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Conserved domains on  [gi|58380350|ref|XP_310480|]
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AGAP000597-PA [Anopheles gambiae str. PEST]

Protein Classification

DNA cross-link repair protein( domain architecture ID 581276)

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

Graphical summary

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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; ...
 1-154 6.25e-26

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 cd16297:

Pssm-ID: 451500  Cd Length: 171  Bit Score: 102.97  E-value: 6.25e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350   1 MSTFPGTVPELPGIGIDRFD-QPVRDRAtlFFLSHCHVDHMQGLPD-------AAPLPGPLYVSPHTAVIVgLRHPQHT- 71
Cdd:cd16297   1 MSSFGGRMKEYPYISIDRFDrENLRARA--YFLSHCHKDHMKGLRApglkrrlKASLKVKLYCSPVTKELL-LTNPKYAf 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350  72 ----LVPVPVREQLNLTVRPPA-GPAYELCVRTVPAEHCPGSVMFYFETKTVRLLYTGDFRLSSASltaIARY------- 139
Cdd:cd16297  78 wenhIVSLEIDTPTQISLVDEAtGEKEDVVVTLLPAGHCPGSVMFLFQGNNGTVLYTGDFRLAVGE---AARMellhsgd 154

                       170
                ....*....|....*.
gi 58380350 140 RVRP-TIVYLDSTFLD 154
Cdd:cd16297 155 RVKDiQSVYLDTTFCD 170
DRMBL super family cl06523
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 227-318 2.33e-11

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.


The actual alignment was detected with superfamily member pfam07522:

Pssm-ID: 429512  Cd Length: 108  Bit Score: 60.37  E-value: 2.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350   227 LDHVFTDDAAGARIHACRGKTLEHERACRAAKPEEKHPDFVLTIRPTArrW-CNLRPGEPFWQQGSG-----NLWYVCYS 300
Cdd:pfam07522   3 ILSLLTTDPLSTQIHVVPMPKLSYEALLDYLTARKDHFDSVLAIRPTG--WtYRPPKTEVSDRIGPSirgriTIYGVPYS 80

                          90
                  ....*....|....*...
gi 58380350   301 SHASSTELVEFLRSLQPD 318
Cdd:pfam07522  81 EHSSFDELKEFVQFLRPK 98
 
Name Accession Description Interval E-value
artemis-SNM1C-like_MBL-fold cd16297
artemis-SNM1C and related proteins; MBL-fold metallo-hydrolase domain; Includes the nuclease ...
 1-154 6.25e-26

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: 102.97  E-value: 6.25e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350   1 MSTFPGTVPELPGIGIDRFD-QPVRDRAtlFFLSHCHVDHMQGLPD-------AAPLPGPLYVSPHTAVIVgLRHPQHT- 71
Cdd:cd16297   1 MSSFGGRMKEYPYISIDRFDrENLRARA--YFLSHCHKDHMKGLRApglkrrlKASLKVKLYCSPVTKELL-LTNPKYAf 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350  72 ----LVPVPVREQLNLTVRPPA-GPAYELCVRTVPAEHCPGSVMFYFETKTVRLLYTGDFRLSSASltaIARY------- 139
Cdd:cd16297  78 wenhIVSLEIDTPTQISLVDEAtGEKEDVVVTLLPAGHCPGSVMFLFQGNNGTVLYTGDFRLAVGE---AARMellhsgd 154

                       170
                ....*....|....*.
gi 58380350 140 RVRP-TIVYLDSTFLD 154
Cdd:cd16297 155 RVKDiQSVYLDTTFCD 170
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 227-318 2.33e-11

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: 60.37  E-value: 2.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350   227 LDHVFTDDAAGARIHACRGKTLEHERACRAAKPEEKHPDFVLTIRPTArrW-CNLRPGEPFWQQGSG-----NLWYVCYS 300
Cdd:pfam07522   3 ILSLLTTDPLSTQIHVVPMPKLSYEALLDYLTARKDHFDSVLAIRPTG--WtYRPPKTEVSDRIGPSirgriTIYGVPYS 80

                          90
                  ....*....|....*...
gi 58380350   301 SHASSTELVEFLRSLQPD 318
Cdd:pfam07522  81 EHSSFDELKEFVQFLRPK 98
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 31-172 4.92e-08

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 54.42  E-value: 4.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350  31 FLSHCHVDHmqglpdAAPLP--------GPLYVSPHTAVIVGLR-----HPQHTLVPVP-------VREQLNLTVRPPAG 90
Cdd:COG1236  55 VLTHAHLDH------SGALPllvkegfrGPIYATPATADLARILlgdsaKIQEEEAEAEplyteedAERALELFQTVDYG 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350  91 PAYELC---VRTVPAEHCPGSVMFYFETKTVRLLYTGDFRLSSASLTAIARYRVRPTIVYLDSTFLDRRYayfPPRQASM 167
Cdd:COG1236 129 EPFEIGgvrVTFHPAGHILGSAQVELEVGGKRIVFSGDYGREDDPLLAPPEPVPPADVLITESTYGDRLH---PPREEVE 205


                ....*
gi 58380350 168 DRIVE 172
Cdd:COG1236 206 AELAE 210
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 31-150 3.71e-06

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: 46.78  E-value: 3.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350     31 FLSHCHVDHMQGLPDAAPLPG-PLYVSPHTA-VIVGLRHPQHTLVPVPVREQLNLTVRPpaGPAYELCVRTVPAEHCPG- 107
Cdd:smart00849  40 ILTHGHPDHIGGLPELLEAPGaPVYAPEGTAeLLKDLLALLGELGAEAEPAPPDRTLKD--GDELDLGGGELEVIHTPGh 117

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 58380350    108 ---SVMFYFETKtvRLLYTGDFRLSSASLTAIARYRVRPTIVYLDS 150
Cdd:smart00849 118 tpgSIVLYLPEG--KILFTGDLLFAGGDGRTLVDGGDAAASDALES 161
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 18-125 2.97e-04

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: 41.53  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350    18 RFDQPVRDRAT---LFFLSHCHVDHMQGLPDAAPL-PGPLYVSPHTAVIVGLRHPqhtLVPVPVREQLNLTVRPPAGPA- 92
Cdd:pfam12706  17 PALQPGRLRDDpidAVLLTHDHYDHLAGLLDLREGrPRPLYAPLGVLAHLRRNFP---YLFLLEHYGVRVHEIDWGESFt 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 58380350    93 ---YELCVRTVPAEH--------CPGSVMFY-FETKTVRLLYTGD 125
Cdd:pfam12706  94 vgdGGLTVTATPARHgsprgldpNPGDTLGFrIEGPGKRVYYAGD 138
 
Name Accession Description Interval E-value
artemis-SNM1C-like_MBL-fold cd16297
artemis-SNM1C and related proteins; MBL-fold metallo-hydrolase domain; Includes the nuclease ...
 1-154 6.25e-26

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: 102.97  E-value: 6.25e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350   1 MSTFPGTVPELPGIGIDRFD-QPVRDRAtlFFLSHCHVDHMQGLPD-------AAPLPGPLYVSPHTAVIVgLRHPQHT- 71
Cdd:cd16297   1 MSSFGGRMKEYPYISIDRFDrENLRARA--YFLSHCHKDHMKGLRApglkrrlKASLKVKLYCSPVTKELL-LTNPKYAf 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350  72 ----LVPVPVREQLNLTVRPPA-GPAYELCVRTVPAEHCPGSVMFYFETKTVRLLYTGDFRLSSASltaIARY------- 139
Cdd:cd16297  78 wenhIVSLEIDTPTQISLVDEAtGEKEDVVVTLLPAGHCPGSVMFLFQGNNGTVLYTGDFRLAVGE---AARMellhsgd 154

                       170
                ....*....|....*.
gi 58380350 140 RVRP-TIVYLDSTFLD 154
Cdd:cd16297 155 RVKDiQSVYLDTTFCD 170
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 11-154 7.16e-24

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: 96.84  E-value: 7.16e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350  11 LPGIGI--DRFDQPVRDRATLFFLSHCHVDHMQGLpDAAPLPGPLYVSPHTA--VIVGLRHPQHTLVPVP--VREQLNLT 84
Cdd:cd16273  19 IPGTSFvvDAFKYGKIPGISAYFLSHFHSDHYGGL-TKSWSHGPIYCSEITAnlVKLKLKVDEEYIVVLPmnTPVEIDGD 97

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58380350  85 VRppagpayelcVRTVPAEHCPGSVMFYFETK-TVRLLYTGDFRLSSASLTAIARYRVRP-TIVYLDSTFLD 154
Cdd:cd16273  98 VS----------VTLLDANHCPGAVMFLFELPdGRRILHTGDFRANPEMLEHPLLLGKRRiDTVYLDTTYCN 159
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 227-318 2.33e-11

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: 60.37  E-value: 2.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350   227 LDHVFTDDAAGARIHACRGKTLEHERACRAAKPEEKHPDFVLTIRPTArrW-CNLRPGEPFWQQGSG-----NLWYVCYS 300
Cdd:pfam07522   3 ILSLLTTDPLSTQIHVVPMPKLSYEALLDYLTARKDHFDSVLAIRPTG--WtYRPPKTEVSDRIGPSirgriTIYGVPYS 80

                          90
                  ....*....|....*...
gi 58380350   301 SHASSTELVEFLRSLQPD 318
Cdd:pfam07522  81 EHSSFDELKEFVQFLRPK 98
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 31-172 4.92e-08

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 54.42  E-value: 4.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350  31 FLSHCHVDHmqglpdAAPLP--------GPLYVSPHTAVIVGLR-----HPQHTLVPVP-------VREQLNLTVRPPAG 90
Cdd:COG1236  55 VLTHAHLDH------SGALPllvkegfrGPIYATPATADLARILlgdsaKIQEEEAEAEplyteedAERALELFQTVDYG 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350  91 PAYELC---VRTVPAEHCPGSVMFYFETKTVRLLYTGDFRLSSASLTAIARYRVRPTIVYLDSTFLDRRYayfPPRQASM 167
Cdd:COG1236 129 EPFEIGgvrVTFHPAGHILGSAQVELEVGGKRIVFSGDYGREDDPLLAPPEPVPPADVLITESTYGDRLH---PPREEVE 205


                ....*
gi 58380350 168 DRIVE 172
Cdd:COG1236 206 AELAE 210
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 5-152 6.00e-08

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: 51.75  E-value: 6.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350   5 PGTvpelpGIGIDRFDQPVRDRATLFFLSHCHVDHMQGLPDAAPLpgPLYVSPHTAVIVGLRhpqhtlvpVPVREQLnLT 84
Cdd:cd16298  20 PGT-----GFTVDAFQYGVIEGCTAYFLTHFHSDHYCGLTKKFKF--PIYCSKITGNLVKSK--------LKVEEQY-IN 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58380350  85 VRPPAGPAYELCVRTV--PAEHCPGSVM--FYFETKTVrLLYTGDFRLSSASLTAIARYRVRPTIVYLDSTF 152
Cdd:cd16298  84 VLPMNTECIVNGVKVVllDANHCPGAVMilFRLPSGTL-VLHTGDFRADPSMERYPELIGQKIHTLYLDTTY 154
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 31-128 7.85e-08

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: 52.23  E-value: 7.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350  31 FLSHCHVDHMQGLPDAAP-LPgpLYVSPHTAVIVGLR------HPQHTLVPVPVREQLNLTVrppaGPayeLCVRTVPAE 103
Cdd:cd07732  80 LLSHAHLDHYGLLNYLRPdIP--VYMGEATKRILKALlpffgeGDPVPRNIRVFESGKSFTI----GD---FTVTPYLVD 150

                        90       100
                ....*....|....*....|....*.
gi 58380350 104 H-CPGSVMFYFETKTVRLLYTGDFRL 128
Cdd:cd07732 151 HsAPGAYAFLIEAPGKRIFYTGDFRF 176
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 31-150 3.71e-06

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: 46.78  E-value: 3.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350     31 FLSHCHVDHMQGLPDAAPLPG-PLYVSPHTA-VIVGLRHPQHTLVPVPVREQLNLTVRPpaGPAYELCVRTVPAEHCPG- 107
Cdd:smart00849  40 ILTHGHPDHIGGLPELLEAPGaPVYAPEGTAeLLKDLLALLGELGAEAEPAPPDRTLKD--GDELDLGGGELEVIHTPGh 117

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 58380350    108 ---SVMFYFETKtvRLLYTGDFRLSSASLTAIARYRVRPTIVYLDS 150
Cdd:smart00849 118 tpgSIVLYLPEG--KILFTGDLLFAGGDGRTLVDGGDAAASDALES 161
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 5-125 4.77e-06

Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. 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: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 46.49  E-value: 4.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350   5 PGTVPELPGIGIDRFDQpvrdraTLFFLSHCHVDHMQGLP------DAAPLPGPLYVSPHTAVIVGL-RHPQHTLVPVPV 77
Cdd:cd16272  35 EGTVYRLLKAGVDPDKL------DAIFLSHFHLDHIGGLPtllfarRYGGRKKPLTIYGPKGIKEFLeKLLNFPVEILPL 108

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 58380350  78 REQLNLTVRPPAGPAYELC---VRTVPAEHCPGSVMFYFETKTVRLLYTGD 125
Cdd:cd16272 109 GFPLEIEELEEGGEVLELGdlkVEAFPVKHSVESLGYRIEAEGKSIVYSGD 159
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
31-158 6.56e-06

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 47.11  E-value: 6.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350  31 FLSHCHVDHMQGLPDAAPL--------PGPLYVSPHTAVIVglrhpQHTLVPVPVREQLNLTVRP-PAGPAYE---LCVR 98
Cdd:COG1234  57 FITHLHGDHIAGLPGLLSTrslagrekPLTIYGPPGTKEFL-----EALLKASGTDLDFPLEFHEiEPGEVFEiggFTVT 131

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350  99 TVPAEHCPGSVMFYFETKTVRLLYTGDFRLSSAsLTAIARyrvRPTIVYLDSTFLDRRYA 158
Cdd:COG1234 132 AFPLDHPVPAYGYRFEEPGRSLVYSGDTRPCEA-LVELAK---GADLLIHEATFLDEEAE 187
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 21-174 7.57e-06

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. 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: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 46.72  E-value: 7.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350  21 QPVRDRATLFFlSHCHVDHMQGLpdaaPLPGPLYVsPHTAVIVGLRHPqhtlVPVPVREQLNLTVRPPAGPayelcvrtV 100
Cdd:cd07715  53 EGPPGEAHLLL-SHTHWDHIQGF----PFFAPAYD-PGNRIHIYGPHK----DGGSLEEVLRRQMSPPYFP--------V 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350 101 PAEHCPGSVMFYF--ETKTVRLlytGDFRLSSASLT----AIArYRVR---PTIVYL-DstfldrrYAYFPPRQASMDRI 170
Cdd:cd07715 115 PLEELLAAIEFHDlePGEPFSI---GGVTVTTIPLNhpggALG-YRIEedgKSVVYAtD-------TEHYPDDGESDEAL 183


                ....
gi 58380350 171 VELC 174
Cdd:cd07715 184 LEFA 187
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 30-125 2.95e-05

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: 45.28  E-value: 2.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350  30 FFLSHCHVDHMQGLPDAAPL-------PGPLYVSPHT-----------------AVIVGLRHPQHTLVPVPVREQLNLTv 85
Cdd:cd07735  69 YLITHAHLDHIAGLPLLSPNdggqrgsPKTIYGLPETidalkkhifnwviwpdfTSIPSGKYPYLRLEPIEPEYPIALT- 147

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 58380350  86 rppagpayELCVRTVPAEH-CPGSVMFYFETKTVRLLYTGD 125
Cdd:cd07735 148 --------GLSVTAFPVSHgVPVSTAFLIRDGGDSFLFFGD 180
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 31-128 3.41e-05

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: 45.09  E-value: 3.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350  31 FLSHCHVDHMQGLPDAAP-LPGPLYVSPHTAVIV-------GLRHPQHtLVPVPVREQLNLtvrppaGPayeLCVRTVPA 102
Cdd:cd07714  60 FITHGHEDHIGALPYLLPeLNVPIYATPLTLALIkkkleefKLIKKVK-LNEIKPGERIKL------GD---FEVEFFRV 129

                        90       100
                ....*....|....*....|....*..
gi 58380350 103 EHC-PGSVMFYFETKTVRLLYTGDFRL 128
Cdd:cd07714 130 THSiPDSVGLAIKTPEGTIVHTGDFKF 156
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 31-180 4.34e-05

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 44.89  E-value: 4.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350  31 FLSHCHVDHMQGLPDAAPL----PGPLYVSPHTAVIVGLRHPQhtlVPVPVREQLNLTVRPPAGP--AYELCVRTVPAEH 104
Cdd:COG1235  73 LLTHEHADHIAGLDDLRPRygpnPIPVYATPGTLEALERRFPY---LFAPYPGKLEFHEIEPGEPfeIGGLTVTPFPVPH 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350 105 CPGSVMFY-FETKTVRLLYTGDF-RLSSASLTAIARYRVrptiVYLDSTFlDRRYAYFPPRQASMDRIVELCSR--WLAH 180
Cdd:COG1235 150 DAGDPVGYrIEDGGKKLAYATDTgYIPEEVLELLRGADL----LILDATY-DDPEPGHLSNEEALELLARLGPKrlVLTH 224
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 18-125 2.97e-04

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: 41.53  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350    18 RFDQPVRDRAT---LFFLSHCHVDHMQGLPDAAPL-PGPLYVSPHTAVIVGLRHPqhtLVPVPVREQLNLTVRPPAGPA- 92
Cdd:pfam12706  17 PALQPGRLRDDpidAVLLTHDHYDHLAGLLDLREGrPRPLYAPLGVLAHLRRNFP---YLFLLEHYGVRVHEIDWGESFt 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 58380350    93 ---YELCVRTVPAEH--------CPGSVMFY-FETKTVRLLYTGD 125
Cdd:pfam12706  94 vgdGGLTVTATPARHgsprgldpNPGDTLGFrIEGPGKRVYYAGD 138
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 32-125 4.80e-04

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. 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. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 41.18  E-value: 4.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350  32 LSHCHVDHMQGLPDAAPLPG----------PLYVS-PHTAVIVGLRHPQHTLVPVPVREQLNLTVrppagPAYELCVRTV 100
Cdd:cd16322  52 LTHAHFDHVGGVADLRRHPGapvylhpddlPLYEAaDLGAKAFGLGIEPLPPPDRLLEDGQTLTL-----GGLEFKVLHT 126

                        90       100
                ....*....|....*....|....*
gi 58380350 101 PAeHCPGSVMFYFETKTvrLLYTGD 125
Cdd:cd16322 127 PG-HSPGHVCFYVEEEG--LLFSGD 148
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
3-128 6.72e-04

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 41.59  E-value: 6.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350   3 TFPGtvPELPGIGI---------DRfdqpvRDRATLFFLSHCHVDHMQGLPDAAPLPG-PLYVSPHTAVIVGLR------ 66
Cdd:COG0595  38 KFPE--DEMPGVDLvipdisyleEN-----KDKIKGIVLTHGHEDHIGALPYLLKELNvPVYGTPLTLALLEAKlkehgl 110

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58380350  67 HPQHTLVPVPVREQLNLtvrppaGPayeLCVRTVPAEH-CPGSVMFYFETKTVRLLYTGDFRL 128
Cdd:COG0595 111 LKKVKLHVVKPGDRIKF------GP---FKVEFFRVTHsIPDSLGLAIRTPAGTIVHTGDFKF 164
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 31-125 1.03e-03

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: 40.06  E-value: 1.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58380350  31 FLSHCHVDHMQGLPDAAPLPG-PLYVSPHTAVIVGLRHPQHTL--VPVPVREQLNLTVRPPAGpAYELCVRTVPAeHCPG 107
Cdd:COG0491  56 LLTHLHPDHVGGLAALAEAFGaPVYAHAAEAEALEAPAAGALFgrEPVPPDRTLEDGDTLELG-GPGLEVIHTPG-HTPG 133

                        90
                ....*....|....*...
gi 58380350 108 SVMFYFETKtvRLLYTGD 125
Cdd:COG0491 134 HVSFYVPDE--KVLFTGD 149
 
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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