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Conserved domains on  [gi|1327793287|ref|XP_023367563|]
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DNA cross-link repair 1A protein [Otolemur garnettii]

Protein Classification

DNA cross-link repair protein 1A( domain architecture ID 10888854)

DNA cross-link repair protein 1A is required for DNA interstrand cross-link repair and checkpoint-mediated cell cycle arrest in early prophase in response to spindle stress

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 691-846 2.70e-108

5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) which is a 5'-exonuclease and functions in interstrand cross-links (ICL) repair. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


:

Pssm-ID: 293856 [Multi-domain]  Cd Length: 157  Bit Score: 333.33  E-value: 2.70e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  691 ESPNIGELRKKTCPFYKKIPGTGFTVDAFQYGVVEGCTAYFLTHFHSDHYAGLSKHFTFPVYCSEITGNLLKNKLHVQEQ 770
Cdd:cd16298      1 SSTNGEGKRKKTCPFYKKIPGTGFTVDAFQYGVIEGCTAYFLTHFHSDHYCGLTKKFKFPIYCSKITGNLVKSKLKVEEQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327793287  771 YIHPLPMDTECVVNGVKVVLLDANHCPGAVMILFYLPNGTIILHTGDFRADPSMERS-LLAGQKVHTLYLDTTYCSP 846
Cdd:cd16298     81 YINVLPMNTECIVNGVKVVLLDANHCPGAVMILFRLPSGTLVLHTGDFRADPSMERYpELIGQKIHTLYLDTTYCSP 157
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 916-1022 4.90e-48

DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in pfam00753 and are common to all metallo-beta-lactamases. The fifth motif appears to be specific to function. This entry represents the fifth motif from metallo-beta-lactamases involved in DNA repair.


:

Pssm-ID: 429512  Cd Length: 108  Bit Score: 166.30  E-value: 4.90e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  916 PEINSLITTDMCSSLVHLLPMMQINFKDLQSHLKKCGGKYDQILAFRPTGWTHSNKLTSIADVIPKT-KGNISIYGIPYS 994
Cdd:pfam07522    1 PEILSLLTTDPLSTQIHVVPMPKLSYEALLDYLTARKDHFDSVLAIRPTGWTYRPPKTEVSDRIGPSiRGRITIYGVPYS 80

                           90       100
                   ....*....|....*....|....*...
gi 1327793287  995 EHSSYLEMKRFVQWLKPQKIIPTVNVGN 1022
Cdd:pfam07522   81 EHSSFDELKEFVQFLRPKKIIPTVNVGG 108
 
Name Accession Description Interval E-value
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 691-846 2.70e-108

5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) which is a 5'-exonuclease and functions in interstrand cross-links (ICL) repair. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293856 [Multi-domain]  Cd Length: 157  Bit Score: 333.33  E-value: 2.70e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  691 ESPNIGELRKKTCPFYKKIPGTGFTVDAFQYGVVEGCTAYFLTHFHSDHYAGLSKHFTFPVYCSEITGNLLKNKLHVQEQ 770
Cdd:cd16298      1 SSTNGEGKRKKTCPFYKKIPGTGFTVDAFQYGVIEGCTAYFLTHFHSDHYCGLTKKFKFPIYCSKITGNLVKSKLKVEEQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327793287  771 YIHPLPMDTECVVNGVKVVLLDANHCPGAVMILFYLPNGTIILHTGDFRADPSMERS-LLAGQKVHTLYLDTTYCSP 846
Cdd:cd16298     81 YINVLPMNTECIVNGVKVVLLDANHCPGAVMILFRLPSGTLVLHTGDFRADPSMERYpELIGQKIHTLYLDTTYCSP 157
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 916-1022 4.90e-48

DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in pfam00753 and are common to all metallo-beta-lactamases. The fifth motif appears to be specific to function. This entry represents the fifth motif from metallo-beta-lactamases involved in DNA repair.


Pssm-ID: 429512  Cd Length: 108  Bit Score: 166.30  E-value: 4.90e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  916 PEINSLITTDMCSSLVHLLPMMQINFKDLQSHLKKCGGKYDQILAFRPTGWTHSNKLTSIADVIPKT-KGNISIYGIPYS 994
Cdd:pfam07522    1 PEILSLLTTDPLSTQIHVVPMPKLSYEALLDYLTARKDHFDSVLAIRPTGWTYRPPKTEVSDRIGPSiRGRITIYGVPYS 80

                           90       100
                   ....*....|....*....|....*...
gi 1327793287  995 EHSSYLEMKRFVQWLKPQKIIPTVNVGN 1022
Cdd:pfam07522   81 EHSSFDELKEFVQFLRPKKIIPTVNVGG 108
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 731-885 3.22e-12

RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 69.83  E-value: 3.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  731 FLTHFHSDHyAGL-----SKHFTFPVYCS----EITGNLLKNKLHVQE------------------QYIHPLPMDTECVV 783
Cdd:COG1236     55 VLTHAHLDH-SGAlpllvKEGFRGPIYATpataDLARILLGDSAKIQEeeaeaeplyteedaeralELFQTVDYGEPFEI 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  784 NGVKVVLLDANHCPGAVMILFYLpNGTIILHTGDF--RADPsmersLLAG----QKVHTLYLDTTYCSPEYtfPSQQEVI 857
Cdd:COG1236    134 GGVRVTFHPAGHILGSAQVELEV-GGKRIVFSGDYgrEDDP-----LLAPpepvPPADVLITESTYGDRLH--PPREEVE 205

                          170       180
                   ....*....|....*....|....*...
gi 1327793287  858 QfAINTAFEAVTLNPCALVVcGTYSIGK 885
Cdd:COG1236    206 A-ELAEWVRETLARGGTVLI-PAFALGR 231
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 731-831 6.29e-08

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 53.71  E-value: 6.29e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287   731 FLTHFHSDHYAG---LSKHFTFPVYCSEITGNLLKNKLHVQEQYIHPLPM--DTECVVNGVKVVLLD--------ANHCP 797
Cdd:smart00849   40 ILTHGHPDHIGGlpeLLEAPGAPVYAPEGTAELLKDLLALLGELGAEAEPapPDRTLKDGDELDLGGgelevihtPGHTP 119

                            90       100       110
                    ....*....|....*....|....*....|....
gi 1327793287   798 GAVMilFYLPNGTiILHTGDFRADPSMERSLLAG 831
Cdd:smart00849  120 GSIV--LYLPEGK-ILFTGDLLFAGGDGRTLVDG 150
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
731-838 1.32e-04

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 44.28  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  731 FLTHFHSDHYAG---LSKHFTFPVY-CSEITGNLLKNKLHVQEQYIHPLPM------------DTECVVNGVKVVLLDAN 794
Cdd:pfam00753   48 ILTHGHFDHIGGlgeLAEATDVPVIvVAEEARELLDEELGLAASRLGLPGPpvvplppdvvleEGDGILGGGLGLLVTHG 127

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1327793287  795 HCPGAVMILFYLPNGTiILHTGDFRADPSMERSLLAGQKVHTLY 838
Cdd:pfam00753  128 PGHGPGHVVVYYGGGK-VLFTGDLLFAGEIGRLDLPLGGLLVLH 170
 
Name Accession Description Interval E-value
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 691-846 2.70e-108

5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) which is a 5'-exonuclease and functions in interstrand cross-links (ICL) repair. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293856 [Multi-domain]  Cd Length: 157  Bit Score: 333.33  E-value: 2.70e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  691 ESPNIGELRKKTCPFYKKIPGTGFTVDAFQYGVVEGCTAYFLTHFHSDHYAGLSKHFTFPVYCSEITGNLLKNKLHVQEQ 770
Cdd:cd16298      1 SSTNGEGKRKKTCPFYKKIPGTGFTVDAFQYGVIEGCTAYFLTHFHSDHYCGLTKKFKFPIYCSKITGNLVKSKLKVEEQ 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327793287  771 YIHPLPMDTECVVNGVKVVLLDANHCPGAVMILFYLPNGTIILHTGDFRADPSMERS-LLAGQKVHTLYLDTTYCSP 846
Cdd:cd16298     81 YINVLPMNTECIVNGVKVVLLDANHCPGAVMILFRLPSGTLVLHTGDFRADPSMERYpELIGQKIHTLYLDTTYCSP 157
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 699-846 1.09e-89

SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) and Saccharomyces cerevisiae Pso2 protein (PSOralen derivative sensitive 2, also known as SNM1, sensitive to nitrogen mustard 1), both proteins are 5'-exonucleases and function in interstrand cross-links (ICL) repair. Also includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein, and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293831  Cd Length: 160  Bit Score: 283.66  E-value: 1.09e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  699 RKKTCPFYKKIPGTGFTVDAFQYGVVEGCTAYFLTHFHSDHYAGLSKHFTF-PVYCSEITGNLLKNKLHVQEQYIHPLPM 777
Cdd:cd16273      9 RKKPCPFYKIIPGTSFVVDAFKYGKIPGISAYFLSHFHSDHYGGLTKSWSHgPIYCSEITANLVKLKLKVDEEYIVVLPM 88

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327793287  778 DTECVVNG-VKVVLLDANHCPGAVMILFYLPNGTIILHTGDFRADPSM--ERSLLAGQKVHTLYLDTTYCSP 846
Cdd:cd16273     89 NTPVEIDGdVSVTLLDANHCPGAVMFLFELPDGRRILHTGDFRANPEMleHPLLLGKRRIDTVYLDTTYCNP 160
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 916-1022 4.90e-48

DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in pfam00753 and are common to all metallo-beta-lactamases. The fifth motif appears to be specific to function. This entry represents the fifth motif from metallo-beta-lactamases involved in DNA repair.


Pssm-ID: 429512  Cd Length: 108  Bit Score: 166.30  E-value: 4.90e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  916 PEINSLITTDMCSSLVHLLPMMQINFKDLQSHLKKCGGKYDQILAFRPTGWTHSNKLTSIADVIPKT-KGNISIYGIPYS 994
Cdd:pfam07522    1 PEILSLLTTDPLSTQIHVVPMPKLSYEALLDYLTARKDHFDSVLAIRPTGWTYRPPKTEVSDRIGPSiRGRITIYGVPYS 80

                           90       100
                   ....*....|....*....|....*...
gi 1327793287  995 EHSSYLEMKRFVQWLKPQKIIPTVNVGN 1022
Cdd:pfam07522   81 EHSSFDELKEFVQFLRPKKIIPTVNVGG 108
artemis-SNM1C-like_MBL-fold cd16297
artemis-SNM1C and related proteins; MBL-fold metallo-hydrolase domain; Includes the nuclease ...
 729-846 1.51e-18

artemis-SNM1C and related proteins; MBL-fold metallo-hydrolase domain; Includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. Inactivation of Artemis causes severe combined immunodeficiency (SCID). Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293855  Cd Length: 171  Bit Score: 84.10  E-value: 1.51e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  729 AYFLTHFHSDHYAGLSKHF---------TFPVYCSEITGNLL--KNKLHVQEQYIHPLPMDTECVVN----------GVK 787
Cdd:cd16297     28 AYFLSHCHKDHMKGLRAPGlkrrlkaslKVKLYCSPVTKELLltNPKYAFWENHIVSLEIDTPTQISlvdeatgekeDVV 107

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327793287  788 VVLLDANHCPGAVMILFYLPNGTiILHTGDFR---ADPSMERSLLAGQKV---HTLYLDTTYCSP 846
Cdd:cd16297    108 VTLLPAGHCPGSVMFLFQGNNGT-VLYTGDFRlavGEAARMELLHSGDRVkdiQSVYLDTTFCDP 171
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 731-885 3.22e-12

RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 69.83  E-value: 3.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  731 FLTHFHSDHyAGL-----SKHFTFPVYCS----EITGNLLKNKLHVQE------------------QYIHPLPMDTECVV 783
Cdd:COG1236     55 VLTHAHLDH-SGAlpllvKEGFRGPIYATpataDLARILLGDSAKIQEeeaeaeplyteedaeralELFQTVDYGEPFEI 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  784 NGVKVVLLDANHCPGAVMILFYLpNGTIILHTGDF--RADPsmersLLAG----QKVHTLYLDTTYCSPEYtfPSQQEVI 857
Cdd:COG1236    134 GGVRVTFHPAGHILGSAQVELEV-GGKRIVFSGDYgrEDDP-----LLAPpepvPPADVLITESTYGDRLH--PPREEVE 205

                          170       180
                   ....*....|....*....|....*...
gi 1327793287  858 QfAINTAFEAVTLNPCALVVcGTYSIGK 885
Cdd:COG1236    206 A-ELAEWVRETLARGGTVLI-PAFALGR 231
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
729-823 1.96e-11

mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 67.78  E-value: 1.96e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  729 AYFLTHFHSDHYAGLS---KHFTFPVYCSEITGNLLKNKL----HVQEQYIHPLPMDTECVVNGVKVVLLDANH-CPGAV 800
Cdd:COG0595     66 GIVLTHGHEDHIGALPyllKELNVPVYGTPLTLALLEAKLkehgLLKKVKLHVVKPGDRIKFGPFKVEFFRVTHsIPDSL 145

                           90       100
                   ....*....|....*....|...
gi 1327793287  801 MILFYLPNGTIIlHTGDFRADPS 823
Cdd:COG0595    146 GLAIRTPAGTIV-HTGDFKFDQT 167
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 731-845 2.69e-11

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 64.74  E-value: 2.69e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  731 FLTHFHSDHYAGLS---KHFTFPVYCSEITGNLLKNKL----HVQEQYIHPLPMDTECVVNGVKVVLLDANHC-PGAVMI 802
Cdd:cd07714     60 FITHGHEDHIGALPyllPELNVPIYATPLTLALIKKKLeefkLIKKVKLNEIKPGERIKLGDFEVEFFRVTHSiPDSVGL 139

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1327793287  803 LFYLPNGTIIlHTGDFRADPS--------MER-SLLAGQKVHTLYLDTTYCS 845
Cdd:cd07714    140 AIKTPEGTIV-HTGDFKFDQTpvdgkptdLEKlAELGKEGVLLLLSDSVHVS 190
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 731-860 5.39e-11

Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism];


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 64.15  E-value: 5.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  731 FLTHFHSDHYAG---LSKHFT---FPVYCSEITGNLLKNKLHVQEQY------IHPLPMDTECVVNGVKVVLLDANHcpG 798
Cdd:COG1235     73 LLTHEHADHIAGlddLRPRYGpnpIPVYATPGTLEALERRFPYLFAPypgkleFHEIEPGEPFEIGGLTVTPFPVPH--D 150

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327793287  799 AVMILFYL--PNGTIILHTGDFRADPSMERSLLAGqkVHTLYLDTTYCSPEYTFPSQQEVIQFA 860
Cdd:COG1235    151 AGDPVGYRieDGGKKLAYATDTGYIPEEVLELLRG--ADLLILDATYDDPEPGHLSNEEALELL 212
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 727-820 2.51e-09

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 58.01  E-value: 2.51e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  727 CTAYFLTHFHSDHYAGLSK-HFTFPVYCSEITGNLLKNKLHV------QEQYIHPLPMDTECVVnG---VKVVLLDanH- 795
Cdd:cd07732     76 VDAVLLSHAHLDHYGLLNYlRPDIPVYMGEATKRILKALLPFfgegdpVPRNIRVFESGKSFTI-GdftVTPYLVD--Hs 152

                           90       100
                   ....*....|....*....|....*
gi 1327793287  796 CPGAVMILFYLPNGTiILHTGDFRA 820
Cdd:cd07732    153 APGAYAFLIEAPGKR-IFYTGDFRF 176
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 731-831 6.29e-08

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 53.71  E-value: 6.29e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287   731 FLTHFHSDHYAG---LSKHFTFPVYCSEITGNLLKNKLHVQEQYIHPLPM--DTECVVNGVKVVLLD--------ANHCP 797
Cdd:smart00849   40 ILTHGHPDHIGGlpeLLEAPGAPVYAPEGTAELLKDLLALLGELGAEAEPapPDRTLKDGDELDLGGgelevihtPGHTP 119

                            90       100       110
                    ....*....|....*....|....*....|....
gi 1327793287   798 GAVMilFYLPNGTiILHTGDFRADPSMERSLLAG 831
Cdd:smart00849  120 GSIV--LYLPEGK-ILFTGDLLFAGGDGRTLVDG 150
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 710-831 2.56e-07

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 51.90  E-value: 2.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  710 PGTGFTVDAFQYGVVEG--CTAYFLTHFHSDHYAG---LSKHFTFPVYCSEITGNLLKN----------KLHVQEQYIHP 774
Cdd:cd06262     27 PGAGALEKILEAIEELGlkIKAILLTHGHFDHIGGlaeLKEAPGAPVYIHEADAELLEDpelnlaffggGPLPPPEPDIL 106

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1327793287  775 LPMDTECVVNGVKVVLLDA-NHCPGAVMilFYLPNGTiILHTGDFRADPSMERSLLAG 831
Cdd:cd06262    107 LEDGDTIELGGLELEVIHTpGHTPGSVC--FYIEEEG-VLFTGDTLFAGSIGRTDLPG 161
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
728-843 2.15e-05

Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 47.11  E-value: 2.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  728 TAYFLTHFHSDHYAGL-----SKHFT-----FPVYCSEITGNLLKNKLHVQEQY------IHPLPMDTECVVNGVKVVLL 791
Cdd:COG1234     54 DAIFITHLHGDHIAGLpgllsTRSLAgrekpLTIYGPPGTKEFLEALLKASGTDldfpleFHEIEPGEVFEIGGFTVTAF 133

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1327793287  792 DANHCPGAVMILFYLPNGTIILhTGDFRADPSMERsllAGQKVHTLYLDTTY 843
Cdd:COG1234    134 PLDHPVPAYGYRFEEPGRSLVY-SGDTRPCEALVE---LAKGADLLIHEATF 181
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 731-817 1.08e-04

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 44.68  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  731 FLTHFHSDHYAG---LSKHFTFPVYCSEITGNLLKNKLHVQEQYIHPLPMDT------ECVVNGVKVVLLDAN-HCPGav 800
Cdd:COG0491     56 LLTHLHPDHVGGlaaLAEAFGAPVYAHAAEAEALEAPAAGALFGREPVPPDRtledgdTLELGGPGLEVIHTPgHTPG-- 133

                           90
                   ....*....|....*..
gi 1327793287  801 MILFYLPNGTiILHTGD 817
Cdd:COG0491    134 HVSFYVPDEK-VLFTGD 149
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 731-801 1.20e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 44.00  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  731 FLTHFHSDHYAGLS--KHFTF------PVYCSEITGNLLKNKLHVQEQY----------IHPLPMDTECVVNGVKVVLLD 792
Cdd:cd16279     71 LLTHAHADHIHGLDdlRPFNRlqqrpiPVYASEETLDDLKRRFPYFFAAtggggvpkldLHIIEPDEPFTIGGLEITPLP 150


                   ....*....
gi 1327793287  793 ANHCPGAVM 801
Cdd:cd16279    151 VLHGKLPSL 159
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
731-838 1.32e-04

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 44.28  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  731 FLTHFHSDHYAG---LSKHFTFPVY-CSEITGNLLKNKLHVQEQYIHPLPM------------DTECVVNGVKVVLLDAN 794
Cdd:pfam00753   48 ILTHGHFDHIGGlgeLAEATDVPVIvVAEEARELLDEELGLAASRLGLPGPpvvplppdvvleEGDGILGGGLGLLVTHG 127

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1327793287  795 HCPGAVMILFYLPNGTiILHTGDFRADPSMERSLLAGQKVHTLY 838
Cdd:pfam00753  128 PGHGPGHVVVYYGGGK-VLFTGDLLFAGEIGRLDLPLGGLLVLH 170
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 731-848 3.04e-03

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 39.99  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  731 FLTHFHSDHYAG---LSKHFTFPVYCSEITGNLLK------NKLHVQEQYIHPLPMDTECVVN--GVKVVLLDANH---- 795
Cdd:pfam12706   33 LLTHDHYDHLAGlldLREGRPRPLYAPLGVLAHLRrnfpylFLLEHYGVRVHEIDWGESFTVGdgGLTVTATPARHgspr 112

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1327793287  796 --CPGAVMILFYL--PNGTIILHTGDFRADPSMERSLLAGQKVhtLYLDTTYCSPEY 848
Cdd:pfam12706  113 glDPNPGDTLGFRieGPGKRVYYAGDTGYFPDEIGERLGGADL--LLLDGGAWRDDE 167
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 710-817 7.25e-03

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 39.13  E-value: 7.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327793287  710 PGTGFTVDAFQYGVVEGCTAYFLTHFHSDHY-----AGLSKHFTfPVYCSEITGNLLKNKLHVQeqyIHPLPMDTECVVN 784
Cdd:COG2220     32 RASPVNPLPLDPEDLPKIDAVLVTHDHYDHLddatlRALKRTGA-TVVAPLGVAAWLRAWGFPR---VTELDWGESVELG 107

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1327793287  785 GVKVVLLDANHCPG--------AVMILFYLPNGTiILHTGD 817
Cdd:COG2220    108 GLTVTAVPARHSSGrpdrngglWVGFVIETDGKT-IYHAGD 147
 
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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