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Conserved domains on  [gi|71985814|ref|NP_001023110|]
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Zinc phosphodiesterase ELAC protein 2 homolog [Caenorhabditis elegans]

Protein Classification

ribonuclease Z( domain architecture ID 11039737)

ribonuclease Z is a tRNA 3-prime endonuclease that is involved in the maturation of tRNA, such as processing of tRNAs that lack an encoded CCA motif at the 3' end, to prepare for the addition of the motif by tRNA nucleotidyltransferase

CATH:  3.60.15.10
EC:  3.1.26.11
Gene Ontology:  GO:0042781|GO:0046872
PubMed:  17597585|11471246|17363966|12032089
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 421-646 1.05e-70

Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; 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; this eukaryotic subgroup includes short forms (ELAC1) and the C-terminus of long forms including human ELAC2. 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: 293804 [Multi-domain]  Cd Length: 204  Bit Score: 230.13  E-value: 1.05e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 421 LTFFGTSSAVPSKYRNVTGYLVEASENSAILIDVGEGTYGQMRAVFGEDGCKQLLVNLNCVLITHAHQDHMNGLYTIIAR 500
Cdd:cd07718   1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEEADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 501 RKEAFESlgaPYRPLVLVCNRNVLKPMKTYSICFENIEHLLEIVDIsrypltppgspggppgkrprLPSPHLPPSRDVLQ 580
Cdd:cd07718  81 RKKLFKP---PSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISN--------------------RVSQSLPESDDPLS 137

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71985814 581 DMSSSFDKKAWKLDELKAVQVHHTRMANGFVMRVA-GKRIVFSGDTKPCDLLVEEGKDADVLVHEST 646
Cdd:cd07718 138 RDLLSNLLEELGLKSIETVPVIHCPDAYGIVLTHEdGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 28-157 2.84e-10

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 cd16272:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 180  Bit Score: 59.97  E-value: 2.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814  28 IEVLGNGTGLLR-----ACFILRTPLKTYMFNCPENACRFLWQLRIRSSSVVDLFITSANWDNIAGISSILLSKESNALS 102
Cdd:cd16272   1 LTFLGTGGAVPSltrntSSYLLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71985814 103 TRLH--GAMNIKHFLECIRPFqDSDYGSCKYPSQVEERPYTMENYEDAGLKVTYIPL 157
Cdd:cd16272  81 KPLTiyGPKGIKEFLEKLLNF-PVEILPLGFPLEIEELEEGGEVLELGDLKVEAFPV 136
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 180-236 7.89e-09

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 PRK00055:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 270  Bit Score: 57.50  E-value: 7.89e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 71985814  180 IAFLIEMKEAARRIDTMKLMELKVPKGPLIGKLKSGEAVTLPDGRTIQPDQVFSSDK 236
Cdd:PRK00055 108 LGYRIAEKDKPGKLDAEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPPR 164
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 613-687 3.30e-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.


The actual alignment was detected with superfamily member PRK02126:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 334  Bit Score: 49.91  E-value: 3.30e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71985814  613 RVAGKRIVFSGDTKP----CDLLVEEGKDADVLVHESTFEDGHEADAMRKRHSTMGQAVDVGKRMNAKHIILTHFSARY 687
Cdd:PRK02126 239 IEPGQKIGYVTDIGYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRY 317
Nup88 super family cl25737
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 208-272 4.58e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


The actual alignment was detected with superfamily member pfam10168:

Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 40.41  E-value: 4.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71985814   208 LIGKLKSGEAVTLP---DGRTIQPDQVFSSDKVEGDKPLLLVTECTTEDHVKALIDSSSLQPFLNGEK 272
Cdd:pfam10168 457 LVCLLSSGEVISLPlliDAVPPSPPLLCSKEDVTVDEPLRGLQEDSFEDHIKSILQRSVSNPILSADK 524
 
Name Accession Description Interval E-value
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 421-646 1.05e-70

Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; 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; this eukaryotic subgroup includes short forms (ELAC1) and the C-terminus of long forms including human ELAC2. 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: 293804 [Multi-domain]  Cd Length: 204  Bit Score: 230.13  E-value: 1.05e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 421 LTFFGTSSAVPSKYRNVTGYLVEASENSAILIDVGEGTYGQMRAVFGEDGCKQLLVNLNCVLITHAHQDHMNGLYTIIAR 500
Cdd:cd07718   1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEEADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 501 RKEAFESlgaPYRPLVLVCNRNVLKPMKTYSICFENIEHLLEIVDIsrypltppgspggppgkrprLPSPHLPPSRDVLQ 580
Cdd:cd07718  81 RKKLFKP---PSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISN--------------------RVSQSLPESDDPLS 137

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71985814 581 DMSSSFDKKAWKLDELKAVQVHHTRMANGFVMRVA-GKRIVFSGDTKPCDLLVEEGKDADVLVHEST 646
Cdd:cd07718 138 RDLLSNLLEELGLKSIETVPVIHCPDAYGIVLTHEdGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
420-713 8.00e-52

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 180.78  E-value: 8.00e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 420 KLTFFGTSSAVPSKYRNVTGYLVEAsENSAILIDVGEGTYGQMRAvFGEDGCKqllvnLNCVLITHAHQDHMNGLYTIIA 499
Cdd:COG1234   2 KLTFLGTGGAVPTPGRATSSYLLEA-GGERLLIDCGEGTQRQLLR-AGLDPRD-----IDAIFITHLHGDHIAGLPGLLS 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 500 RRkeafeSLGAPYRPLVLVCNRNVLkpmktysicfENIEHLLEIVDIS-RYPLTppgspggppgkrprlpsphlppsrdv 578
Cdd:COG1234  75 TR-----SLAGREKPLTIYGPPGTK----------EFLEALLKASGTDlDFPLE-------------------------- 113

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 579 LQDMSssfDKKAWKLDELK--AVQVHHTRMANGFVMRVAGKRIVFSGDTKPCDLLVEEGKDADVLVHESTFEDGHEADAM 656
Cdd:COG1234 114 FHEIE---PGEVFEIGGFTvtAFPLDHPVPAYGYRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAK 190

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71985814 657 RKRHSTMGQAVDVGKRMNAKHIILTHFSARYPKvpvLPEYLD------KENIGVAMDMLRVRF 713
Cdd:COG1234 191 ETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDD---PEELLAearavfPGPVELAEDGMVIEL 250
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 420-713 1.03e-40

ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN. [Transcription, RNA processing]


Pssm-ID: 274246 [Multi-domain]  Cd Length: 299  Bit Score: 151.22  E-value: 1.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814   420 KLTFFGTSSAVPSKYRNVTGYLVEAsENSAILIDVGEGTYGQMRAV---FGedgckqllvNLNCVLITHAHQDHMNGLYT 496
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-NGELWLFDCGEGTQRQMLRSgisPM---------KIDRIFITHLHGDHILGLPG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814   497 IIARRkeafeSLGAPYRPL----------VLVCNRNVLKPMKTYSICFENIEHLLEIVDISRYPLTPpgspggppgkrpr 566
Cdd:TIGR02651  71 LLSTM-----SFQGRKEPLtiygppgikeFIETSLRVSYTYLNYPIKIHEIEEGGLVFEDDGFKVEA------------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814   567 LPSPHLPPS---RDVLQDMSSSFDKKawKLDEL--------------KAVQVhhtrmANGFVMR---VA-----GKRIVF 621
Cdd:TIGR02651 133 FPLDHSIPSlgyRFEEKDRPGKFDRE--KAKELgippgplygklkrgETVTL-----IDGRIIDpedVLgpprkGRKIAY 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814   622 SGDTKPCDLLVEEGKDADVLVHESTFEDGHEADAMRKRHSTMGQAVDVGKRMNAKHIILTHFSARYPKVPVLPEYLDK-- 699
Cdd:TIGR02651 206 TGDTRPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDEEELLEEAKKif 285

                         330
                  ....*....|....
gi 71985814   700 ENIGVAMDMLRVRF 713
Cdd:TIGR02651 286 PNTYIAEDFMEIEI 299
PRK00055 PRK00055
ribonuclease Z; Reviewed
 420-714 2.37e-40

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 149.56  E-value: 2.37e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814  420 KLTFFGTSSAVPSKYRNVTGYLVEAsENSAILIDVGEGTYGQMRAV---FGedgckqllvNLNCVLITHAHQDHMNGLYT 496
Cdd:PRK00055   3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQLLKTgikPR---------KIDKIFITHLHGDHIFGLPG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814  497 IIARRkeafeSLGAPYRPLVLVCnrnvlkPMKTysicFENIEHLLEIVDISRYPLTPPGspggppgKRPRLP-----SPH 571
Cdd:PRK00055  73 LLSTR-----SLSGRTEPLTIYG------PKGI----KEFVETLLRASGSLGYRIAEKD-------KPGKLDaeklkALG 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814  572 LPPSRDV--LQDmsssfdKKAWKLDElkavqvhHTRMANGFVMRVA--GKRIVFSGDTKPCDLLVEEGKDADVLVHESTF 647
Cdd:PRK00055 131 VPPGPLFgkLKR------GEDVTLED-------GRIINPADVLGPPrkGRKVAYCGDTRPCEALVELAKGADLLVHEATF 197

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71985814  648 EDGHEADAMRKRHSTMGQAVDVGKRMNAKHIILTHFSARYPKVPvlPEYLDK-----ENIGVAMDMLRVRFD 714
Cdd:PRK00055 198 GDEDEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTGDP--EELLKEareifPNTELAEDLMRVEVP 267
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 450-683 2.54e-13

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: 69.26  E-value: 2.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814   450 ILIDVGEGTYGQMRAVFgeDGCKQLLVNLNCVLITHAHQDHMNGLYTIiarRKEAFESLGAPYRPLVLVCNRNVLkpmkt 529
Cdd:pfam12706   3 ILIDPGPDLRQQALPAL--QPGRLRDDPIDAVLLTHDHYDHLAGLLDL---REGRPRPLYAPLGVLAHLRRNFPY----- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814   530 ysiCFENIEHLLEIVDI---SRYPLTPPGSPGGPpgkrprLPSPHLPPSRDVLqdmsssfdkkawkldelkavqvhHTRM 606
Cdd:pfam12706  73 ---LFLLEHYGVRVHEIdwgESFTVGDGGLTVTA------TPARHGSPRGLDP-----------------------NPGD 120

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71985814   607 ANGFVMRVAGKRIVFSGDTKPC-DLLVEEGKDADVLVHESTFEDGHEADAMRkrHSTMGQAVDVGKRMNAKHIILTHF 683
Cdd:pfam12706 121 TLGFRIEGPGKRVYYAGDTGYFpDEIGERLGGADLLLLDGGAWRDDEMIHMG--HMTPEEAVEAAADLGARRKVLIHI 196
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 28-157 2.84e-10

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: 59.97  E-value: 2.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814  28 IEVLGNGTGLLR-----ACFILRTPLKTYMFNCPENACRFLWQLRIRSSSVVDLFITSANWDNIAGISSILLSKESNALS 102
Cdd:cd16272   1 LTFLGTGGAVPSltrntSSYLLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71985814 103 TRLH--GAMNIKHFLECIRPFqDSDYGSCKYPSQVEERPYTMENYEDAGLKVTYIPL 157
Cdd:cd16272  81 KPLTiyGPKGIKEFLEKLLNF-PVEILPLGFPLEIEELEEGGEVLELGDLKVEAFPV 136
PRK00055 PRK00055
ribonuclease Z; Reviewed
 180-236 7.89e-09

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 57.50  E-value: 7.89e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 71985814  180 IAFLIEMKEAARRIDTMKLMELKVPKGPLIGKLKSGEAVTLPDGRTIQPDQVFSSDK 236
Cdd:PRK00055 108 LGYRIAEKDKPGKLDAEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPPR 164
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 440-500 2.06e-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: 48.70  E-value: 2.06e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71985814    440 YLVEaSENSAILIDVGEGTYGQMRAVFGEDGckqlLVNLNCVLITHAHQDHMNGLYTIIAR 500
Cdd:smart00849   3 YLVR-DDGGAILIDTGPGEAEDLLAELKKLG----PKKIDAIILTHGHPDHIGGLPELLEA 58
PRK02126 PRK02126
ribonuclease Z; Provisional
 613-687 3.30e-06

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 49.91  E-value: 3.30e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71985814  613 RVAGKRIVFSGDTKP----CDLLVEEGKDADVLVHESTFEDGHEADAMRKRHSTMGQAVDVGKRMNAKHIILTHFSARY 687
Cdd:PRK02126 239 IEPGQKIGYVTDIGYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRY 317
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 208-272 4.58e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 40.41  E-value: 4.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71985814   208 LIGKLKSGEAVTLP---DGRTIQPDQVFSSDKVEGDKPLLLVTECTTEDHVKALIDSSSLQPFLNGEK 272
Cdd:pfam10168 457 LVCLLSSGEVISLPlliDAVPPSPPLLCSKEDVTVDEPLRGLQEDSFEDHIKSILQRSVSNPILSADK 524
 
Name Accession Description Interval E-value
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 421-646 1.05e-70

Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; 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; this eukaryotic subgroup includes short forms (ELAC1) and the C-terminus of long forms including human ELAC2. 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: 293804 [Multi-domain]  Cd Length: 204  Bit Score: 230.13  E-value: 1.05e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 421 LTFFGTSSAVPSKYRNVTGYLVEASENSAILIDVGEGTYGQMRAVFGEDGCKQLLVNLNCVLITHAHQDHMNGLYTIIAR 500
Cdd:cd07718   1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEEADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 501 RKEAFESlgaPYRPLVLVCNRNVLKPMKTYSICFENIEHLLEIVDIsrypltppgspggppgkrprLPSPHLPPSRDVLQ 580
Cdd:cd07718  81 RKKLFKP---PSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISN--------------------RVSQSLPESDDPLS 137

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71985814 581 DMSSSFDKKAWKLDELKAVQVHHTRMANGFVMRVA-GKRIVFSGDTKPCDLLVEEGKDADVLVHEST 646
Cdd:cd07718 138 RDLLSNLLEELGLKSIETVPVIHCPDAYGIVLTHEdGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
420-713 8.00e-52

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 180.78  E-value: 8.00e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 420 KLTFFGTSSAVPSKYRNVTGYLVEAsENSAILIDVGEGTYGQMRAvFGEDGCKqllvnLNCVLITHAHQDHMNGLYTIIA 499
Cdd:COG1234   2 KLTFLGTGGAVPTPGRATSSYLLEA-GGERLLIDCGEGTQRQLLR-AGLDPRD-----IDAIFITHLHGDHIAGLPGLLS 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 500 RRkeafeSLGAPYRPLVLVCNRNVLkpmktysicfENIEHLLEIVDIS-RYPLTppgspggppgkrprlpsphlppsrdv 578
Cdd:COG1234  75 TR-----SLAGREKPLTIYGPPGTK----------EFLEALLKASGTDlDFPLE-------------------------- 113

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 579 LQDMSssfDKKAWKLDELK--AVQVHHTRMANGFVMRVAGKRIVFSGDTKPCDLLVEEGKDADVLVHESTFEDGHEADAM 656
Cdd:COG1234 114 FHEIE---PGEVFEIGGFTvtAFPLDHPVPAYGYRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAK 190

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71985814 657 RKRHSTMGQAVDVGKRMNAKHIILTHFSARYPKvpvLPEYLD------KENIGVAMDMLRVRF 713
Cdd:COG1234 191 ETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDD---PEELLAearavfPGPVELAEDGMVIEL 250
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 421-693 2.28e-49

Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; 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. 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. 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; this subgroup includes the short form (ELAC1). Only the short form exists in bacteria. 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: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 173.79  E-value: 2.28e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 421 LTFFGTSSAVPSKYRNVTGYLVEAsENSAILIDVGEGTYGQMRAVfgedGCKqlLVNLNCVLITHAHQDHMNGLYTIIAR 500
Cdd:cd07717   1 LTFLGTGSAVPTPERNLSSIALRL-EGELWLFDCGEGTQRQLLRA----GLS--PSKIDRIFITHLHGDHILGLPGLLST 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 501 RkeafeSLGAPYRPLVLV----------CNRNVLKPMKTYSICFENIEHLLEIVdisrypltppgspggppgkrprlpsp 570
Cdd:cd07717  74 M-----SLLGRTEPLTIYgpkglkefleTLLRLSASRLPYPIEVHELEPDPGLV-------------------------- 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 571 hlppsrdvlqdmsssFDKKAWKLdelKAVQVHHTRMANGFVMRVaGKRIVFSGDTKPCDLLVEEGKDADVLVHESTFEDG 650
Cdd:cd07717 123 ---------------FEDDGFTV---TAFPLDHRVPCFGYRFEE-GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDD 183

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 71985814 651 HEADAMRKRHSTMGQAVDVGKRMNAKHIILTHFSARYPKVPVL 693
Cdd:cd07717 184 DAEKAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARYKDPEEL 226
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 420-713 1.03e-40

ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN. [Transcription, RNA processing]


Pssm-ID: 274246 [Multi-domain]  Cd Length: 299  Bit Score: 151.22  E-value: 1.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814   420 KLTFFGTSSAVPSKYRNVTGYLVEAsENSAILIDVGEGTYGQMRAV---FGedgckqllvNLNCVLITHAHQDHMNGLYT 496
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-NGELWLFDCGEGTQRQMLRSgisPM---------KIDRIFITHLHGDHILGLPG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814   497 IIARRkeafeSLGAPYRPL----------VLVCNRNVLKPMKTYSICFENIEHLLEIVDISRYPLTPpgspggppgkrpr 566
Cdd:TIGR02651  71 LLSTM-----SFQGRKEPLtiygppgikeFIETSLRVSYTYLNYPIKIHEIEEGGLVFEDDGFKVEA------------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814   567 LPSPHLPPS---RDVLQDMSSSFDKKawKLDEL--------------KAVQVhhtrmANGFVMR---VA-----GKRIVF 621
Cdd:TIGR02651 133 FPLDHSIPSlgyRFEEKDRPGKFDRE--KAKELgippgplygklkrgETVTL-----IDGRIIDpedVLgpprkGRKIAY 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814   622 SGDTKPCDLLVEEGKDADVLVHESTFEDGHEADAMRKRHSTMGQAVDVGKRMNAKHIILTHFSARYPKVPVLPEYLDK-- 699
Cdd:TIGR02651 206 TGDTRPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDEEELLEEAKKif 285

                         330
                  ....*....|....
gi 71985814   700 ENIGVAMDMLRVRF 713
Cdd:TIGR02651 286 PNTYIAEDFMEIEI 299
PRK00055 PRK00055
ribonuclease Z; Reviewed
 420-714 2.37e-40

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 149.56  E-value: 2.37e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814  420 KLTFFGTSSAVPSKYRNVTGYLVEAsENSAILIDVGEGTYGQMRAV---FGedgckqllvNLNCVLITHAHQDHMNGLYT 496
Cdd:PRK00055   3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQLLKTgikPR---------KIDKIFITHLHGDHIFGLPG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814  497 IIARRkeafeSLGAPYRPLVLVCnrnvlkPMKTysicFENIEHLLEIVDISRYPLTPPGspggppgKRPRLP-----SPH 571
Cdd:PRK00055  73 LLSTR-----SLSGRTEPLTIYG------PKGI----KEFVETLLRASGSLGYRIAEKD-------KPGKLDaeklkALG 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814  572 LPPSRDV--LQDmsssfdKKAWKLDElkavqvhHTRMANGFVMRVA--GKRIVFSGDTKPCDLLVEEGKDADVLVHESTF 647
Cdd:PRK00055 131 VPPGPLFgkLKR------GEDVTLED-------GRIINPADVLGPPrkGRKVAYCGDTRPCEALVELAKGADLLVHEATF 197

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71985814  648 EDGHEADAMRKRHSTMGQAVDVGKRMNAKHIILTHFSARYPKVPvlPEYLDK-----ENIGVAMDMLRVRFD 714
Cdd:PRK00055 198 GDEDEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTGDP--EELLKEareifPNTELAEDLMRVEVP 267
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 421-645 4.16e-31

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: 120.06  E-value: 4.16e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 421 LTFFGTSSAVPSKYRNVTGYLVEAsENSAILIDVGEGTYGQMRAvfgedgCKQLLVNLNCVLITHAHQDHMNGLYTIIAR 500
Cdd:cd16272   1 LTFLGTGGAVPSLTRNTSSYLLET-GGTRILLDCGEGTVYRLLK------AGVDPDKLDAIFLSHFHLDHIGGLPTLLFA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 501 RKEAFESlgapyRPLVLVCNRNVLKPMKTYSICFENIEHLleivdisRYPLTPpgspggppgkrprlpsPHLPPSRDVLQ 580
Cdd:cd16272  74 RRYGGRK-----KPLTIYGPKGIKEFLEKLLNFPVEILPL-------GFPLEI----------------EELEEGGEVLE 125

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71985814 581 DmsssfdkkawKLDELKAVQVHHTRMANGFVMRVAGKRIVFSGDTKPCDLLVEEGKDADVLVHES 645
Cdd:cd16272 126 L----------GDLKVEAFPVKHSVESLGYRIEAEGKSIVYSGDTGPCENLVELAKGADLLIHEC 180
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 420-713 1.58e-22

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 97.66  E-value: 1.58e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 420 KLTFFGTSSAVPS---------------KY-RNVTGYLVEAsENSAILIDVGEGTYGQMRAvFGEDgckqlLVNLNCVLI 483
Cdd:COG1235   2 KVTFLGSGSSGGVpqigcdcpvcastdpRYgRTRSSILVEA-DGTRLLIDAGPDLREQLLR-LGLD-----PSKIDAILL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 484 THAHQDHMNGLYTIIARRKEafeslgapyRPLVLVCNRNVLKPMKT-YSICFENIEHLLEIVDISRYpltppgspggppg 562
Cdd:COG1235  75 THEHADHIAGLDDLRPRYGP---------NPIPVYATPGTLEALERrFPYLFAPYPGKLEFHEIEPG------------- 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 563 krprlpsphlppsrdvlqdmsssfdkKAWKLDELK--AVQVHHTRMAN-GFVMRVAGKRIVFSGDTKP-CDLLVEEGKDA 638
Cdd:COG1235 133 --------------------------EPFEIGGLTvtPFPVPHDAGDPvGYRIEDGGKKLAYATDTGYiPEEVLELLRGA 186

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 639 DVLVHESTFEDGHEAdamrkrHSTMGQAVDVGKRMNAKHIILTHFSARYPKvPVLPE-----YLDKENIGVAMDMLRVRF 713
Cdd:COG1235 187 DLLILDATYDDPEPG------HLSNEEALELLARLGPKRLVLTHLSPDNND-HELDYdeleaALLPAGVEVAYDGMEIEL 259
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 420-643 2.09e-20

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: 89.50  E-value: 2.09e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 420 KLTFFGTSSAVPSKYRNVTGYLVEAsENSAILIDVGEGTYGQMRAVfgedGCKqlLVNLNCVLITHAHQDHMNGLYTII- 498
Cdd:cd07719   1 RVTLLGTGGPIPDPDRAGPSTLVVV-GGRVYLVDAGSGVVRRLAQA----GLP--LGDLDAVFLTHLHSDHVADLPALLl 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 499 ----ARRKEAFESLGAPyrplvlvcnrnvlkpmktysicfeniehlleivDISRYPLTPPGSPGGPPGKRPRLPSPHLPP 574
Cdd:cd07719  74 tawlAGRKTPLPVYGPP---------------------------------GTRALVDGLLAAYALDIDYRARIGDEGRPD 120

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71985814 575 SRDVLQDMSSSFDKKAWKLDELK--AVQVHHTRMANGFVMRV--AGKRIVFSGDTKPCDLLVEEGKDADVLVH 643
Cdd:cd07719 121 PGALVEVHEIAAGGVVYEDDGVKvtAFLVDHGPVPPALAYRFdtPGRSVVFSGDTGPSENLIELAKGADLLVH 193
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 420-645 3.36e-15

uncharacterized bacterial subgroup of Ribonuclease Z, short form; 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. Members of this bacterial 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: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 74.02  E-value: 3.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 420 KLTFFGTSSAVPSKYRNVTGYLVEAsENSAILIDVGEGTYGQMRAVfgedgckQLLVNLNCVLITHAHQDHMNGLYTI-I 498
Cdd:cd07716   1 KLTVLGCSGSYPGPGGACSGYLLEA-DGFRILLDCGSGVLSRLQRY-------IDPEDLDAVVLSHLHPDHCADLGVLqY 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 499 ARRkeaFESLGAPYRPLVLVCnrnvlkpmktysicfeniehlleivdisrypltppgspggppgkrPRLPSPHLppsrDV 578
Cdd:cd07716  73 ARR---YHPRGARKPPLPLYG---------------------------------------------PAGPAERL----AA 100

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71985814 579 LQDMSSSFDKKAWKLDE--------LKAVQVHHTrmANGFVMRV--AGKRIVFSGDTKPCDLLVEEGKDADVLVHES 645
Cdd:cd07716 101 LYGLEDVFDFHPIEPGEpleigpftITFFRTVHP--VPCYAMRIedGGKVLVYTGDTGYCDELVEFARGADLLLCEA 175
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 422-650 4.05e-15

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) 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: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 74.60  E-value: 4.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 422 TFFGTSSAVPSKYRNVTGYLVeASENSAILIDVGEGTYGQMRAvFGEDgckqlLVNLNCVLITHAHQDHMNGL------Y 495
Cdd:cd07740   1 TFLGSGDAFGSGGRLNTCFHV-ASEAGRFLIDCGASSLIALKR-AGID-----PNAIDAIFITHLHGDHFGGLpfflldA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 496 TIIARRKeafeslgapyRPLVLVCNRNVLkpmktysicfENIEHLLEIVdisrypltppgspggppgkrprlpsphLPPS 575
Cdd:cd07740  74 QFVAKRT----------RPLTIAGPPGLR----------ERLRRAMEAL---------------------------FPGS 106

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 576 RDVLQdmssSFDkkaWKLDEL-------------KAVQVHHTRMANGFVMR--VAGKRIVFSGDTKPCDLLVEEGKDADV 640
Cdd:cd07740 107 SKVPR----RFD---LEVIELepgepttlggvtvTAFPVVHPSGALPLALRleAAGRVLAYSGDTEWTDALVPLARGADL 179

                       250
                ....*....|
gi 71985814 641 LVHESTFEDG 650
Cdd:cd07740 180 FICECYFFEK 189
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 450-683 2.54e-13

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: 69.26  E-value: 2.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814   450 ILIDVGEGTYGQMRAVFgeDGCKQLLVNLNCVLITHAHQDHMNGLYTIiarRKEAFESLGAPYRPLVLVCNRNVLkpmkt 529
Cdd:pfam12706   3 ILIDPGPDLRQQALPAL--QPGRLRDDPIDAVLLTHDHYDHLAGLLDL---REGRPRPLYAPLGVLAHLRRNFPY----- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814   530 ysiCFENIEHLLEIVDI---SRYPLTPPGSPGGPpgkrprLPSPHLPPSRDVLqdmsssfdkkawkldelkavqvhHTRM 606
Cdd:pfam12706  73 ---LFLLEHYGVRVHEIdwgESFTVGDGGLTVTA------TPARHGSPRGLDP-----------------------NPGD 120

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71985814   607 ANGFVMRVAGKRIVFSGDTKPC-DLLVEEGKDADVLVHESTFEDGHEADAMRkrHSTMGQAVDVGKRMNAKHIILTHF 683
Cdd:pfam12706 121 TLGFRIEGPGKRVYYAGDTGYFpDEIGERLGGADLLLLDGGAWRDDEMIHMG--HMTPEEAVEAAADLGARRKVLIHI 196
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 28-157 2.84e-10

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: 59.97  E-value: 2.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814  28 IEVLGNGTGLLR-----ACFILRTPLKTYMFNCPENACRFLWQLRIRSSSVVDLFITSANWDNIAGISSILLSKESNALS 102
Cdd:cd16272   1 LTFLGTGGAVPSltrntSSYLLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71985814 103 TRLH--GAMNIKHFLECIRPFqDSDYGSCKYPSQVEERPYTMENYEDAGLKVTYIPL 157
Cdd:cd16272  81 KPLTiyGPKGIKEFLEKLLNF-PVEILPLGFPLEIEELEEGGEVLELGDLKVEAFPV 136
PRK00055 PRK00055
ribonuclease Z; Reviewed
 180-236 7.89e-09

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 57.50  E-value: 7.89e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 71985814  180 IAFLIEMKEAARRIDTMKLMELKVPKGPLIGKLKSGEAVTLPDGRTIQPDQVFSSDK 236
Cdd:PRK00055 108 LGYRIAEKDKPGKLDAEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPPR 164
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 440-500 2.06e-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: 48.70  E-value: 2.06e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71985814    440 YLVEaSENSAILIDVGEGTYGQMRAVFGEDGckqlLVNLNCVLITHAHQDHMNGLYTIIAR 500
Cdd:smart00849   3 YLVR-DDGGAILIDTGPGEAEDLLAELKKLG----PKKIDAIILTHGHPDHIGGLPELLEA 58
PRK14866 PRK14866
hypothetical protein; Provisional
 191-231 3.22e-06

hypothetical protein; Provisional


Pssm-ID: 237840  Cd Length: 451  Bit Score: 50.38  E-value: 3.22e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 71985814  191 RRIDTMKLMELKVPKGPLIGKLKSGEAVTLpDGRTIQPDQV 231
Cdd:PRK14866 396 ERFDPELARKLGVPEGPAFGKLAAGQPVEV-DGETITPEMV 435
PRK02126 PRK02126
ribonuclease Z; Provisional
 613-687 3.30e-06

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 49.91  E-value: 3.30e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71985814  613 RVAGKRIVFSGDTKP----CDLLVEEGKDADVLVHESTFEDGHEADAMRKRHSTMGQAVDVGKRMNAKHIILTHFSARY 687
Cdd:PRK02126 239 IEPGQKIGYVTDIGYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRY 317
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 421-682 1.10e-05

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) 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: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 47.18  E-value: 1.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 421 LTFFGTSSAvpskyRNVTGYLVEAS-------ENSAILIDVGEGTYGQMrAVFGEDgckqlLVNLNCVLITHAHQDHMNG 493
Cdd:cd07741   1 IIFLGTGGG-----RFVVITQLRASggiwielNGKNIHIDPGPGALVRM-CRPKLD-----PTKLDAIILSHRHLDHSND 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 494 LYTIIarrkEAFeSLGAPYRPLVLVCNRNVLKpmktysicfENIEHLLEIVdisrypltppgspggppgkRPRLPSPHLP 573
Cdd:cd07741  70 ANVLI----EAM-TEGGFKKRGTLLAPEDALN---------GEPVVLLYYH-------------------RRKLEEIEIL 116

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 574 PsrdvlqdmsssfDKKAWKLDELKAVQV---HHTRMANGFVMRVAGKRIVFSGDTKPCDLLVEEGKDADVLVHESTFEDG 650
Cdd:cd07741 117 E------------EGDEYELGGIKIEATrhkHSDPTTYGFIFRTSDKKIGYISDTRYFEELIEYYSNCDVLIINVTRPRP 184

                       250       260       270
                ....*....|....*....|....*....|..
gi 71985814 651 HEadamRKRHSTMGQAVDVGKRMNAKHIILTH 682
Cdd:cd07741 185 RK----GVDHLSVEDVEKILKEIKPKLAILTH 212
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 436-512 1.63e-05

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: 46.12  E-value: 1.63e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71985814 436 NVTGYLVEASENSAILIDVGEGTYGQMRAVFGEDGCKqllvnLNCVLITHAHQDHMNGLYTIiarrKEAFeslGAPY 512
Cdd:cd06262   9 QTNCYLVSDEEGEAILIDPGAGALEKILEAIEELGLK-----IKAILLTHGHFDHIGGLAEL----KEAP---GAPV 73
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 421-490 1.89e-05

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: 46.30  E-value: 1.89e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71985814 421 LTFFGtsSAvpskyRNVTG--YLVEAsENSAILIDVG-----EGTYGQMRAVFGEDgckqlLVNLNCVLITHAHQDH 490
Cdd:cd16295   1 LTFLG--AA-----REVTGscYLLET-GGKRILLDCGlfqggKELEELNNEPFPFD-----PKEIDAVILTHAHLDH 64
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 420-494 2.23e-05

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: 45.93  E-value: 2.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 420 KLTFFGT--SSAVP-----------SKYRNV---TGYLVEaSENSAILIDVG-EgtygqMRAvfgedgckQLLVN----L 478
Cdd:cd16279   2 KLTFLGTgtSSGVPvigcdcgvcdsSDPKNRrlrSSILIE-TGGKNILIDTGpD-----FRQ--------QALRAgirkL 67

                        90
                ....*....|....*.
gi 71985814 479 NCVLITHAHQDHMNGL 494
Cdd:cd16279  68 DAVLLTHAHADHIHGL 83
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 437-500 3.96e-05

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: 45.29  E-value: 3.96e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71985814 437 VTGYLVEaSENSAILIDVG-EGTYGQMRAVFGEDGCKqlLVNLNCVLITHAHQDHMNGLYTIIAR 500
Cdd:cd07721  11 VNAYLIE-DDDGLTLIDTGlPGSAKRILKALRELGLS--PKDIRRILLTHGHIDHIGSLAALKEA 72
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
440-658 5.17e-05

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 45.05  E-value: 5.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814   440 YLVEaSENSAILIDVGEGTYGQMRAVFGEDGCKQLlvNLNCVLITHAHQDHMNGLYTIIARRKeafeslgapyrplvlvc 519
Cdd:pfam00753   9 YLIE-GGGGAVLIDTGGSAEAALLLLLAALGLGPK--DIDAVILTHGHFDHIGGLGELAEATD----------------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814   520 nrnvlkpmktysicfeniEHLLEIVDISRYPLTPPGSPGGPPGKRPRLPSPHLPPSRDVLQDMSssfdkkawKLDELKAV 599
Cdd:pfam00753  69 ------------------VPVIVVAEEARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDG--------ILGGGLGL 122

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71985814   600 QVHHTRM--ANGFVMRVAGKRIVFSGDT---KPCDLLVEEGKDADVLVHESTFEDGHEADAMRK 658
Cdd:pfam00753 123 LVTHGPGhgPGHVVVYYGGGKVLFTGDLlfaGEIGRLDLPLGGLLVLHPSSAESSLESLLKLAK 186
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 420-647 9.19e-05

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 45.56  E-value: 9.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 420 KLTFFGTSsavpskyRNVTG--YLVEAsENSAILIDVG--EGTYGQMRAVFGEDgckqlLVNLNCVLITHAHQDHmngly 495
Cdd:COG1236   2 KLTFLGAA-------GEVTGscYLLET-GGTRILIDCGlfQGGKERNWPPFPFR-----PSDVDAVVLTHAHLDH----- 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 496 tiiARR-----KEAFEslgAPY---RPlvlvcNRNVLKPMktysicFENIEHLLEIvDISRYPLTPPgspggppgkrprl 567
Cdd:COG1236  64 ---SGAlpllvKEGFR---GPIyatPA-----TADLARIL------LGDSAKIQEE-EAEAEPLYTE------------- 112

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 568 psphlppsRDVLQDMSSsfdkkawkldeLKAVQVHHTRMANGF----------------VMRVAGKRIVFSGDTKPCDLL 631
Cdd:COG1236 113 --------EDAERALEL-----------FQTVDYGEPFEIGGVrvtfhpaghilgsaqvELEVGGKRIVFSGDYGREDDP 173

                       250       260
                ....*....|....*....|
gi 71985814 632 VEEG----KDADVLVHESTF 647
Cdd:COG1236 174 LLAPpepvPPADVLITESTY 193
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 28-231 1.79e-04

Ribonuclease Z, N-terminus of human ELAC2 and related proteins; 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. This eukaryotic subgroup includes the N-terminus of human ELAC2 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.


Pssm-ID: 293854 [Multi-domain]  Cd Length: 175  Bit Score: 43.02  E-value: 1.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814  28 IEVLGNGTGLLRACFILRTPLKTYMFNCPENACRFLWQLRIRSSSVVDLFITSANWDNIAGISSILLSKESNALStrlhg 107
Cdd:cd16296   1 LQVVAAGSRDMGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLP----- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 108 amnikhflECIRPfqdsdyGSCKypsqveerpytmenyedaglkvtyiplSPPLNIGSNNEKSknVKVNNVDIAFLIEMK 187
Cdd:cd16296  76 --------KCVLS------GPNK---------------------------QSPDKIGVRRQIL--ERDPSLVVAFICKLH 112

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 71985814 188 EAARRIDTMKLMELKVPKG-----PLIGKLKSGEAVTLpDGRTIQPDQV 231
Cdd:cd16296 113 LKKGNFLVLKAKELGLPVGtaaiaPIIAAVKDGKSITF-EGREILAEEL 160
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 441-502 2.72e-04

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 43.31  E-value: 2.72e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71985814 441 LVEASENSAILIDVGEGTYGQMravfGEDGCKQLLVNLNC-----VLITHAHQDHMNGLYTIIARRK 502
Cdd:COG2333  15 LIRTPDGKTILIDTGPRPSFDA----GERVVLPYLRALGIrrldlLVLTHPDADHIGGLAAVLEAFP 77
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 420-683 4.34e-04

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 42.60  E-value: 4.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 420 KLTFFGTSSavpskyrnvtgYLVEaSENSAILID---VGEGTYGQMRAVFGEDgckqlLVNLNCVLITHAHQDHMNglYT 496
Cdd:COG2220   5 KITWLGHAT-----------FLIE-TGGKRILIDpvfSGRASPVNPLPLDPED-----LPKIDAVLVTHDHYDHLD--DA 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 497 IIARRKEAfeslGAPYrplvlVCNRNVLKPMKTYSicFENIE--HLLEIVDISRYPLTppgspggppgkrpRLPSPHLPP 574
Cdd:COG2220  66 TLRALKRT----GATV-----VAPLGVAAWLRAWG--FPRVTelDWGESVELGGLTVT-------------AVPARHSSG 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 575 SRDvlqdmsssfdkkawkldelkavqvHHTRMANGFVMRVAGKRIVFSGDTKPCDLLVEEGKDADV---LVHestfedgh 651
Cdd:COG2220 122 RPD------------------------RNGGLWVGFVIETDGKTIYHAGDTGYFPEMKEIGERFPIdvaLLP-------- 169

                       250       260       270
                ....*....|....*....|....*....|..
gi 71985814 652 eADAMRkRHSTMGQAVDVGKRMNAKHIILTHF 683
Cdd:COG2220 170 -IGAYP-FTMGPEEAAEAARDLKPKVVIPIHY 199
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 420-494 4.48e-04

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: 42.58  E-value: 4.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 420 KLTFFGTSSAVPSkyRNVTGYLV-EASENSAILIDVGEGTYG----QMRAVFGEDGCK---QLLVNLNCVLITHAHQDHM 491
Cdd:cd07735   2 ELVVLGCSGGPDE--GNTSSFLLdPAGSDGDILLDAGTGVGAlsleEMFNDILFPSQKaayELYQRIRHYLITHAHLDHI 79


                ...
gi 71985814 492 NGL 494
Cdd:cd07735  80 AGL 82
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 419-497 1.07e-03

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. 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: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 40.68  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 419 PKLTFFGTSSA--VPS---------KYRNVTGY-------LVEAsENSAILIDVGEGTYGQMRAVfgedgckqllVNLNC 480
Cdd:cd07736   1 MKLTFLGTGDAggVPVygcdcsacqRARQDPSYrrrpcsaLIEV-DGERILLDAGLTDLAERFPP----------GSIDA 69

                        90
                ....*....|....*..
gi 71985814 481 VLITHAHQDHMNGLYTI 497
Cdd:cd07736  70 ILLTHFHMDHVQGLFHL 86
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 436-505 2.35e-03

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. 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: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 40.61  E-value: 2.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985814 436 NVTGYLVEaSENSAILIDVGEGtyGQMRAVFGedgckQLLVNL----------NCVLITHAHQDHMNGLYTiiARRKEAF 505
Cdd:cd07720  48 SVNAFLVR-TGGRLILVDTGAG--GLFGPTAG-----KLLANLaaagidpediDDVLLTHLHPDHIGGLVD--AGGKPVF 117
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 440-494 2.90e-03

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. 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: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 39.44  E-value: 2.90e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71985814 440 YLVeASENSAILIDVGEG--TYGQ-MRAVFGEDGCKQLlvnlNCVLITHAHQDHMNGL 494
Cdd:cd07722  21 YLV-GTGKRRILIDTGEGrpSYIPlLKSVLDSEGNATI----SDILLTHWHHDHVGGL 73
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 208-272 4.58e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 40.41  E-value: 4.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71985814   208 LIGKLKSGEAVTLP---DGRTIQPDQVFSSDKVEGDKPLLLVTECTTEDHVKALIDSSSLQPFLNGEK 272
Cdd:pfam10168 457 LVCLLSSGEVISLPlliDAVPPSPPLLCSKEDVTVDEPLRGLQEDSFEDHIKSILQRSVSNPILSADK 524
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 440-494 8.04e-03

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: 38.48  E-value: 8.04e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71985814 440 YLVEASE-NSAILIDVGEGTYgQMRAVFGEDGCKqllvnLNCVLITHAHQDHMNGL 494
Cdd:cd16322  14 YLVADEGgGEAVLVDPGDESE-KLLARFGTTGLT-----LLYILLTHAHFDHVGGV 63
 
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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