPKLPHLKEAEILFFIDNIDAKMNMFEKAFKKTDK-GQFTERIFGMENRqFYNP 309
Cdd:COG3481  243 LLLLKHMILSHHGELEWGSPKRPKTPEAEILHYADNLDAKMNMFERALEKVEPgGEWTEYIRALDRR-FYKP 313
YhaM_OBF_like cd04492
YhaM_OBF_like: A subfamily of OB folds similar to that found in Bacillus subtilis YhaM and ...
14-94 1.55e-28

YhaM_OBF_like: A subfamily of OB folds similar to that found in Bacillus subtilis YhaM and Staphylococcus aureus cmp-binding factor-1 (SaCBF1). Both these proteins are 3'-to-5'exoribonucleases. YhaM requires Mn2+ or Co2+ for activity and is inactive in the presence of Mg2+. YhaM also has a Mn2+ dependent 3'-to-5'single-stranded DNA exonuclease activity. SaCBF is also a double-stranded DNA binding protein, binding specifically to cmp, the replication enhancer found in S. aureus plasmid pT181. Proteins in this group combine an N-terminal OB fold with a C-terminal HD domain. The HD domain is found in metal-dependent phosphohydrolases.


Pssm-ID: 239938 [Multi-domain]  Cd Length: 83  Bit Score: 104.98  E-value: 1.55e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086  14 ENFFLIHRATQGVTAQGKDYMTLFLQDKSGDIEAKLWTVSKEDMQILKPETIVWVKGDVINYRGRKQMKVNQFRLAKPED 93
Cdd:cd04492    1 DGFFLIKSKELRTAKNGKPYLALTLQDKTGEIEAKLWDASEEDEEKFKPGDIVHVKGRVEEYRGRLQLKIQRIRLVTEED 80

                 .
gi 515498086  94 G 94
Cdd:cd04492   81 G 81
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
150-277 3.40e-11

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 59.62  E-value: 3.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086   150 SHHHNFasglsYHVLTMLEIAKSLCNIYPLLNRSLLYSSIILHDLGKVRELSGPVATTytveGNLLGHISIAsdevAEAA 229
Cdd:smart00471   1 SDYHVF-----EHSLRVAQLAAALAEELGLLDIELLLLAALLHDIGKPGTPDSFLVKT----SVLEDHHFIG----AEIL 67
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 515498086   230 KELGIDGEEVMLLRHMILAHHGkMEFGSPKLPHLKEAEILFFIDNIDA 277
Cdd:smart00471  68 LEEEEPRILEEILRTAILSHHE-RPDGLRGEPITLEARIVKVADRLDA 114
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
161-277 7.85e-11

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 58.40  E-value: 7.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086  161 YHVLTMLEIAKSLCNIYPLLNRSLLYSSIILHDLGKvrelsGPVATTYTVEGNLLGHISIASDEVAEAAKELGidgeeVM 240
Cdd:pfam01966   3 EHSLRVALLARELAEELGELDRELLLLAALLHDIGK-----GPFGDEKPEFEIFLGHAVVGAEILRELEKRLG-----LE 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 515498086  241 LLRHMILAHHGKMEFGSPKLPHLKEAEILFFIDNIDA 277
Cdd:pfam01966  73 DVLKLILEHHESWEGAGYPEEISLEARIVKLADRLDA 109
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
152-288 7.50e-09

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 53.50  E-value: 7.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086 152 HHNFasglsYHVLTMLEIAKSLCNIYPL--LNRSLLYSSIILHDLGKVRELSGPvattYTVEGNLLGHISIASDEVAEAA 229
Cdd:cd00077    1 EHRF-----EHSLRVAQLARRLAEELGLseEDIELLRLAALLHDIGKPGTPDAI----TEEESELEKDHAIVGAEILREL 71
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498086 230 KELGIDGEEVMLLRHMILAHHGKMEFGSPKL-----PHLKEAEILFFIDNIDAKMNMFEKAFKK 288
Cdd:cd00077   72 LLEEVIKLIDELILAVDASHHERLDGLGYPDglkgeEITLEARIVKLADRLDALRRDSREKRRR 135
tRNA_anti-codon pfam01336
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ...
29-88 3.23e-05

OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.


Pssm-ID: 460164 [Multi-domain]  Cd Length: 75  Bit Score: 41.45  E-value: 3.23e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498086   29 QGKDYMTLFLQDKSGDIEAKLW-TVSKEDMQILKPETIVWVKGDVINYRGRK-QMKVNQFRL 88
Cdd:pfam01336  13 SGGKLLFLTLRDGTGSIQVVVFkEEAEKLAKKLKEGDVVRVTGKVKKRKGGElELVVEEIEL 74
RPA2_OBF_family cd03524
RPA2_OBF_family: A family of oligonucleotide binding (OB) folds with similarity to the OB fold ...
29-88 3.03e-04

RPA2_OBF_family: A family of oligonucleotide binding (OB) folds with similarity to the OB fold of the single strand (ss) DNA-binding domain (DBD)-D of human RPA2 (also called RPA32). RPA2 is a subunit of Replication protein A (RPA). RPA is a nuclear ssDNA-binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). RPA contains six OB folds, which are involved in ssDNA binding and in trimerization. The ssDNA binding mechanism is believed to be multistep and to involve conformational change. This family also includes OB folds similar to those found in Escherichia coli SSB, the wedge domain of E. coli RecG (a branched-DNA-specific helicase), E. coli ssDNA specific exodeoxyribonuclease VII large subunit, Pyrococcus abyssi DNA polymerase II (Pol II) small subunit, Sulfolobus solfataricus SSB, and Bacillus subtilis YhaM (a 3'-to-5'exoribonuclease). It also includes the OB folds of breast cancer susceptibility gene 2 protein (BRCA2), Oxytricha nova telomere end binding protein (TEBP), Saccharomyces cerevisiae telomere-binding protein (Cdc13), and human protection of telomeres 1 protein (POT1).


Pssm-ID: 239601 [Multi-domain]  Cd Length: 75  Bit Score: 38.88  E-value: 3.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498086  29 QGKDYMTLFLQDKSGD-IEAKLWT-VSKEDMQILKPETIVWVKGDVINYRGRKQMKVNQFRL 88
Cdd:cd03524   14 TEGKVLIFTLTDGTGGtIRVTLFGeLAEELENLLKEGQVVYIKGKVKKFRGRLQLIVESIEL 75
cas3_HD TIGR01596
CRISPR-associated endonuclease Cas3-HD; CRISPR/Cas systems are widespread, mobile systems for ...
159-252 3.19e-04

CRISPR-associated endonuclease Cas3-HD; CRISPR/Cas systems are widespread, mobile systems for host defense against invasive elements such as phage. In these systems, Cas3 designates one of the core proteins shared widely by multiple types of CRISPR/Cas system. This model represents an HD-like endonuclease that occurs either separately or as the N-terminal region of Cas3, the helicase-containing CRISPR-associated protein.


Pssm-ID: 273711 [Multi-domain]  Cd Length: 176  Bit Score: 40.65  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086  159 LSYHVLTMLEIAKSLCNIYPLLN-------RSLLYSSIILHDLGKVRE-----LSGPvatTYTVEGNLLGHiSIASDEVA 226
Cdd:TIGR01596   1 LKEHLLDVAAVAEALPALRPRLAeklglelRELLKLAGLLHDLGKASPafqkkLRKA---EERGDRGEVRH-STLSAALL 76
                          90       100
                  ....*....|....*....|....*..
gi 515498086  227 -EAAKELGIDGEEVMLLRHMILAHHGK 252
Cdd:TIGR01596  77 yDLLEELGLEEELALLLALAIAGHHGG 103
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
180-311 3.89e-04

HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal structure and biogenesis, General function prediction only];


Pssm-ID: 441028 [Multi-domain]  Cd Length: 191  Bit Score: 40.65  E-value: 3.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086 180 LNRSLLYSSIILHDLGKVRElsgpvattYTVEGNllgHISIASDEVAEAAKELGIDGEEVMLLRHMILAHHGKMEfgspK 259
Cdd:COG1418   39 ADVEVAKRAALLHDIGKAKD--------HEVEGS---HAEIGAELARKYLESLGFPEEEIEAVVHAIEAHSFSGG----I 103
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515498086 260 LPHLKEAEILFFIDNIDA-KMNMFEKAFkktdkgqfteRIFGMENRQFYNPEK 311
Cdd:COG1418  104 EPESLEAKIVQDADRLDAlGAIGVARAF----------AIGGQAGRELRDPED 146
Cas3''_I cd09641
CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced Short ...
159-288 5.40e-03

CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; HD-like nuclease, specifically digesting double-stranded oligonucleotides and preferably cleaving at G:C pairs; signature gene for Type I


Pssm-ID: 193608 [Multi-domain]  Cd Length: 200  Bit Score: 37.25  E-value: 5.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498086 159 LSYHVL----TMLEIAKSLCN---IYPLLNRSLLYSSIILHDLGKVRE-----LSGPVATTYTVEGNLLGHiSIASDEVA 226
Cdd:cd09641    9 LLEHLLdvaaWDAELAEEFARklgLELGLSRELLALAGLLHDLGKATPafqkyLRGGKEALREGKRKEVRH-SLLGALLL 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515498086 227 -EAAKELGIDGEEVMLLRHMILAHHGKMEFGSPKLPHLKEAEILFFIDNIDAKMNMFEKAFKK 288
Cdd:cd09641   88 yELLKELGLDEELALLLAYAIAGHHGGLPDVLLLLDEDDESALKERLEELDEEKLLLELWEEE 150
 
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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