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Conserved domains on  [gi|1907137773|ref|XP_011237273|]
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protein artemis isoform X8 [Mus musculus]

Protein Classification

protein artemis( domain architecture ID 10888846)

artemis is a single-strand-specific 5' to 3' exonuclease which after complex formation with, and phosphorylation by, DNA-dependent protein kinase, gains endonucleolytic activity on hairpins and 5' and 3' overhangs

Gene Ontology:  GO:0006974
PubMed:  12177301|32576658|34387696

Graphical summary

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List of domain hits

 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 ...
 1-171 2.91e-125

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: 359.51  E-value: 2.91e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773   1 MSSFQGQMAEYPTISIDRFDRENLKARAYFLSHCHKDHMKGLRAPSLKRRLECSLKVFLYCSPVTKELLLTSPKYRFWEN 80
Cdd:cd16297     1 MSSFGGRMKEYPYISIDRFDRENLRARAYFLSHCHKDHMKGLRAPGLKRRLKASLKVKLYCSPVTKELLLTNPKYAFWEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  81 RIITIEIETPTQISLVDEASGEKEEVVVTLLPAGHCPGSVMFLFQGSNGTVLYTGDFRLAKGEASRMELLHSGGRVKDIQ 160
Cdd:cd16297    81 HIVSLEIDTPTQISLVDEATGEKEDVVVTLLPAGHCPGSVMFLFQGNNGTVLYTGDFRLAVGEAARMELLHSGDRVKDIQ 160

                         170
                  ....*....|.
gi 1907137773 161 SVYLDTTFCDP 171
Cdd:cd16297   161 SVYLDTTFCDP 171
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 239-345 4.80e-29

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: 109.29  E-value: 4.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773 239 PDILHHLTTD-RNTQIHACRHPKAEecfqWNKLPCGITSQNKTALHTISIKPSTmwFGERTRKTNVIVRTGES------S 311
Cdd:pfam07522   1 PEILSLLTTDpLSTQIHVVPMPKLS----YEALLDYLTARKDHFDSVLAIRPTG--WTYRPPKTEVSDRIGPSirgritI 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907137773 312 YRACFSFHSSFSEIKDFLSYICPVNVYPNVIPVG 345
Cdd:pfam07522  75 YGVPYSEHSSFDELKEFVQFLRPKKIIPTVNVGG 108
 
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 ...
 1-171 2.91e-125

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: 359.51  E-value: 2.91e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773   1 MSSFQGQMAEYPTISIDRFDRENLKARAYFLSHCHKDHMKGLRAPSLKRRLECSLKVFLYCSPVTKELLLTSPKYRFWEN 80
Cdd:cd16297     1 MSSFGGRMKEYPYISIDRFDRENLRARAYFLSHCHKDHMKGLRAPGLKRRLKASLKVKLYCSPVTKELLLTNPKYAFWEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  81 RIITIEIETPTQISLVDEASGEKEEVVVTLLPAGHCPGSVMFLFQGSNGTVLYTGDFRLAKGEASRMELLHSGGRVKDIQ 160
Cdd:cd16297    81 HIVSLEIDTPTQISLVDEATGEKEDVVVTLLPAGHCPGSVMFLFQGNNGTVLYTGDFRLAVGEAARMELLHSGDRVKDIQ 160

                         170
                  ....*....|.
gi 1907137773 161 SVYLDTTFCDP 171
Cdd:cd16297   161 SVYLDTTFCDP 171
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 239-345 4.80e-29

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: 109.29  E-value: 4.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773 239 PDILHHLTTD-RNTQIHACRHPKAEecfqWNKLPCGITSQNKTALHTISIKPSTmwFGERTRKTNVIVRTGES------S 311
Cdd:pfam07522   1 PEILSLLTTDpLSTQIHVVPMPKLS----YEALLDYLTARKDHFDSVLAIRPTG--WTYRPPKTEVSDRIGPSirgritI 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907137773 312 YRACFSFHSSFSEIKDFLSYICPVNVYPNVIPVG 345
Cdd:pfam07522  75 YGVPYSEHSSFDELKEFVQFLRPKKIIPTVNVGG 108
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 30-144 1.35e-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: 54.10  E-value: 1.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773   30 FLSHCHKDHMKGLraPSLKRRLECslKVflYCSPVTKELLLTSPKYRFWENRIITIEIETPTqISLVDEASGEKEEVVVT 109
Cdd:smart00849  40 ILTHGHPDHIGGL--PELLEAPGA--PV--YAPEGTAELLKDLLALLGELGAEAEPAPPDRT-LKDGDELDLGGGELEVI 112

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907137773  110 LLPaGHCPGSVMFLFQGSNgtVLYTGDFRLAKGEA 144
Cdd:smart00849 113 HTP-GHTPGSIVLYLPEGK--ILFTGDLLFAGGDG 144
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 30-191 3.60e-07

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 52.11  E-value: 3.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  30 FLSHCHKDHMKGLraPSLKRRlECSLKVflYCSPVTKELL---------------LTSPKY-----RFWENRIITIEIET 89
Cdd:COG1236    55 VLTHAHLDHSGAL--PLLVKE-GFRGPI--YATPATADLArillgdsakiqeeeaEAEPLYteedaERALELFQTVDYGE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  90 PTQIslvdeasgekEEVVVTLLPAGHCPGSVMFLFQGSNGTVLYTGDFrlaKGEASRmeLLHSGGRVKDIQSVYLDTTFC 169
Cdd:COG1236   130 PFEI----------GGVRVTFHPAGHILGSAQVELEVGGKRIVFSGDY---GREDDP--LLAPPEPVPPADVLITESTYG 194

                         170       180
                  ....*....|....*....|..
gi 1907137773 170 DPRFyqiPSREQCLRGILELVR 191
Cdd:COG1236   195 DRLH---PPREEVEAELAEWVR 213
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 30-178 3.13e-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: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  30 FLSHCHKDHMKGLraPSLKRRLECSlkvfLYCSPVTKELLLTSPKYRFWEN----RIITIEIETPTQISLVDeasgekee 105
Cdd:pfam12706  33 LLTHDHYDHLAGL--LDLREGRPRP----LYAPLGVLAHLRRNFPYLFLLEhygvRVHEIDWGESFTVGDGG-------- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773 106 VVVTLLPAGH--------CPGSVM-FLFQGSNGTVLYTGDFRLAKGEAsrmellhsGGRVKDIQSVYLDTTFCDPRFYQI 176
Cdd:pfam12706  99 LTVTATPARHgsprgldpNPGDTLgFRIEGPGKRVYYAGDTGYFPDEI--------GERLGGADLLLLDGGAWRDDEMIH 170


                  ..
gi 1907137773 177 PS 178
Cdd:pfam12706 171 MG 172
 
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 ...
 1-171 2.91e-125

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: 359.51  E-value: 2.91e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773   1 MSSFQGQMAEYPTISIDRFDRENLKARAYFLSHCHKDHMKGLRAPSLKRRLECSLKVFLYCSPVTKELLLTSPKYRFWEN 80
Cdd:cd16297     1 MSSFGGRMKEYPYISIDRFDRENLRARAYFLSHCHKDHMKGLRAPGLKRRLKASLKVKLYCSPVTKELLLTNPKYAFWEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  81 RIITIEIETPTQISLVDEASGEKEEVVVTLLPAGHCPGSVMFLFQGSNGTVLYTGDFRLAKGEASRMELLHSGGRVKDIQ 160
Cdd:cd16297    81 HIVSLEIDTPTQISLVDEATGEKEDVVVTLLPAGHCPGSVMFLFQGNNGTVLYTGDFRLAVGEAARMELLHSGDRVKDIQ 160

                         170
                  ....*....|.
gi 1907137773 161 SVYLDTTFCDP 171
Cdd:cd16297   161 SVYLDTTFCDP 171
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 13-171 7.12e-44

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: 150.38  E-value: 7.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  13 TISIDRFDRENLK-ARAYFLSHCHKDHMKGLRapslkrrlecslKVF----LYCSPVTKELLLTspKYRFWENRIITIEI 87
Cdd:cd16273    23 SFVVDAFKYGKIPgISAYFLSHFHSDHYGGLT------------KSWshgpIYCSEITANLVKL--KLKVDEEYIVVLPM 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  88 ETPTQISlvdeasgekEEVVVTLLPAGHCPGSVMFLFQGSNG-TVLYTGDFRLAKGEASRMELLHSggrvKDIQSVYLDT 166
Cdd:cd16273    89 NTPVEID---------GDVSVTLLDANHCPGAVMFLFELPDGrRILHTGDFRANPEMLEHPLLLGK----RRIDTVYLDT 155


                  ....*
gi 1907137773 167 TFCDP 171
Cdd:cd16273   156 TYCNP 160
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 239-345 4.80e-29

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: 109.29  E-value: 4.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773 239 PDILHHLTTD-RNTQIHACRHPKAEecfqWNKLPCGITSQNKTALHTISIKPSTmwFGERTRKTNVIVRTGES------S 311
Cdd:pfam07522   1 PEILSLLTTDpLSTQIHVVPMPKLS----YEALLDYLTARKDHFDSVLAIRPTG--WTYRPPKTEVSDRIGPSirgritI 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907137773 312 YRACFSFHSSFSEIKDFLSYICPVNVYPNVIPVG 345
Cdd:pfam07522  75 YGVPYSEHSSFDELKEFVQFLRPKKIIPTVNVGG 108
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 28-171 2.44e-19

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: 84.49  E-value: 2.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  28 AYFLSHCHKDHMKGLRAPSlkrrlecslKVFLYCSPVTKELLltSPKYRFWENRIITIEIETPTQISLVDeasgekeevv 107
Cdd:cd16298    39 AYFLTHFHSDHYCGLTKKF---------KFPIYCSKITGNLV--KSKLKVEEQYINVLPMNTECIVNGVK---------- 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907137773 108 VTLLPAGHCPGSVMFLFQGSNGT-VLYTGDFRLAKGEASRMELLhsGGRvkdIQSVYLDTTFCDP 171
Cdd:cd16298    98 VVLLDANHCPGAVMILFRLPSGTlVLHTGDFRADPSMERYPELI--GQK---IHTLYLDTTYCSP 157
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 16-137 8.15e-11

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: 60.76  E-value: 8.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  16 IDRFDRENLKARAYFLSHCHKDHMKGLRApsLKRRLECslKVflYCSPVTKELLLTSPKYRFWENRIITIEIETPTQISL 95
Cdd:cd06262    36 LEAIEELGLKIKAILLTHGHFDHIGGLAE--LKEAPGA--PV--YIHEADAELLEDPELNLAFFGGGPLPPPEPDILLED 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907137773  96 VDEASGEKEEVVVTLLPaGHCPGSVMFLFQGSNgtVLYTGDF 137
Cdd:cd06262   110 GDTIELGGLELEVIHTP-GHTPGSVCFYIEEEG--VLFTGDT 148
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 28-146 1.63e-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: 60.32  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  28 AYFLSHCHKDHMKGLR--APSLKrrlecslkvfLYCSPVTKELLLTSpkyrfweNRIITIEIETPTQISLVDeaSGEKEE 105
Cdd:cd07732    78 AVLLSHAHLDHYGLLNylRPDIP----------VYMGEATKRILKAL-------LPFFGEGDPVPRNIRVFE--SGKSFT 138

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907137773 106 V---VVTLLPAGH-CPGSVMFLFQGSNGTVLYTGDFRL--AKGEASR 146
Cdd:cd07732   139 IgdfTVTPYLVDHsAPGAYAFLIEAPGKRIFYTGDFRFhgRKPELTE 185
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 27-136 4.51e-10

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: 59.92  E-value: 4.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  27 RAYFLSHCHKDHMKGL--RAPSLKRRLECSLKVflYCSPVTKELLLT---------------SPKYRFwenriITIEIET 89
Cdd:cd07735    67 RHYLITHAHLDHIAGLplLSPNDGGQRGSPKTI--YGLPETIDALKKhifnwviwpdftsipSGKYPY-----LRLEPIE 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907137773  90 PTQISLVDEASgekeevvVTLLPAGH-CPGSVMFLFQGSNGTVLYTGD 136
Cdd:cd07735   140 PEYPIALTGLS-------VTAFPVSHgVPVSTAFLIRDGGDSFLFFGD 180
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 30-137 5.78e-10

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. 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: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 58.62  E-value: 5.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  30 FLSHCHKDHMkGlRAPSLKRRlecSLKVFLYCSPVTKELL------------------LTSPKYRF-----WENRIITIE 86
Cdd:cd16295    56 ILTHAHLDHS-G-RLPLLVKE---GFRGPIYATPATKDLAelllldsakiqeeeaehpPAEPLYTEedvekALKHFRPVE 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907137773  87 IETPTQISlvdeasgekEEVVVTLLPAGHCPGSVMFLFQ-GSNGTVLYTGDF 137
Cdd:cd16295   131 YGEPFEIG---------PGVKVTFYDAGHILGSASVELEiGGGKRILFSGDL 173
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 25-139 6.62e-09

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: 56.26  E-value: 6.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  25 KARAYFLSHCHKDHMKGLraPSLKRRLECslKVflYCSPVTKELLltspKYRFWE------NRIITIEIETPTQISlvde 98
Cdd:cd07714    55 KIKGIFITHGHEDHIGAL--PYLLPELNV--PI--YATPLTLALI----KKKLEEfklikkVKLNEIKPGERIKLG---- 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907137773  99 asgekeEVVVTLLPAGHC-PGSVMFLFQGSNGTVLYTGDFRL 139
Cdd:cd07714   121 ------DFEVEFFRVTHSiPDSVGLAIKTPEGTIVHTGDFKF 156
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 30-144 1.35e-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: 54.10  E-value: 1.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773   30 FLSHCHKDHMKGLraPSLKRRLECslKVflYCSPVTKELLLTSPKYRFWENRIITIEIETPTqISLVDEASGEKEEVVVT 109
Cdd:smart00849  40 ILTHGHPDHIGGL--PELLEAPGA--PV--YAPEGTAELLKDLLALLGELGAEAEPAPPDRT-LKDGDELDLGGGELEVI 112

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907137773  110 LLPaGHCPGSVMFLFQGSNgtVLYTGDFRLAKGEA 144
Cdd:smart00849 113 HTP-GHTPGSIVLYLPEGK--ILFTGDLLFAGGDG 144
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 30-191 3.60e-07

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 52.11  E-value: 3.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  30 FLSHCHKDHMKGLraPSLKRRlECSLKVflYCSPVTKELL---------------LTSPKY-----RFWENRIITIEIET 89
Cdd:COG1236    55 VLTHAHLDHSGAL--PLLVKE-GFRGPI--YATPATADLArillgdsakiqeeeaEAEPLYteedaERALELFQTVDYGE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  90 PTQIslvdeasgekEEVVVTLLPAGHCPGSVMFLFQGSNGTVLYTGDFrlaKGEASRmeLLHSGGRVKDIQSVYLDTTFC 169
Cdd:COG1236   130 PFEI----------GGVRVTFHPAGHILGSAQVELEVGGKRIVFSGDY---GREDDP--LLAPPEPVPPADVLITESTYG 194

                         170       180
                  ....*....|....*....|..
gi 1907137773 170 DPRFyqiPSREQCLRGILELVR 191
Cdd:COG1236   195 DRLH---PPREEVEAELAEWVR 213
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
21-139 3.87e-06

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 48.90  E-value: 3.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  21 RENL-KARAYFLSHCHKDHMKGLraPSLKRRLECSLkvflYCSPVTKELLltspKYRFWENRII----TIEIETPTQISL 95
Cdd:COG0595    58 EENKdKIKGIVLTHGHEDHIGAL--PYLLKELNVPV----YGTPLTLALL----EAKLKEHGLLkkvkLHVVKPGDRIKF 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907137773  96 vdeasgekEEVVVTLLPAGH-CPGSVMFLFQGSNGTVLYTGDFRL 139
Cdd:COG0595   128 --------GPFKVEFFRVTHsIPDSLGLAIRTPAGTIVHTGDFKF 164
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 30-171 6.74e-06

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 47.20  E-value: 6.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  30 FLSHCHKDHMKGLraPSLKRRLECSlKVFLYCSPVTKELLLTSPKYRFWENR----IITIEIETPTQIslvdeasgekEE 105
Cdd:COG1235    73 LLTHEHADHIAGL--DDLRPRYGPN-PIPVYATPGTLEALERRFPYLFAPYPgkleFHEIEPGEPFEI----------GG 139

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907137773 106 VVVTLLPAGH-CPGSVMFLFQGSNGTVLYTGDfrLAKGEASRMELLhsggrvKDIQSVYLDTTFCDP 171
Cdd:COG1235   140 LTVTPFPVPHdAGDPVGYRIEDGGKKLAYATD--TGYIPEEVLELL------RGADLLILDATYDDP 198
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 16-152 1.28e-05

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: 45.84  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  16 IDRFDRENLKARAYFLSHCHKDHMKGLRApsLKRRLECSlkvfLYCSPVTKELLLTSPKYRFWENRII--TIEIETPTQI 93
Cdd:COG0491    42 LAALAALGLDIKAVLLTHLHPDHVGGLAA--LAEAFGAP----VYAHAAEAEALEAPAAGALFGREPVppDRTLEDGDTL 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907137773  94 SLVDeasgekEEVVVTLLPaGHCPGSVMFLFQGSNgtVLYTGDF-------RLAKGEASRMELLHS 152
Cdd:COG0491   116 ELGG------PGLEVIHTP-GHTPGHVSFYVPDEK--VLFTGDAlfsggvgRPDLPDGDLAQWLAS 172
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 27-137 9.37e-05

Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. 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: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 43.09  E-value: 9.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  27 RAYFLSHCHKDHMKGLraPSLKRrlECSLKVFLYCSPVTKEL--LLTSPKYRFWENRIITIEIETPTQI-SLVDEAS--- 100
Cdd:cd07734    51 DAILISHFHLDHCGAL--PYLFR--GFIFRGPIYATHPTVALgrLLLEDYVKSAERIGQDQSLYTPEDIeEALKHIVplg 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907137773 101 -GEKEE----VVVTLLPAGHCPGSVMFLFQGSNGTVLYTGDF 137
Cdd:cd07734   127 yGQSIDlfpaLSLTAYNAGHVLGAAMWEIQIYGEKLVYTGDF 168
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
5-136 1.11e-04

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 43.65  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773   5 QGQMAEYpTISIDRFDrenlkarAYFLSHCHKDHMKGL----RAPSLKRRLEcslKVFLYCSPVTKELLLTSPKYRFWEN 80
Cdd:COG1234    40 QRQLLRA-GLDPRDID-------AIFITHLHGDHIAGLpgllSTRSLAGREK---PLTIYGPPGTKEFLEALLKASGTDL 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907137773  81 --RIITIEIETPTQISLvdeasgekEEVVVTLLPAGHCPGSVMFLFQGSNGTVLYTGD 136
Cdd:COG1234   109 dfPLEFHEIEPGEVFEI--------GGFTVTAFPLDHPVPAYGYRFEEPGRSLVYSGD 158
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 30-178 3.13e-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: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  30 FLSHCHKDHMKGLraPSLKRRLECSlkvfLYCSPVTKELLLTSPKYRFWEN----RIITIEIETPTQISLVDeasgekee 105
Cdd:pfam12706  33 LLTHDHYDHLAGL--LDLREGRPRP----LYAPLGVLAHLRRNFPYLFLLEhygvRVHEIDWGESFTVGDGG-------- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773 106 VVVTLLPAGH--------CPGSVM-FLFQGSNGTVLYTGDFRLAKGEAsrmellhsGGRVKDIQSVYLDTTFCDPRFYQI 176
Cdd:pfam12706  99 LTVTATPARHgsprgldpNPGDTLgFRIEGPGKRVYYAGDTGYFPDEI--------GERLGGADLLLLDGGAWRDDEMIH 170


                  ..
gi 1907137773 177 PS 178
Cdd:pfam12706 171 MG 172
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 16-149 3.60e-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: 41.57  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  16 IDRFDRENLKARAYFLSHCHKDHMKGLraPSLKRRleCSLKVflYCSPvtkellLTSPKYRFWEN--RIITIEIETPTQI 93
Cdd:cd16322    37 LARFGTTGLTLLYILLTHAHFDHVGGV--ADLRRH--PGAPV--YLHP------DDLPLYEAADLgaKAFGLGIEPLPPP 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907137773  94 S-LVDEAS----GEKE-EVVVTllPaGHCPGSVMFLFQgsNGTVLYTGDFrLAKGEASRMEL 149
Cdd:cd16322   105 DrLLEDGQtltlGGLEfKVLHT--P-GHSPGHVCFYVE--EEGLLFSGDL-LFQGSIGRTDL 160
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 30-136 9.35e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase 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, 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 annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 40.71  E-value: 9.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  30 FLSHCHKDHMKGLRA-PSLKrrlecslkvfLYCSPVTKELLLTSPKYRFWENRIITIEIETPTQISLVDEASGEK----E 104
Cdd:cd07730    88 ILSHLHWDHIGGLSDfPNAR----------LIVGPGAKEALRPPGYPSGFLPELLPSDFEGRLVRWEEDDFLWVPlgpfP 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907137773 105 EVV-------VTLLPA-GHCPGSVMFLFQGSNGT-VLYTGD 136
Cdd:cd07730   158 RALdlfgdgsLYLVDLpGHAPGHLGLLARTTSGTwVFLAGD 198
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
30-144 9.51e-04

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 40.04  E-value: 9.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  30 FLSHCHKDHMKGLRApsLKRRLECSLkvflYCSPVTKELLLTSPKYRFWENRIITIEIETPTQISLV-DEASGEKEEVVV 108
Cdd:pfam00753  48 ILTHGHFDHIGGLGE--LAEATDVPV----IVVAEEARELLDEELGLAASRLGLPGPPVVPLPPDVVlEEGDGILGGGLG 121

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907137773 109 TLLPAGHCPGSVMFLFQGSNGTVLYTGDFRLAKGEA 144
Cdd:pfam00753 122 LLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIG 157
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 30-144 1.50e-03

uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Bacillus subtilis yflN protein. 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. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are 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: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 39.51  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  30 FLSHCHKDHMKGLRApsLKRRLECslKVflYCSPVTKELLL--TSPKYRFWENRIITIEIETPTQISLVDE--ASGEKEE 105
Cdd:cd07721    54 LLTHGHIDHIGSLAA--LKEAPGA--PV--YAHEREAPYLEgeKPYPPPVRLGLLGLLSPLLPVKPVPVDRtlEDGDTLD 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907137773 106 VVVTL----LPaGHCPGSVMFLFQGSNgtVLYTGD-FRLAKGEA 144
Cdd:cd07721   128 LAGGLrvihTP-GHTPGHISLYLEEDG--VLIAGDaLVTVGGEL 168
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 30-136 9.12e-03

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: 36.86  E-value: 9.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907137773  30 FLSHCHKDHMKGLraPSL--KRRLECSLK-VFLYCSPVTKELLLTSPKYRFWENR----IITIEIEtPTQISLvdeasgE 102
Cdd:cd16272    55 FLSHFHLDHIGGL--PTLlfARRYGGRKKpLTIYGPKGIKEFLEKLLNFPVEILPlgfpLEIEELE-EGGEVL------E 125

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907137773 103 KEEVVVTLLPAGHCPGSVMFLFQGSNGTVLYTGD 136
Cdd:cd16272   126 LGDLKVEAFPVKHSVESLGYRIEAEGKSIVYSGD 159
 
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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