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Conserved domains on  [gi|19113935|ref|NP_593023|]
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3' tRNA-processing endonuclease tRNAse Z L2 Trz1 [Schizosaccharomyces pombe]

Protein Classification

ribonuclease Z( domain architecture ID 11224874)

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 ...
 500-711 1.45e-92

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: 288.68  E-value: 1.45e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 500 ICTLGTGSAMPSLYRNVSSTYVRIPvdkkcmedsaiSMKNILLDCGEGTLGRLSRQYGDNLKYEI-ASLRWIYISHMHAD 578
Cdd:cd07718   1 VVFLGTGSAIPSKYRNVSGILLRIP-----------GDGSILLDCGEGTLGQLRRHYGPEEADEVlRNLKCIFISHLHAD 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 579 HHAGVIGVLKAWTKYSDGRSK-LFITAPPQFEFWLLEYSRIDYLPLSNIVFISNSALRTDRKPSALESSR-LSSLFKEFD 656
Cdd:cd07718  70 HHLGLIRLLAERKKLFKPPSPpLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDlLSNLLEELG 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19113935 657 LVSFRTVPAIHCPYSYCMEITNSSGWKIAYSGDTRPSEDFANIAKDSTLLIHEAT 711
Cdd:cd07718 150 LKSIETVPVIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 16-73 7.45e-22

tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related structurally to the Lactamase_B family members. tRNase Z is the endonuclease that is involved in tRNA 3'-end maturation through removal of the 3'-trailer sequences from tRNA precursors. The fission yeast Schizosaccharomyces pombe contains two candidate tRNase Zs encoded by two essential genes. The first, Swiss:Q10155, is targeted to the nucleus and has an SV40 nuclear localization signal at its N-terminus, consisting of four consecutive arginine and lysine residues between residues 208 and 211 (KKRK) that is critical for the NLS function. The second, Swiss:P87168, is targeted to the mitochondria, with an N-terminal mitochondrial targeting signal within the first 38 residues.


:

Pssm-ID: 404562 [Multi-domain]  Cd Length: 63  Bit Score: 89.57  E-value: 7.45e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19113935    16 QFVSVSSRDTScIPCIHLFFDSKRYVFGSVGEGCQRAILSQQLRLSKIKDVFLMQGSS 73
Cdd:pfam13691   1 QVVTTPTADTP-GPLLLLHFDSKRYLFGNVGEGTQRALNEQKVRLSKLEDIFLTGKVS 57
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 266-328 1.42e-12

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: 68.67  E-value: 1.42e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113935  266 FISYIVQSHPTPGKFDAAKAKSLGITKGLDCGRLARGEPVTLENGKTVYPKEVIGPSIPGSSF 328
Cdd:PRK00055 107 SLGYRIAEKDKPGKLDAEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPPRKGRKV 169
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 681-752 1.31e-07

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


The actual alignment was detected with superfamily member PRK02126:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 334  Bit Score: 54.15  E-value: 1.31e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113935  681 GWKIAYSGDTRPSEDFAN----IAKDSTLLIHEATLEDSMHEIAIKKQHSTYSEALEVAKKAGTKNVILTHFSQRY 752
Cdd:PRK02126 242 GQKIGYVTDIGYTEENLAriveLAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRY 317
 
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 ...
 500-711 1.45e-92

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: 288.68  E-value: 1.45e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 500 ICTLGTGSAMPSLYRNVSSTYVRIPvdkkcmedsaiSMKNILLDCGEGTLGRLSRQYGDNLKYEI-ASLRWIYISHMHAD 578
Cdd:cd07718   1 VVFLGTGSAIPSKYRNVSGILLRIP-----------GDGSILLDCGEGTLGQLRRHYGPEEADEVlRNLKCIFISHLHAD 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 579 HHAGVIGVLKAWTKYSDGRSK-LFITAPPQFEFWLLEYSRIDYLPLSNIVFISNSALRTDRKPSALESSR-LSSLFKEFD 656
Cdd:cd07718  70 HHLGLIRLLAERKKLFKPPSPpLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDlLSNLLEELG 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19113935 657 LVSFRTVPAIHCPYSYCMEITNSSGWKIAYSGDTRPSEDFANIAKDSTLLIHEAT 711
Cdd:cd07718 150 LKSIETVPVIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
498-778 7.39e-55

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 189.64  E-value: 7.39e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 498 IQICTLGTGSAMPSLYRNVSSTYVRIpvdkkcmEDsaismKNILLDCGEGTLGRLSRqygdnLKYEIASLRWIYISHMHA 577
Cdd:COG1234   1 MKLTFLGTGGAVPTPGRATSSYLLEA-------GG-----ERLLIDCGEGTQRQLLR-----AGLDPRDIDAIFITHLHG 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 578 DHHAGVIGVLKAWTkYSDGRSKLFITAPPQFEFWLLEYSRIDYLPLS-NIVFIsnsALRTDRKpsalessrlsslfKEFD 656
Cdd:COG1234  64 DHIAGLPGLLSTRS-LAGREKPLTIYGPPGTKEFLEALLKASGTDLDfPLEFH---EIEPGEV-------------FEIG 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 657 LVSFRTVPAIHCPYSYCMEITnSSGWKIAYSGDTRPSEDFANIAKDSTLLIHEATLEDSMHEIAIKKQHSTYSEALEVAK 736
Cdd:COG1234 127 GFTVTAFPLDHPVPAYGYRFE-EPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAA 205

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 19113935 737 KAGTKNVILTHFSQRYPKLPDI--DISTE-DLHIALAFDGMTLKI 778
Cdd:COG1234 206 EAGVKRLVLTHFSPRYDDPEELlaEARAVfPGPVELAEDGMVIEL 250
PRK00055 PRK00055
ribonuclease Z; Reviewed
 498-778 2.69e-43

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 158.03  E-value: 2.69e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935  498 IQICTLGTGSAMPSLYRNVSSTYVRIPVDKkcmedsaismknILLDCGEGTLGRLSRQygdNLKyeIASLRWIYISHMHA 577
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGGEL------------FLFDCGEGTQRQLLKT---GIK--PRKIDKIFITHLHG 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935  578 DHHAGVIGVLKawTKYSDGRSK-LFITAPPqfefwlleySRIDYLPLSNIVFISNS-ALRTDRKPSALESSRLSSL---- 651
Cdd:PRK00055  65 DHIFGLPGLLS--TRSLSGRTEpLTIYGPK---------GIKEFVETLLRASGSLGyRIAEKDKPGKLDAEKLKALgvpp 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935  652 ---------FKEFDLVSFRTVPaihcPYSYCMEITnsSGWKIAYSGDTRPSEDFANIAKDSTLLIHEATLEDSMHEIAIK 722
Cdd:PRK00055 134 gplfgklkrGEDVTLEDGRIIN----PADVLGPPR--KGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEELAKE 207

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19113935  723 KQHSTYSEALEVAKKAGTKNVILTHFSQRYPKLPDI---DISTEDLHIALAFDGMTLKI 778
Cdd:PRK00055 208 YGHSTARQAAEIAKEAGVKRLILTHFSPRYTGDPEEllkEAREIFPNTELAEDLMRVEV 266
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 500-778 1.93e-41

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: 153.53  E-value: 1.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935   500 ICTLGTGSAMPSLYRNVSSTYVRIPvdkkcmedsaisMKNILLDCGEGTLGRLsrqygdnLKYEIA--SLRWIYISHMHA 577
Cdd:TIGR02651   2 ITFLGTGGGVPTKERNLPSIALKLN------------GELWLFDCGEGTQRQM-------LRSGISpmKIDRIFITHLHG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935   578 DHHAGVIGVLKAWtKYSDGRSKLFITAPP---QFEFWLLE--YSRIDY------LPLSNIVFISNS----ALRTD-RKPS 641
Cdd:TIGR02651  63 DHILGLPGLLSTM-SFQGRKEPLTIYGPPgikEFIETSLRvsYTYLNYpikiheIEEGGLVFEDDGfkveAFPLDhSIPS 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935   642 alessrLSSLFKEFDLVSF---RTVPAIHCPYSYCM--------------EITNSS--------GWKIAYSGDTRPSEDF 696
Cdd:TIGR02651 142 ------LGYRFEEKDRPGKfdrEKAKELGIPPGPLYgklkrgetvtlidgRIIDPEdvlgpprkGRKIAYTGDTRPCEEV 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935   697 ANIAKDSTLLIHEATLEDSMHEIAIKKQHSTYSEALEVAKKAGTKNVILTHFSQRYPKLPDIDISTEDL--HIALAFDGM 774
Cdd:TIGR02651 216 IEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDEEELLEEAKKIfpNTYIAEDFM 295


                  ....
gi 19113935   775 TLKI 778
Cdd:TIGR02651 296 EIEI 299
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 16-73 7.45e-22

tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related structurally to the Lactamase_B family members. tRNase Z is the endonuclease that is involved in tRNA 3'-end maturation through removal of the 3'-trailer sequences from tRNA precursors. The fission yeast Schizosaccharomyces pombe contains two candidate tRNase Zs encoded by two essential genes. The first, Swiss:Q10155, is targeted to the nucleus and has an SV40 nuclear localization signal at its N-terminus, consisting of four consecutive arginine and lysine residues between residues 208 and 211 (KKRK) that is critical for the NLS function. The second, Swiss:P87168, is targeted to the mitochondria, with an N-terminal mitochondrial targeting signal within the first 38 residues.


Pssm-ID: 404562 [Multi-domain]  Cd Length: 63  Bit Score: 89.57  E-value: 7.45e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19113935    16 QFVSVSSRDTScIPCIHLFFDSKRYVFGSVGEGCQRAILSQQLRLSKIKDVFLMQGSS 73
Cdd:pfam13691   1 QVVTTPTADTP-GPLLLLHFDSKRYLFGNVGEGTQRALNEQKVRLSKLEDIFLTGKVS 57
PRK00055 PRK00055
ribonuclease Z; Reviewed
 266-328 1.42e-12

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 68.67  E-value: 1.42e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113935  266 FISYIVQSHPTPGKFDAAKAKSLGITKGLDCGRLARGEPVTLENGKTVYPKEVIGPSIPGSSF 328
Cdd:PRK00055 107 SLGYRIAEKDKPGKLDAEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPPRKGRKV 169
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 539-748 1.18e-07

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: 52.70  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935   539 NILLDCGEGTLGRLSRQYgDNLKYEIASLRWIYISHMHADHHAGVIGVLKAWTKysdgrsKLFITAPPqfefwlleysrI 618
Cdd:pfam12706   2 RILIDPGPDLRQQALPAL-QPGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPR------PLYAPLGV-----------L 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935   619 DYLPLSNIVFISNSALRTDRKPSALESS-RLSSLfkefdLVSFRTVPAIH-CPYSYCMEITNSSGW-------KIAYSGD 689
Cdd:pfam12706  64 AHLRRNFPYLFLLEHYGVRVHEIDWGESfTVGDG-----GLTVTATPARHgSPRGLDPNPGDTLGFriegpgkRVYYAGD 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113935   690 TRP-SEDFANIAKDSTLLIHEATL--EDSMHEIaikkQHSTYSEALEVAKKAGTKNVILTHF 748
Cdd:pfam12706 139 TGYfPDEIGERLGGADLLLLDGGAwrDDEMIHM----GHMTPEEAVEAAADLGARRKVLIHI 196
PRK02126 PRK02126
ribonuclease Z; Provisional
 681-752 1.31e-07

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 54.15  E-value: 1.31e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113935  681 GWKIAYSGDTRPSEDFAN----IAKDSTLLIHEATLEDSMHEIAIKKQHSTYSEALEVAKKAGTKNVILTHFSQRY 752
Cdd:PRK02126 242 GQKIGYVTDIGYTEENLAriveLAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRY 317
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 263-333 2.92e-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: 42.25  E-value: 2.92e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113935 263 PELFISYIVQSHPTPGKFDAAKAKSLGITKGLDC-----GRLARGEPVTLEnGKTVYPKEVIGPSIPGSSFFIIHC 333
Cdd:cd16296 101 PSLVVAFICKLHLKKGNFLVLKAKELGLPVGTAAiapiiAAVKDGKSITFE-GREILAEELCTPPDPGIVFIVVEC 175
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 538-590 4.45e-04

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: 41.77  E-value: 4.45e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 19113935    538 KNILLDCGEGTLGRLSRQYgdnLKYEIASLRWIYISHMHADHHAGVIGVLKAW 590
Cdd:smart00849  10 GAILIDTGPGEAEDLLAEL---KKLGPKKIDAIILTHGHPDHIGGLPELLEAP 59
 
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 ...
 500-711 1.45e-92

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: 288.68  E-value: 1.45e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 500 ICTLGTGSAMPSLYRNVSSTYVRIPvdkkcmedsaiSMKNILLDCGEGTLGRLSRQYGDNLKYEI-ASLRWIYISHMHAD 578
Cdd:cd07718   1 VVFLGTGSAIPSKYRNVSGILLRIP-----------GDGSILLDCGEGTLGQLRRHYGPEEADEVlRNLKCIFISHLHAD 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 579 HHAGVIGVLKAWTKYSDGRSK-LFITAPPQFEFWLLEYSRIDYLPLSNIVFISNSALRTDRKPSALESSR-LSSLFKEFD 656
Cdd:cd07718  70 HHLGLIRLLAERKKLFKPPSPpLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDlLSNLLEELG 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19113935 657 LVSFRTVPAIHCPYSYCMEITNSSGWKIAYSGDTRPSEDFANIAKDSTLLIHEAT 711
Cdd:cd07718 150 LKSIETVPVIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
498-778 7.39e-55

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 189.64  E-value: 7.39e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 498 IQICTLGTGSAMPSLYRNVSSTYVRIpvdkkcmEDsaismKNILLDCGEGTLGRLSRqygdnLKYEIASLRWIYISHMHA 577
Cdd:COG1234   1 MKLTFLGTGGAVPTPGRATSSYLLEA-------GG-----ERLLIDCGEGTQRQLLR-----AGLDPRDIDAIFITHLHG 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 578 DHHAGVIGVLKAWTkYSDGRSKLFITAPPQFEFWLLEYSRIDYLPLS-NIVFIsnsALRTDRKpsalessrlsslfKEFD 656
Cdd:COG1234  64 DHIAGLPGLLSTRS-LAGREKPLTIYGPPGTKEFLEALLKASGTDLDfPLEFH---EIEPGEV-------------FEIG 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 657 LVSFRTVPAIHCPYSYCMEITnSSGWKIAYSGDTRPSEDFANIAKDSTLLIHEATLEDSMHEIAIKKQHSTYSEALEVAK 736
Cdd:COG1234 127 GFTVTAFPLDHPVPAYGYRFE-EPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAA 205

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 19113935 737 KAGTKNVILTHFSQRYPKLPDI--DISTE-DLHIALAFDGMTLKI 778
Cdd:COG1234 206 EAGVKRLVLTHFSPRYDDPEELlaEARAVfPGPVELAEDGMVIEL 250
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 500-776 2.73e-52

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: 182.26  E-value: 2.73e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 500 ICTLGTGSAMPSLYRNVSSTYVRIPvdkkcmedsaisMKNILLDCGEGTLGRLSRQygdNLKyeIASLRWIYISHMHADH 579
Cdd:cd07717   1 LTFLGTGSAVPTPERNLSSIALRLE------------GELWLFDCGEGTQRQLLRA---GLS--PSKIDRIFITHLHGDH 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 580 HAGVIGVLKawTKYSDGRSK-LFITAPPQFEFWLLEYSRIDYLPLS-NIVFIsnsalrtdrkpsalESSRLSSLFKEFDL 657
Cdd:cd07717  64 ILGLPGLLS--TMSLLGRTEpLTIYGPKGLKEFLETLLRLSASRLPyPIEVH--------------ELEPDPGLVFEDDG 127

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 658 VSFRTVPAIH---CpYSYCMEItnssGWKIAYSGDTRPSEDFANIAKDSTLLIHEATLEDSMHEIAIKKQHSTYSEALEV 734
Cdd:cd07717 128 FTVTAFPLDHrvpC-FGYRFEE----GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKAKETGHSTAKQAAEI 202

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 19113935 735 AKKAGTKNVILTHFSQRYPKLPDI--DISTEDLHIALAFDGMTL 776
Cdd:cd07717 203 AKKAGVKKLVLTHFSARYKDPEELlkEARAVFPNTILAEDFMTI 246
PRK00055 PRK00055
ribonuclease Z; Reviewed
 498-778 2.69e-43

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 158.03  E-value: 2.69e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935  498 IQICTLGTGSAMPSLYRNVSSTYVRIPVDKkcmedsaismknILLDCGEGTLGRLSRQygdNLKyeIASLRWIYISHMHA 577
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGGEL------------FLFDCGEGTQRQLLKT---GIK--PRKIDKIFITHLHG 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935  578 DHHAGVIGVLKawTKYSDGRSK-LFITAPPqfefwlleySRIDYLPLSNIVFISNS-ALRTDRKPSALESSRLSSL---- 651
Cdd:PRK00055  65 DHIFGLPGLLS--TRSLSGRTEpLTIYGPK---------GIKEFVETLLRASGSLGyRIAEKDKPGKLDAEKLKALgvpp 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935  652 ---------FKEFDLVSFRTVPaihcPYSYCMEITnsSGWKIAYSGDTRPSEDFANIAKDSTLLIHEATLEDSMHEIAIK 722
Cdd:PRK00055 134 gplfgklkrGEDVTLEDGRIIN----PADVLGPPR--KGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEELAKE 207

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19113935  723 KQHSTYSEALEVAKKAGTKNVILTHFSQRYPKLPDI---DISTEDLHIALAFDGMTLKI 778
Cdd:PRK00055 208 YGHSTARQAAEIAKEAGVKRLILTHFSPRYTGDPEEllkEAREIFPNTELAEDLMRVEV 266
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 500-778 1.93e-41

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: 153.53  E-value: 1.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935   500 ICTLGTGSAMPSLYRNVSSTYVRIPvdkkcmedsaisMKNILLDCGEGTLGRLsrqygdnLKYEIA--SLRWIYISHMHA 577
Cdd:TIGR02651   2 ITFLGTGGGVPTKERNLPSIALKLN------------GELWLFDCGEGTQRQM-------LRSGISpmKIDRIFITHLHG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935   578 DHHAGVIGVLKAWtKYSDGRSKLFITAPP---QFEFWLLE--YSRIDY------LPLSNIVFISNS----ALRTD-RKPS 641
Cdd:TIGR02651  63 DHILGLPGLLSTM-SFQGRKEPLTIYGPPgikEFIETSLRvsYTYLNYpikiheIEEGGLVFEDDGfkveAFPLDhSIPS 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935   642 alessrLSSLFKEFDLVSF---RTVPAIHCPYSYCM--------------EITNSS--------GWKIAYSGDTRPSEDF 696
Cdd:TIGR02651 142 ------LGYRFEEKDRPGKfdrEKAKELGIPPGPLYgklkrgetvtlidgRIIDPEdvlgpprkGRKIAYTGDTRPCEEV 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935   697 ANIAKDSTLLIHEATLEDSMHEIAIKKQHSTYSEALEVAKKAGTKNVILTHFSQRYPKLPDIDISTEDL--HIALAFDGM 774
Cdd:TIGR02651 216 IEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDEEELLEEAKKIfpNTYIAEDFM 295


                  ....
gi 19113935   775 TLKI 778
Cdd:TIGR02651 296 EIEI 299
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 503-710 4.10e-30

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: 117.36  E-value: 4.10e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 503 LGTGSAMPSLYRNVSSTYVRIPvdkkcmedsaisMKNILLDCGEGTLGRLSRQYGDNLKyeiasLRWIYISHMHADHHAG 582
Cdd:cd16272   4 LGTGGAVPSLTRNTSSYLLETG------------GTRILLDCGEGTVYRLLKAGVDPDK-----LDAIFLSHFHLDHIGG 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 583 VIGVLKAWtKYSDGRSKLFITAPPQFEfWLLEYsridylplsnivfISNSALRTDRKPSALESSRLSSLFKEFDLVSF-- 660
Cdd:cd16272  67 LPTLLFAR-RYGGRKKPLTIYGPKGIK-EFLEK-------------LLNFPVEILPLGFPLEIEELEEGGEVLELGDLkv 131

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 19113935 661 RTVPAIHCPYSYcMEITNSSGWKIAYSGDTRPSEDFANIAKDSTLLIHEA 710
Cdd:cd16272 132 EAFPVKHSVESL-GYRIEAEGKSIVYSGDTGPCENLVELAKGADLLIHEC 180
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 16-73 7.45e-22

tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related structurally to the Lactamase_B family members. tRNase Z is the endonuclease that is involved in tRNA 3'-end maturation through removal of the 3'-trailer sequences from tRNA precursors. The fission yeast Schizosaccharomyces pombe contains two candidate tRNase Zs encoded by two essential genes. The first, Swiss:Q10155, is targeted to the nucleus and has an SV40 nuclear localization signal at its N-terminus, consisting of four consecutive arginine and lysine residues between residues 208 and 211 (KKRK) that is critical for the NLS function. The second, Swiss:P87168, is targeted to the mitochondria, with an N-terminal mitochondrial targeting signal within the first 38 residues.


Pssm-ID: 404562 [Multi-domain]  Cd Length: 63  Bit Score: 89.57  E-value: 7.45e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19113935    16 QFVSVSSRDTScIPCIHLFFDSKRYVFGSVGEGCQRAILSQQLRLSKIKDVFLMQGSS 73
Cdd:pfam13691   1 QVVTTPTADTP-GPLLLLHFDSKRYLFGNVGEGTQRALNEQKVRLSKLEDIFLTGKVS 57
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 499-778 1.87e-20

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 91.88  E-value: 1.87e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 499 QICTLGTGS----------------AMPSLYRNVSSTYVRipVDKKcmedsaismkNILLDCGEGTlgrlsRQYGDNLKY 562
Cdd:COG1235   2 KVTFLGSGSsggvpqigcdcpvcasTDPRYGRTRSSILVE--ADGT----------RLLIDAGPDL-----REQLLRLGL 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 563 EIASLRWIYISHMHADHHAGvIGVLKAwtKYSDGRSKLFITAPPqFEFWLLEYSRIDYLPLSNIVFisnsalrtdrkpsa 642
Cdd:COG1235  65 DPSKIDAILLTHEHADHIAG-LDDLRP--RYGPNPIPVYATPGT-LEALERRFPYLFAPYPGKLEF-------------- 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 643 lessRLSSLFKEFDL--VSFRTVPAIH---CPYSYCMEitnSSGWKIAYSGDT-RPSEDFANIAKDSTLLIHEATLEDSM 716
Cdd:COG1235 127 ----HEIEPGEPFEIggLTVTPFPVPHdagDPVGYRIE---DGGKKLAYATDTgYIPEEVLELLRGADLLILDATYDDPE 199

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113935 717 HEiaikkqHSTYSEALEVAKKAGTKNVILTHFSQRY--PKLPDIDISTEDL--HIALAFDGMTLKI 778
Cdd:COG1235 200 PG------HLSNEEALELLARLGPKRLVLTHLSPDNndHELDYDELEAALLpaGVEVAYDGMEIEL 259
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 539-710 4.76e-16

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: 76.71  E-value: 4.76e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 539 NILLDCGEGTLGRLsRQYGDnlkyeIASLRWIYISHMHADHHA--GVIGVLKAWTKYSDGRSKLFITAPPQFEFWLleyS 616
Cdd:cd07716  29 RILLDCGSGVLSRL-QRYID-----PEDLDAVVLSHLHPDHCAdlGVLQYARRYHPRGARKPPLPLYGPAGPAERL---A 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 617 RIDYLPlsnivfiSNSALRTDRKPSALEssrlsslFKEFDLVSFRTVpaiHCPYSYCMEITNSSGwKIAYSGDTRPSEDF 696
Cdd:cd07716 100 ALYGLE-------DVFDFHPIEPGEPLE-------IGPFTITFFRTV---HPVPCYAMRIEDGGK-VLVYTGDTGYCDEL 161

                       170
                ....*....|....
gi 19113935 697 ANIAKDSTLLIHEA 710
Cdd:cd07716 162 VEFARGADLLLCEA 175
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 502-708 1.06e-15

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: 76.02  E-value: 1.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 502 TLGTGSAMPSLYRNVSSTYVRipVDKKcmedsaismkNILLDCGEGTLGRLSRqygdnLKYEIASLRWIYISHMHADHHA 581
Cdd:cd07719   4 LLGTGGPIPDPDRAGPSTLVV--VGGR----------VYLVDAGSGVVRRLAQ-----AGLPLGDLDAVFLTHLHSDHVA 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 582 GVIGVLK-AWTkySDGRSKLFITAPPQFEFWlleysrIDYLPLSNIVFISNSALRTDRKPSALESS------RLSSLFKE 654
Cdd:cd07719  67 DLPALLLtAWL--AGRKTPLPVYGPPGTRAL------VDGLLAAYALDIDYRARIGDEGRPDPGALvevheiAAGGVVYE 138

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 19113935 655 FDLVSFRTVPAIHCP----YSYCMEITNSSgwkIAYSGDTRPSEDFANIAKDSTLLIH 708
Cdd:cd07719 139 DDGVKVTAFLVDHGPvppaLAYRFDTPGRS---VVFSGDTGPSENLIELAKGADLLVH 193
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 503-710 6.80e-13

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: 68.05  E-value: 6.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 503 LGTGSAMPSLYRNVSSTYVripvdkkcmedsAISMKNILLDCGEGTLGRLSRqYGDNLkyeiASLRWIYISHMHADHHAG 582
Cdd:cd07740   3 LGSGDAFGSGGRLNTCFHV------------ASEAGRFLIDCGASSLIALKR-AGIDP----NAIDAIFITHLHGDHFGG 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 583 VIG-VLKAWTKYsdGRSK-LFITAPPQFEFWLLEysridylplsnivfisnsALRTDRKPSALESSRLSSLFKEF----- 655
Cdd:cd07740  66 LPFfLLDAQFVA--KRTRpLTIAGPPGLRERLRR------------------AMEALFPGSSKVPRRFDLEVIELepgep 125

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113935 656 ---DLVSFRTVPAIH---CPySYCMEITNsSGWKIAYSGDTRPSEDFANIAKDSTLLIHEA 710
Cdd:cd07740 126 ttlGGVTVTAFPVVHpsgAL-PLALRLEA-AGRVLAYSGDTEWTDALVPLARGADLFICEC 184
PRK00055 PRK00055
ribonuclease Z; Reviewed
 266-328 1.42e-12

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 68.67  E-value: 1.42e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113935  266 FISYIVQSHPTPGKFDAAKAKSLGITKGLDCGRLARGEPVTLENGKTVYPKEVIGPSIPGSSF 328
Cdd:PRK00055 107 SLGYRIAEKDKPGKLDAEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPPRKGRKV 169
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 538-747 4.95e-10

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: 60.28  E-value: 4.95e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 538 KNILLDCGEGTLGRLSRqygdnLKYEIASLRWIYISHMHADHHAGVIGVLKAWTKYsdGRSKLFITAPPqfEFWLLEYSR 617
Cdd:cd07741  30 KNIHIDPGPGALVRMCR-----PKLDPTKLDAIILSHRHLDHSNDANVLIEAMTEG--GFKKRGTLLAP--EDALNGEPV 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 618 IDYLPLSNIvfisnsalrtdrkpsaLESSRLSSLFKEFDL--VSFRTVPAIH-CPYSYCMEITNSSGwKIAYSGDTRPSE 694
Cdd:cd07741 101 VLLYYHRRK----------------LEEIEILEEGDEYELggIKIEATRHKHsDPTTYGFIFRTSDK-KIGYISDTRYFE 163

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 19113935 695 DFANIAKDSTLLIHEATLEDSMHeiaiKKQHSTYSEALEVAKKAGTKNVILTH 747
Cdd:cd07741 164 ELIEYYSNCDVLIINVTRPRPRK----GVDHLSVEDVEKILKEIKPKLAILTH 212
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 539-748 1.18e-07

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: 52.70  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935   539 NILLDCGEGTLGRLSRQYgDNLKYEIASLRWIYISHMHADHHAGVIGVLKAWTKysdgrsKLFITAPPqfefwlleysrI 618
Cdd:pfam12706   2 RILIDPGPDLRQQALPAL-QPGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPR------PLYAPLGV-----------L 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935   619 DYLPLSNIVFISNSALRTDRKPSALESS-RLSSLfkefdLVSFRTVPAIH-CPYSYCMEITNSSGW-------KIAYSGD 689
Cdd:pfam12706  64 AHLRRNFPYLFLLEHYGVRVHEIDWGESfTVGDG-----GLTVTATPARHgSPRGLDPNPGDTLGFriegpgkRVYYAGD 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113935   690 TRP-SEDFANIAKDSTLLIHEATL--EDSMHEIaikkQHSTYSEALEVAKKAGTKNVILTHF 748
Cdd:pfam12706 139 TGYfPDEIGERLGGADLLLLDGGAwrDDEMIHM----GHMTPEEAVEAAADLGARRKVLIHI 196
PRK02126 PRK02126
ribonuclease Z; Provisional
 681-752 1.31e-07

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 54.15  E-value: 1.31e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113935  681 GWKIAYSGDTRPSEDFAN----IAKDSTLLIHEATLEDSMHEIAIKKQHSTYSEALEVAKKAGTKNVILTHFSQRY 752
Cdd:PRK02126 242 GQKIGYVTDIGYTEENLAriveLAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRY 317
PRK14866 PRK14866
hypothetical protein; Provisional
 279-318 1.11e-04

hypothetical protein; Provisional


Pssm-ID: 237840  Cd Length: 451  Bit Score: 45.38  E-value: 1.11e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 19113935  279 KFDAAKAKSLGITKGLDCGRLARGEPVTLEnGKTVYPKEV 318
Cdd:PRK14866 397 RFDPELARKLGVPEGPAFGKLAAGQPVEVD-GETITPEMV 435
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
538-747 1.62e-04

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 43.51  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935   538 KNILLDCGEGTLGRLSRQYGDnLKYEIASLRWIYISHMHADHHAGVIGVLKAWTKYSDGRSKLfitAPPQFEFWLLEYSR 617
Cdd:pfam00753  16 GAVLIDTGGSAEAALLLLLAA-LGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEE---ARELLDEELGLAAS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935   618 IDYLPLSNIVFISNSALRTDRkpsalessrlsslfkEFDLVSFRTVPAIHCP--YSYCMEITNSSGwKIAYSGDTRPSED 695
Cdd:pfam00753  92 RLGLPGPPVVPLPPDVVLEEG---------------DGILGGGLGLLVTHGPghGPGHVVVYYGGG-KVLFTGDLLFAGE 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 19113935   696 FANIAKDSTLliheatLEDSMHEIaikkqHSTYSEALEVAKKAGTKNVILTH 747
Cdd:pfam00753 156 IGRLDLPLGG------LLVLHPSS-----AESSLESLLKLAKLKAAVIVPGH 196
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 263-333 2.92e-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: 42.25  E-value: 2.92e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113935 263 PELFISYIVQSHPTPGKFDAAKAKSLGITKGLDC-----GRLARGEPVTLEnGKTVYPKEVIGPSIPGSSFFIIHC 333
Cdd:cd16296 101 PSLVVAFICKLHLKKGNFLVLKAKELGLPVGTAAiapiiAAVKDGKSITFE-GREILAEELCTPPDPGIVFIVVEC 175
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 538-590 4.45e-04

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: 41.77  E-value: 4.45e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 19113935    538 KNILLDCGEGTLGRLSRQYgdnLKYEIASLRWIYISHMHADHHAGVIGVLKAW 590
Cdd:smart00849  10 GAILIDTGPGEAEDLLAEL---KKLGPKKIDAIILTHGHPDHIGGLPELLEAP 59
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 540-589 6.08e-04

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: 41.75  E-value: 6.08e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19113935 540 ILLDCGEGtlgrlSRQYGDNLK-----YEIASLRWIYISHMHADHHAGVIGVLKA 589
Cdd:cd07722  30 ILIDTGEG-----RPSYIPLLKsvldsEGNATISDILLTHWHHDHVGGLPDVLDL 79
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 538-612 2.84e-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: 40.22  E-value: 2.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 538 KNILLDCGEG-----TLGRLsrqyGDNLK---YEIASLRWIYISHMHADHHAGVIGvlkawtkysDGRSKLF-----ITA 604
Cdd:cd07720  59 RLILVDTGAGglfgpTAGKL----LANLAaagIDPEDIDDVLLTHLHPDHIGGLVD---------AGGKPVFpnaevHVS 125


                ....*...
gi 19113935 605 PPQFEFWL 612
Cdd:cd07720 126 EAEWDFWL 133
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 569-695 4.47e-03

Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase domain; Includes Dictyostelium discoideum cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A (also known as cyclic GMP-binding protein A, phosphodiesterase 5, phosphodiesterase D, and PDE5) and cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B (also known as cyclic GMP-binding protein B, phosphodiesterase 6, phosphodiesterase E, and PDE6. 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: 293824  Cd Length: 189  Bit Score: 39.20  E-value: 4.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113935 569 WIYISHMHADHHAGVIGVLkawtkYSDGRSKLfITAPPQFEFWLLEYSRIDYLPLSnivFISNsaLRTDRKPSALESSRL 648
Cdd:cd07738  51 HVILTHCHADHDAGTFQKI-----LEEEKITL-YTTRTINESFLRKYAALTGLPPD---FLEE--LFDFRPVIIGEKTKI 119

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 19113935 649 SSLFKEFDLvSFRTVPAIHCPYSYCmeitnssGWKIAYSGDTRPSED 695
Cdd:cd07738 120 NGAEFEFDY-SFHSIPTIRFKVSYG-------GKSIAYSGDTRYDPD 158
 
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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