NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1338686468|ref|NP_001347368|]
View 

DNA cross-link repair 1A protein isoform 3 [Mus musculus]

Protein Classification

DNA cross-link repair protein( domain architecture ID 11039898)

DNA cross-link repair protein similar to Arabidopsis thaliana SNM1, which is involved in the repair of DNA lesions formed by oxidative stress

Gene Ontology:  GO:0006974|GO:0005634
PubMed:  12177301|20528238

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 160-315 2.84e-102

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.


The actual alignment was detected with superfamily member cd16298:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 157  Bit Score: 303.67  E-value: 2.84e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 160 SESSGAGEVRRTCPFYKRIPGTGFTVDAFQYGEIEGCTAYFLTHFHSDHYAGLSKDFTRPVYCSEITGNLLKKKLRVQEQ 239
Cdd:cd16298     1 SSTNGEGKRKKTCPFYKKIPGTGFTVDAFQYGVIEGCTAYFLTHFHSDHYCGLTKKFKFPIYCSKITGNLVKSKLKVEEQ 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1338686468 240 YIRQLPMDTECVVDSVKVVLLDANHCPGATMILFQLPNGAVILHTGDFRADPSMERS-RLAGRKVHTLFLDTTYCSP 315
Cdd:cd16298    81 YINVLPMNTECIVNGVKVVLLDANHCPGAVMILFRLPSGTLVLHTGDFRADPSMERYpELIGQKIHTLYLDTTYCSP 157
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 385-491 2.36e-50

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: 167.45  E-value: 2.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 385 PEVSSLITTDMCDSLVHLLPMMQINFKGLQSHLKKCGGKYDQILAFRPTGWTHSNNITS-TADIIPQTRGNISIYGIPYS 463
Cdd:pfam07522   1 PEILSLLTTDPLSTQIHVVPMPKLSYEALLDYLTARKDHFDSVLAIRPTGWTYRPPKTEvSDRIGPSIRGRITIYGVPYS 80

                          90       100
                  ....*....|....*....|....*...
gi 1338686468 464 EHSSYLEMKRFVQWLKPQKIIPTVNVGS 491
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 ...
 160-315 2.84e-102

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: 303.67  E-value: 2.84e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 160 SESSGAGEVRRTCPFYKRIPGTGFTVDAFQYGEIEGCTAYFLTHFHSDHYAGLSKDFTRPVYCSEITGNLLKKKLRVQEQ 239
Cdd:cd16298     1 SSTNGEGKRKKTCPFYKKIPGTGFTVDAFQYGVIEGCTAYFLTHFHSDHYCGLTKKFKFPIYCSKITGNLVKSKLKVEEQ 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1338686468 240 YIRQLPMDTECVVDSVKVVLLDANHCPGATMILFQLPNGAVILHTGDFRADPSMERS-RLAGRKVHTLFLDTTYCSP 315
Cdd:cd16298    81 YINVLPMNTECIVNGVKVVLLDANHCPGAVMILFRLPSGTLVLHTGDFRADPSMERYpELIGQKIHTLYLDTTYCSP 157
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 385-491 2.36e-50

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: 167.45  E-value: 2.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 385 PEVSSLITTDMCDSLVHLLPMMQINFKGLQSHLKKCGGKYDQILAFRPTGWTHSNNITS-TADIIPQTRGNISIYGIPYS 463
Cdd:pfam07522   1 PEILSLLTTDPLSTQIHVVPMPKLSYEALLDYLTARKDHFDSVLAIRPTGWTYRPPKTEvSDRIGPSIRGRITIYGVPYS 80

                          90       100
                  ....*....|....*....|....*...
gi 1338686468 464 EHSSYLEMKRFVQWLKPQKIIPTVNVGS 491
Cdd:pfam07522  81 EHSSFDELKEFVQFLRPKKIIPTVNVGG 108
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 157-354 7.80e-13

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 70.22  E-value: 7.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 157 MNISESSGAGEVRRTCpFYKRIPGTGFTVDA--FQYGEIEGCTAY----------FLTHFHSDHyAGL-----SKDFTRP 219
Cdd:COG1236     1 MKLTFLGAAGEVTGSC-YLLETGGTRILIDCglFQGGKERNWPPFpfrpsdvdavVLTHAHLDH-SGAlpllvKEGFRGP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 220 VYCS----EITGNLLKKKLRVQE------------------QYIRQLPMDTECVVDSVKVVLLDANHCPGATMILFQLpN 277
Cdd:COG1236    79 IYATpataDLARILLGDSAKIQEeeaeaeplyteedaeralELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEV-G 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1338686468 278 GAVILHTGDF--RADPSMERSRLAgRKVHTLFLDTTYCSPEYtfPSQQEVIQfAINTAFEAVTLNPRALVVcGTYCIGK 354
Cdd:COG1236   158 GKRIVFSGDYgrEDDPLLAPPEPV-PPADVLITESTYGDRLH--PPREEVEA-ELAEWVRETLARGGTVLI-PAFALGR 231
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 200-300 9.82e-07

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: 49.09  E-value: 9.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468  200 FLTHFHSDHYAG---LSKDFTRPVYCSEITGNLLKKKLRVQEQ--YIRQLPMDTECVVDSVKVVL----LDANHCPGATM 270
Cdd:smart00849  40 ILTHGHPDHIGGlpeLLEAPGAPVYAPEGTAELLKDLLALLGElgAEAEPAPPDRTLKDGDELDLgggeLEVIHTPGHTP 119

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1338686468  271 --ILFQLPNGaVILHTGDFRADPSMERSRLAG 300
Cdd:smart00849 120 gsIVLYLPEG-KILFTGDLLFAGGDGRTLVDG 150
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 200-317 2.92e-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: 38.83  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 200 FLTHFHSDHYAG---LSKDFTRPVYCSEITGNLLKK---KLRVQEQYIRQL-PMD----TECVVDSVKVVLLDANH-CPG 267
Cdd:pfam12706  33 LLTHDHYDHLAGlldLREGRPRPLYAPLGVLAHLRRnfpYLFLLEHYGVRVhEIDwgesFTVGDGGLTVTATPARHgSPR 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1338686468 268 ATMILFQLPNGAVI-------LHTGDFRADPSMERSRLAGRKVhtLFLDTTYCSPEY 317
Cdd:pfam12706 113 GLDPNPGDTLGFRIegpgkrvYYAGDTGYFPDEIGERLGGADL--LLLDGGAWRDDE 167
 
Name Accession Description Interval E-value
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 160-315 2.84e-102

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: 303.67  E-value: 2.84e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 160 SESSGAGEVRRTCPFYKRIPGTGFTVDAFQYGEIEGCTAYFLTHFHSDHYAGLSKDFTRPVYCSEITGNLLKKKLRVQEQ 239
Cdd:cd16298     1 SSTNGEGKRKKTCPFYKKIPGTGFTVDAFQYGVIEGCTAYFLTHFHSDHYCGLTKKFKFPIYCSKITGNLVKSKLKVEEQ 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1338686468 240 YIRQLPMDTECVVDSVKVVLLDANHCPGATMILFQLPNGAVILHTGDFRADPSMERS-RLAGRKVHTLFLDTTYCSP 315
Cdd:cd16298    81 YINVLPMNTECIVNGVKVVLLDANHCPGAVMILFRLPSGTLVLHTGDFRADPSMERYpELIGQKIHTLYLDTTYCSP 157
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 169-315 1.11e-87

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: 266.33  E-value: 1.11e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 169 RRTCPFYKRIPGTGFTVDAFQYGEIEGCTAYFLTHFHSDHYAGLSKDFTR-PVYCSEITGNLLKKKLRVQEQYIRQLPMD 247
Cdd:cd16273    10 KKPCPFYKIIPGTSFVVDAFKYGKIPGISAYFLSHFHSDHYGGLTKSWSHgPIYCSEITANLVKLKLKVDEEYIVVLPMN 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1338686468 248 TECVVDS-VKVVLLDANHCPGATMILFQLPNGAVILHTGDFRADPSM--ERSRLAGRKVHTLFLDTTYCSP 315
Cdd:cd16273    90 TPVEIDGdVSVTLLDANHCPGAVMFLFELPDGRRILHTGDFRANPEMleHPLLLGKRRIDTVYLDTTYCNP 160
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 385-491 2.36e-50

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: 167.45  E-value: 2.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 385 PEVSSLITTDMCDSLVHLLPMMQINFKGLQSHLKKCGGKYDQILAFRPTGWTHSNNITS-TADIIPQTRGNISIYGIPYS 463
Cdd:pfam07522   1 PEILSLLTTDPLSTQIHVVPMPKLSYEALLDYLTARKDHFDSVLAIRPTGWTYRPPKTEvSDRIGPSIRGRITIYGVPYS 80

                          90       100
                  ....*....|....*....|....*...
gi 1338686468 464 EHSSYLEMKRFVQWLKPQKIIPTVNVGS 491
Cdd:pfam07522  81 EHSSFDELKEFVQFLRPKKIIPTVNVGG 108
artemis-SNM1C-like_MBL-fold cd16297
artemis-SNM1C and related proteins; MBL-fold metallo-hydrolase domain; Includes the nuclease ...
 184-315 5.03e-20

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: 87.18  E-value: 5.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 184 TVDAFQYGEIEGcTAYFLTHFHSDHYAGLSKDFTRP---------VYCSEITGNLL--KKKLRVQEQYIRQLPMDTEC-- 250
Cdd:cd16297    15 SIDRFDRENLRA-RAYFLSHCHKDHMKGLRAPGLKRrlkaslkvkLYCSPVTKELLltNPKYAFWENHIVSLEIDTPTqi 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1338686468 251 -VVD-------SVKVVLLDANHCPGATMILFQLPNGAViLHTGDFR----ADPSMERSRLAGR--KVHTLFLDTTYCSP 315
Cdd:cd16297    94 sLVDeatgekeDVVVTLLPAGHCPGSVMFLFQGNNGTV-LYTGDFRlavgEAARMELLHSGDRvkDIQSVYLDTTFCDP 171
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 157-354 7.80e-13

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 70.22  E-value: 7.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 157 MNISESSGAGEVRRTCpFYKRIPGTGFTVDA--FQYGEIEGCTAY----------FLTHFHSDHyAGL-----SKDFTRP 219
Cdd:COG1236     1 MKLTFLGAAGEVTGSC-YLLETGGTRILIDCglFQGGKERNWPPFpfrpsdvdavVLTHAHLDH-SGAlpllvKEGFRGP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 220 VYCS----EITGNLLKKKLRVQE------------------QYIRQLPMDTECVVDSVKVVLLDANHCPGATMILFQLpN 277
Cdd:COG1236    79 IYATpataDLARILLGDSAKIQEeeaeaeplyteedaeralELFQTVDYGEPFEIGGVRVTFHPAGHILGSAQVELEV-G 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1338686468 278 GAVILHTGDF--RADPSMERSRLAgRKVHTLFLDTTYCSPEYtfPSQQEVIQfAINTAFEAVTLNPRALVVcGTYCIGK 354
Cdd:COG1236   158 GKRIVFSGDYgrEDDPLLAPPEPV-PPADVLITESTYGDRLH--PPREEVEA-ELAEWVRETLARGGTVLI-PAFALGR 231
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 200-360 6.10e-12

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: 65.51  E-value: 6.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 200 FLTHFHSDHYAGLS---KDFTRPVYCSEITGNLLKKKLR----VQEQYIRQLPMDTECVVDSVKVVLLDANHC-PGATMI 271
Cdd:cd07714    60 FITHGHEDHIGALPyllPELNVPIYATPLTLALIKKKLEefklIKKVKLNEIKPGERIKLGDFEVEFFRVTHSiPDSVGL 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 272 LFQLPNGaVILHTGDFRADPS--------MER-SRLAGRKVHTLFLDTTYCSPeytFPSQQEVIQFaINtafeavTLNPR 342
Cdd:cd07714   140 AIKTPEG-TIVHTGDFKFDQTpvdgkptdLEKlAELGKEGVLLLLSDSVHVSG---HASQEDLKLM-IN------LLKPK 208

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1338686468 343 ALV-VCGTY-------------CIGKEKVFLA 360
Cdd:cd07714   209 YFIpVHGEYrhlvahaklaeelGIPEENIFLL 240
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
198-335 6.99e-12

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 67.78  E-value: 6.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 198 AYFLTHFHSDHYAGLS---KDFTRPVYCSEITGNLLKKKLR----VQEQYIRQLPMDTECVVDSVKVVLLDANH-CPGAT 269
Cdd:COG0595    66 GIVLTHGHEDHIGALPyllKELNVPVYGTPLTLALLEAKLKehglLKKVKLHVVKPGDRIKFGPFKVEFFRVTHsIPDSL 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1338686468 270 MILFQLPNGaVILHTGDFRADPS--------MER-SRLAGRKVHTLFLDTTYC-SPEYTfPSQQEVIQfAINTAFE 335
Cdd:COG0595   146 GLAIRTPAG-TIVHTGDFKFDQTpvdgeptdLARlAELGEEGVLALLSDSTNAeRPGFT-PSEREVGP-TLEEIFA 218
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 178-289 8.49e-10

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: 58.39  E-value: 8.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 178 IPGTGFTVDAFQYGEIEG---CTAYFLTHFHSDHYAGLSK-DFTRPVYCSEITGNLLKKKLRV---QEQYIRQL----PM 246
Cdd:cd07732    55 IVGLYRDPLLLGGLRSEEdpsVDAVLLSHAHLDHYGLLNYlRPDIPVYMGEATKRILKALLPFfgeGDPVPRNIrvfeSG 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1338686468 247 DTECVVD-SVKVVLLDanH-CPGATMILFQLPnGAVILHTGDFRA 289
Cdd:cd07732   135 KSFTIGDfTVTPYLVD--HsAPGAYAFLIEAP-GKRIFYTGDFRF 176
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 200-329 1.45e-09

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 58.75  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 200 FLTHFHSDHYAGLsKDFTR-------PVYCSEITGNLLKKKLRVQEQY------IRQLPMDTECVVDSVKVVLLDANH-C 265
Cdd:COG1235    73 LLTHEHADHIAGL-DDLRPrygpnpiPVYATPGTLEALERRFPYLFAPypgkleFHEIEPGEPFEIGGLTVTPFPVPHdA 151

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1338686468 266 PGATMILFQLPNGAVILhTGDFRADPSMERSRLAGrkVHTLFLDTTYCSPEYTFPSQQEVIQFA 329
Cdd:COG1235   152 GDPVGYRIEDGGKKLAY-ATDTGYIPEEVLELLRG--ADLLILDATYDDPEPGHLSNEEALELL 212
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 200-300 9.82e-07

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: 49.09  E-value: 9.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468  200 FLTHFHSDHYAG---LSKDFTRPVYCSEITGNLLKKKLRVQEQ--YIRQLPMDTECVVDSVKVVL----LDANHCPGATM 270
Cdd:smart00849  40 ILTHGHPDHIGGlpeLLEAPGAPVYAPEGTAELLKDLLALLGElgAEAEPAPPDRTLKDGDELDLgggeLEVIHTPGHTP 119

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1338686468  271 --ILFQLPNGaVILHTGDFRADPSMERSRLAG 300
Cdd:smart00849 120 gsIVLYLPEG-KILFTGDLLFAGGDGRTLVDG 150
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 179-311 7.59e-06

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: 46.51  E-value: 7.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 179 PGTGFTVDAFQYGEIEG--CTAYFLTHFHSDHYAGLS--KDFTR-PVYCSEITGNLLKK----------KLRVQEQYIRQ 243
Cdd:cd06262    27 PGAGALEKILEAIEELGlkIKAILLTHGHFDHIGGLAelKEAPGaPVYIHEADAELLEDpelnlaffggGPLPPPEPDIL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 244 LPMDTECVVDSVKVVLLDA-NHCPGATMILFQLPNgavILHTGDFRADPSMERSRLAG-----------RKVHTLFLDTT 311
Cdd:cd06262   107 LEDGDTIELGGLELEVIHTpGHTPGSVCFYIEEEG---VLFTGDTLFAGSIGRTDLPGgdpeqliesikKLLLLLPDDTV 183
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
197-312 1.98e-04

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 42.87  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 197 TAYFLTHFHSDHYAGL--------SKDFTRP--VYCSEITGNLLKKKLRVQEQY------IRQLPMDTECVVDSVKVVLL 260
Cdd:COG1234    54 DAIFITHLHGDHIAGLpgllstrsLAGREKPltIYGPPGTKEFLEALLKASGTDldfpleFHEIEPGEVFEIGGFTVTAF 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1338686468 261 DANHCPGATMILFQLPnGAVILHTGDFRADPSMERsrlAGRKVHTLFLDTTY 312
Cdd:COG1234   134 PLDHPVPAYGYRFEEP-GRSLVYSGDTRPCEALVE---LAKGADLLIHEATF 181
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 200-286 5.14e-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: 41.60  E-value: 5.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 200 FLTHFHSDHYAG---LSKDFTRPVYCSEITGNLLKKKLRvQEQYIRQLPMDTECVVDSVKVVLLDAN----HCPGAT--M 270
Cdd:COG0491    56 LLTHLHPDHVGGlaaLAEAFGAPVYAHAAEAEALEAPAA-GALFGREPVPPDRTLEDGDTLELGGPGleviHTPGHTpgH 134

                          90
                  ....*....|....*.
gi 1338686468 271 ILFQLPnGAVILHTGD 286
Cdd:COG0491   135 VSFYVP-DEKVLFTGD 149
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 179-286 1.02e-03

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 40.67  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 179 PGTGFTVDAFQYGEIEGCTAYFLTHFHSDHY-----AGLSKDFTrPVYCSEITGNLLKKK--LRVQEqyirqLPMDTECV 251
Cdd:COG2220    32 RASPVNPLPLDPEDLPKIDAVLVTHDHYDHLddatlRALKRTGA-TVVAPLGVAAWLRAWgfPRVTE-----LDWGESVE 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1338686468 252 VDSVKVVLLDANHCPGATMILFQLPNGAVI-------LHTGD 286
Cdd:COG2220   106 LGGLTVTAVPARHSSGRPDRNGGLWVGFVIetdgktiYHAGD 147
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 200-317 2.92e-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: 38.83  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 200 FLTHFHSDHYAG---LSKDFTRPVYCSEITGNLLKK---KLRVQEQYIRQL-PMD----TECVVDSVKVVLLDANH-CPG 267
Cdd:pfam12706  33 LLTHDHYDHLAGlldLREGRPRPLYAPLGVLAHLRRnfpYLFLLEHYGVRVhEIDwgesFTVGDGGLTVTATPARHgSPR 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1338686468 268 ATMILFQLPNGAVI-------LHTGDFRADPSMERSRLAGRKVhtLFLDTTYCSPEY 317
Cdd:pfam12706 113 GLDPNPGDTLGFRIegpgkrvYYAGDTGYFPDEIGERLGGADL--LLLDGGAWRDDE 167
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 200-270 3.60e-03

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: 38.61  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 200 FLTHFHSDHYAGLS--KDFTR------PVYCSEITGNLLKKKLRVQEQY----------IRQLPMDTECVVDSVKVVLLD 261
Cdd:cd16279    71 LLTHAHADHIHGLDdlRPFNRlqqrpiPVYASEETLDDLKRRFPYFFAAtggggvpkldLHIIEPDEPFTIGGLEITPLP 150


                  ....*....
gi 1338686468 262 ANHCPGATM 270
Cdd:cd16279   151 VLHGKLPSL 159
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 198-314 4.41e-03

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. 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: 293821  Cd Length: 259  Bit Score: 39.12  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 198 AYFLTHFHSDHYAGL---------SKDFTRPVYCSEITGNLLKKKL-------------RVQEQYIRQLPMDTECVV--D 253
Cdd:cd07735    68 HYLITHAHLDHIAGLpllspndggQRGSPKTIYGLPETIDALKKHIfnwviwpdftsipSGKYPYLRLEPIEPEYPIalT 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1338686468 254 SVKVVLLDANH-CPGATMILFQlPNGAVILHTGDFRADPSMERSR----------LAGRKVHTLFLDTTYCS 314
Cdd:cd07735   148 GLSVTAFPVSHgVPVSTAFLIR-DGGDSFLFFGDTGPDSVSKSPRldalwralapLIPKKLKAIIIECSFPN 218
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 200-212 5.11e-03

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 38.27  E-value: 5.11e-03
                          10
                  ....*....|...
gi 1338686468 200 FLTHFHSDHYAGL 212
Cdd:cd07719    56 FLTHLHSDHVADL 68
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
200-307 5.44e-03

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 38.12  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686468 200 FLTHFHSDHYAGL----SKDFTRPVYCSEITGNLLKKKLRVQEQYIRQLPM------------DTECVVDSVKVVLLDAN 263
Cdd:pfam00753  48 ILTHGHFDHIGGLgelaEATDVPVIVVAEEARELLDEELGLAASRLGLPGPpvvplppdvvleEGDGILGGGLGLLVTHG 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1338686468 264 HCPGATMILFQLPNGaVILHTGDFRADPSMERSRLAGRKVHTLF 307
Cdd:pfam00753 128 PGHGPGHVVVYYGGG-KVLFTGDLLFAGEIGRLDLPLGGLLVLH 170
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH