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Conserved domains on  [gi|1370471831|ref|XP_024306629|]
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zinc phosphodiesterase ELAC protein 2 isoform X1 [Homo sapiens]

Protein Classification

ribonuclease Z family protein( domain architecture ID 11039737)

ribonuclease Z family protein such as the tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase), which 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;

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 ...
 389-594 2.42e-103

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: 314.87  E-value: 2.42e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 389 IIFLGTGSAIPMKIRNVSATLVNISPDTSLLLDCGEGTFGQLCRHYGDQ-VDRVLGTLAAVFVSHLHADHHTGLPSILLQ 467
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 468 RERALAslgKPLHPLLVVAPNQLKAWLQQYHNQCQEVLHHISMIPAKCLQEGAEISSPAVERLISSLLRTCDLEEFQTCL 547
Cdd:cd07718    81 RKKLFK---PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKSIETVP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1370471831 548 VRHCKHAFGCALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEAT 594
Cdd:cd07718   158 VIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 1-217 7.76e-78

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 cd16296:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 175  Bit Score: 247.18  E-value: 7.76e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831   1 MQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLSGPpqlekyleaikifsgplkgielavrphsapeye 80
Cdd:cd16296    36 MQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLSGP--------------------------------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831  81 detmtvyqipihseqrrgkhqpwqsperplsrlsperssdsesnENEPHLPHGVSQRRGVRDSSLVVAFICKLHLKRGNF 160
Cdd:cd16296    83 --------------------------------------------NKQSPDKIGVRRQILERDPSLVVAFICKLHLKKGNF 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370471831 161 LVLKAKEMGLPVGTAAIAPIIAAVKDGKSITHEGREILAEELCTPPDPGAAFVVVEC 217
Cdd:cd16296   119 LVLKAKELGLPVGTAAIAPIIAAVKDGKSITFEGREILAEELCTPPDPGIVFIVVEC 175
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 562-636 3.99e-04

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: 43.37  E-value: 3.99e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370471831 562 TSGWKVVYSGDTMP----CEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRYA 636
Cdd:PRK02126  240 EPGQKIGYVTDIGYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQ 318
 
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 ...
 389-594 2.42e-103

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: 314.87  E-value: 2.42e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 389 IIFLGTGSAIPMKIRNVSATLVNISPDTSLLLDCGEGTFGQLCRHYGDQ-VDRVLGTLAAVFVSHLHADHHTGLPSILLQ 467
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 468 RERALAslgKPLHPLLVVAPNQLKAWLQQYHNQCQEVLHHISMIPAKCLQEGAEISSPAVERLISSLLRTCDLEEFQTCL 547
Cdd:cd07718    81 RKKLFK---PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKSIETVP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1370471831 548 VRHCKHAFGCALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEAT 594
Cdd:cd07718   158 VIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 1-217 7.76e-78

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: 247.18  E-value: 7.76e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831   1 MQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLSGPpqlekyleaikifsgplkgielavrphsapeye 80
Cdd:cd16296    36 MQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLSGP--------------------------------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831  81 detmtvyqipihseqrrgkhqpwqsperplsrlsperssdsesnENEPHLPHGVSQRRGVRDSSLVVAFICKLHLKRGNF 160
Cdd:cd16296    83 --------------------------------------------NKQSPDKIGVRRQILERDPSLVVAFICKLHLKKGNF 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370471831 161 LVLKAKEMGLPVGTAAIAPIIAAVKDGKSITHEGREILAEELCTPPDPGAAFVVVEC 217
Cdd:cd16296   119 LVLKAKELGLPVGTAAIAPIIAAVKDGKSITFEGREILAEELCTPPDPGIVFIVVEC 175
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
388-658 3.91e-50

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 175.77  E-value: 3.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 388 EIIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLCRHYGDqvdrvLGTLAAVFVSHLHADHHTGLPSILLQ 467
Cdd:COG1234     2 KLTFLGTGGAVPTPGRATSSYLLEA-GGERLLIDCGEGTQRQLLRAGLD-----PRDIDAIFITHLHGDHIAGLPGLLST 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 468 ReralaSLGKPLHPLLVVAPNQLKAWLQQYHNQCQEVLH-HISMIPakcLQEGAEIsspaverlissllrtcDLEEFQ-- 544
Cdd:COG1234    76 R-----SLAGREKPLTIYGPPGTKEFLEALLKASGTDLDfPLEFHE---IEPGEVF----------------EIGGFTvt 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 545 TCLVRHCKHAFGcALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAE 624
Cdd:COG1234   132 AFPLDHPVPAYG-YRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVK 210

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1370471831 625 FIMLNHFSQRYAKVPLF----SPNFSEKVGVAFDHMKV 658
Cdd:COG1234   211 RLVLTHFSPRYDDPEELlaeaRAVFPGPVELAEDGMVI 248
PRK00055 PRK00055
ribonuclease Z; Reviewed
 388-635 3.04e-40

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 148.79  E-value: 3.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 388 EIIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLcRHYG---DQVDRvlgtlaaVFVSHLHADHHTGLPSI 464
Cdd:PRK00055    3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQL-LKTGikpRKIDK-------IFITHLHGDHIFGLPGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 465 LLQReralaSLGKPLHPLLVVAPnqlkAWLQQYHNQCQEVLHHIS----------MIPAKCLQEGAEISSPAVERLISSl 534
Cdd:PRK00055   74 LSTR-----SLSGRTEPLTIYGP----KGIKEFVETLLRASGSLGyriaekdkpgKLDAEKLKALGVPPGPLFGKLKRG- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 535 lrtcdlEEFQTCLVRHCKHAFGCALVHTsGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQA 614
Cdd:PRK00055  144 ------EDVTLEDGRIINPADVLGPPRK-GRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEELAKEYGHSTARQA 216

                         250       260
                  ....*....|....*....|.
gi 1370471831 615 ISVGMRMNAEFIMLNHFSQRY 635
Cdd:PRK00055  217 AEIAKEAGVKRLILTHFSPRY 237
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 388-635 8.38e-33

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: 128.49  E-value: 8.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 388 EIIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLcRHYG---DQVDRVlgtlaavFVSHLHADHHTGLPSI 464
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-NGELWLFDCGEGTQRQM-LRSGispMKIDRI-------FITHLHGDHILGLPGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 465 LLQReralaSLGKPLHPLLVVAPNQLKAWLQqyhNQCQEVLHHISMIPakclqEGAEISSPAVERlissllrtcDLEEFQ 544
Cdd:TIGR02651  72 LSTM-----SFQGRKEPLTIYGPPGIKEFIE---TSLRVSYTYLNYPI-----KIHEIEEGGLVF---------EDDGFK 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 545 --TCLVRHCKHAFGCALV-------------------------------------------------HTSGWKVVYSGDT 573
Cdd:TIGR02651 130 veAFPLDHSIPSLGYRFEekdrpgkfdrekakelgippgplygklkrgetvtlidgriidpedvlgpPRKGRKIAYTGDT 209

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370471831 574 MPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRY 635
Cdd:TIGR02651 210 RPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY 271
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 418-631 3.04e-06

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: 48.46  E-value: 3.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 418 LLLDCGEGTFGQLcRHYGDQVDRVLGTLAAVFVSHLHADHHTGLPSIllqRERALASLGKPLHPLLVVAPN-QLKAWLQQ 496
Cdd:pfam12706   3 ILIDPGPDLRQQA-LPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDL---REGRPRPLYAPLGVLAHLRRNfPYLFLLEH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 497 YHNQCQEV-----------LHHISMIPAkclQEGAEISSPAVERLISSLlrtcdleefqtclvrhckhafgcaLVHTSGW 565
Cdd:pfam12706  79 YGVRVHEIdwgesftvgdgGLTVTATPA---RHGSPRGLDPNPGDTLGF------------------------RIEGPGK 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370471831 566 KVVYSGDTMPCEALV--RMGkDATLLIHEATLEDglEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHF 631
Cdd:pfam12706 132 RVYYAGDTGYFPDEIgeRLG-GADLLLLDGGAWR--DDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 406-597 1.01e-05

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 46.78  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831  406 SATLVnISPDTSLLLDCGEGT----FGQLCRHYGDQVDrvlgtlaAVFVSHLHADHHTGLPSILlqreralaslgkPLHP 481
Cdd:smart00849   1 NSYLV-RDDGGAILIDTGPGEaedlLAELKKLGPKKID-------AIILTHGHPDHIGGLPELL------------EAPG 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831  482 LLVVAPNQLKAWLQQYHNQCQEVLHHI-SMIPAKCLQEGAEIsspaverlissllrtcDLEEFQTCLVRHCKHAFGCALV 560
Cdd:smart00849  61 APVYAPEGTAELLKDLLALLGELGAEAePAPPDRTLKDGDEL----------------DLGGGELEVIHTPGHTPGSIVL 124

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1370471831  561 HTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLED 597
Cdd:smart00849 125 YLPEGKILFTGDLLFAGGDGRTLVDGGDAAASDALES 161
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 1-26 9.18e-05

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: 41.04  E-value: 9.18e-05
                          10        20
                  ....*....|....*....|....*..
gi 1370471831   1 MQEHKLKVARLDNIFLTRMH-WSNVGG 26
Cdd:pfam13691  37 LNEQKVRLSKLEDIFLTGKVsWSNIGG 63
PRK02126 PRK02126
ribonuclease Z; Provisional
 562-636 3.99e-04

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 43.37  E-value: 3.99e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370471831 562 TSGWKVVYSGDTMP----CEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRYA 636
Cdd:PRK02126  240 EPGQKIGYVTDIGYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQ 318
 
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 ...
 389-594 2.42e-103

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: 314.87  E-value: 2.42e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 389 IIFLGTGSAIPMKIRNVSATLVNISPDTSLLLDCGEGTFGQLCRHYGDQ-VDRVLGTLAAVFVSHLHADHHTGLPSILLQ 467
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 468 RERALAslgKPLHPLLVVAPNQLKAWLQQYHNQCQEVLHHISMIPAKCLQEGAEISSPAVERLISSLLRTCDLEEFQTCL 547
Cdd:cd07718    81 RKKLFK---PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKSIETVP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1370471831 548 VRHCKHAFGCALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEAT 594
Cdd:cd07718   158 VIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 1-217 7.76e-78

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: 247.18  E-value: 7.76e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831   1 MQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLSGPpqlekyleaikifsgplkgielavrphsapeye 80
Cdd:cd16296    36 MQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLSGP--------------------------------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831  81 detmtvyqipihseqrrgkhqpwqsperplsrlsperssdsesnENEPHLPHGVSQRRGVRDSSLVVAFICKLHLKRGNF 160
Cdd:cd16296    83 --------------------------------------------NKQSPDKIGVRRQILERDPSLVVAFICKLHLKKGNF 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370471831 161 LVLKAKEMGLPVGTAAIAPIIAAVKDGKSITHEGREILAEELCTPPDPGAAFVVVEC 217
Cdd:cd16296   119 LVLKAKELGLPVGTAAIAPIIAAVKDGKSITFEGREILAEELCTPPDPGIVFIVVEC 175
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
388-658 3.91e-50

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 175.77  E-value: 3.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 388 EIIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLCRHYGDqvdrvLGTLAAVFVSHLHADHHTGLPSILLQ 467
Cdd:COG1234     2 KLTFLGTGGAVPTPGRATSSYLLEA-GGERLLIDCGEGTQRQLLRAGLD-----PRDIDAIFITHLHGDHIAGLPGLLST 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 468 ReralaSLGKPLHPLLVVAPNQLKAWLQQYHNQCQEVLH-HISMIPakcLQEGAEIsspaverlissllrtcDLEEFQ-- 544
Cdd:COG1234    76 R-----SLAGREKPLTIYGPPGTKEFLEALLKASGTDLDfPLEFHE---IEPGEVF----------------EIGGFTvt 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 545 TCLVRHCKHAFGcALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAE 624
Cdd:COG1234   132 AFPLDHPVPAYG-YRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVK 210

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1370471831 625 FIMLNHFSQRYAKVPLF----SPNFSEKVGVAFDHMKV 658
Cdd:COG1234   211 RLVLTHFSPRYDDPEELlaeaRAVFPGPVELAEDGMVI 248
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 389-635 4.67e-48

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: 169.94  E-value: 4.67e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 389 IIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLcRHYGdqvdRVLGTLAAVFVSHLHADHHTGLPSiLLQR 468
Cdd:cd07717     1 LTFLGTGSAVPTPERNLSSIALRL-EGELWLFDCGEGTQRQL-LRAG----LSPSKIDRIFITHLHGDHILGLPG-LLST 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 469 eralASLGKPLHPLLVVAPNQLKAWLQQYHNQCQEVLhhismipakclqeGAEIsspAVERLISSLLRTCDLEEFQ--TC 546
Cdd:cd07717    74 ----MSLLGRTEPLTIYGPKGLKEFLETLLRLSASRL-------------PYPI---EVHELEPDPGLVFEDDGFTvtAF 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 547 LVRHCKHAFGCALvhTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFI 626
Cdd:cd07717   134 PLDHRVPCFGYRF--EEGRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKAKETGHSTAKQAAEIAKKAGVKKL 211


                  ....*....
gi 1370471831 627 MLNHFSQRY 635
Cdd:cd07717   212 VLTHFSARY 220
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 389-593 9.01e-44

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: 155.50  E-value: 9.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 389 IIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLCRHYGDqvdrvLGTLAAVFVSHLHADHHTGLPSILLQR 468
Cdd:cd16272     1 LTFLGTGGAVPSLTRNTSSYLLET-GGTRILLDCGEGTVYRLLKAGVD-----PDKLDAIFLSHFHLDHIGGLPTLLFAR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 469 EralasLGKPLHPLLVVAPNQLKAWLQQYHNQCQEVLHHISMIpakclqEGAEISSPAVERLISSLlrtcdleEFQTCLV 548
Cdd:cd16272    75 R-----YGGRKKPLTIYGPKGIKEFLEKLLNFPVEILPLGFPL------EIEELEEGGEVLELGDL-------KVEAFPV 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1370471831 549 RHCKHAFGCALVHTsGWKVVYSGDTMPCEALVRMGKDATLLIHEA 593
Cdd:cd16272   137 KHSVESLGYRIEAE-GKSIVYSGDTGPCENLVELAKGADLLIHEC 180
PRK00055 PRK00055
ribonuclease Z; Reviewed
 388-635 3.04e-40

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 148.79  E-value: 3.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 388 EIIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLcRHYG---DQVDRvlgtlaaVFVSHLHADHHTGLPSI 464
Cdd:PRK00055    3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQL-LKTGikpRKIDK-------IFITHLHGDHIFGLPGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 465 LLQReralaSLGKPLHPLLVVAPnqlkAWLQQYHNQCQEVLHHIS----------MIPAKCLQEGAEISSPAVERLISSl 534
Cdd:PRK00055   74 LSTR-----SLSGRTEPLTIYGP----KGIKEFVETLLRASGSLGyriaekdkpgKLDAEKLKALGVPPGPLFGKLKRG- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 535 lrtcdlEEFQTCLVRHCKHAFGCALVHTsGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQA 614
Cdd:PRK00055  144 ------EDVTLEDGRIINPADVLGPPRK-GRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEELAKEYGHSTARQA 216

                         250       260
                  ....*....|....*....|.
gi 1370471831 615 ISVGMRMNAEFIMLNHFSQRY 635
Cdd:PRK00055  217 AEIAKEAGVKRLILTHFSPRY 237
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 388-635 8.38e-33

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: 128.49  E-value: 8.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 388 EIIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLcRHYG---DQVDRVlgtlaavFVSHLHADHHTGLPSI 464
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-NGELWLFDCGEGTQRQM-LRSGispMKIDRI-------FITHLHGDHILGLPGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 465 LLQReralaSLGKPLHPLLVVAPNQLKAWLQqyhNQCQEVLHHISMIPakclqEGAEISSPAVERlissllrtcDLEEFQ 544
Cdd:TIGR02651  72 LSTM-----SFQGRKEPLTIYGPPGIKEFIE---TSLRVSYTYLNYPI-----KIHEIEEGGLVF---------EDDGFK 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 545 --TCLVRHCKHAFGCALV-------------------------------------------------HTSGWKVVYSGDT 573
Cdd:TIGR02651 130 veAFPLDHSIPSLGYRFEekdrpgkfdrekakelgippgplygklkrgetvtlidgriidpedvlgpPRKGRKIAYTGDT 209

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370471831 574 MPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRY 635
Cdd:TIGR02651 210 RPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY 271
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 388-591 3.75e-23

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: 97.59  E-value: 3.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 388 EIIFLGTGSAIPMKIRNVSATLVnISPDTSLLLDCGEGTFGQLCrhygdQVDRVLGTLAAVFVSHLHADHHTGLPSILLQ 467
Cdd:cd07719     1 RVTLLGTGGPIPDPDRAGPSTLV-VVGGRVYLVDAGSGVVRRLA-----QAGLPLGDLDAVFLTHLHSDHVADLPALLLT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 468 ReralaSLGKPLHPLLVVAPNQLKAW---LQQYHNQCQEVLHHISMIPAkcLQEGA-----EISSPAVerlissllrTCD 539
Cdd:cd07719    75 A-----WLAGRKTPLPVYGPPGTRALvdgLLAAYALDIDYRARIGDEGR--PDPGAlvevhEIAAGGV---------VYE 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370471831 540 LEEFQ--TCLVRH--CKHAFgcAL-VHTSGWKVVYSGDTMPCEALVRMGKDATLLIH 591
Cdd:cd07719   139 DDGVKvtAFLVDHgpVPPAL--AYrFDTPGRSVVFSGDTGPSENLIELAKGADLLVH 193
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 413-593 1.39e-20

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: 89.42  E-value: 1.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 413 SPDTSLLLDCGEGTFGQLCRHygdqVDrvLGTLAAVFVSHLHADHHTGLPSilLQRERALASLGKPLHPLLVVAPNQLKA 492
Cdd:cd07716    25 ADGFRILLDCGSGVLSRLQRY----ID--PEDLDAVVLSHLHPDHCADLGV--LQYARRYHPRGARKPPLPLYGPAGPAE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 493 WLQQ-YHNQCQEVLHHISmiPAKCLQEGaeisspaverlissllrtcDLeEFQTCLVRHCKHAFGCALVHtSGWKVVYSG 571
Cdd:cd07716    97 RLAAlYGLEDVFDFHPIE--PGEPLEIG-------------------PF-TITFFRTVHPVPCYAMRIED-GGKVLVYTG 153

                         170       180
                  ....*....|....*....|..
gi 1370471831 572 DTMPCEALVRMGKDATLLIHEA 593
Cdd:cd07716   154 DTGYCDELVEFARGADLLLCEA 175
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 390-593 2.21e-18

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: 83.85  E-value: 2.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 390 IFLGTGSAIPMKIRNVSATLVNiSPDTSLLLDCGEGTFGQLCRhYGdqVDRVlgTLAAVFVSHLHADHHTGLPSILL--- 466
Cdd:cd07740     1 TFLGSGDAFGSGGRLNTCFHVA-SEAGRFLIDCGASSLIALKR-AG--IDPN--AIDAIFITHLHGDHFGGLPFFLLdaq 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 467 ---QRERalaslgkplhPLLVVAPNQLKAWLQQyhnqCQEVLH-HISMIPAKclqegAEISSPAVERLISSLLRTCDLEE 542
Cdd:cd07740    75 fvaKRTR----------PLTIAGPPGLRERLRR----AMEALFpGSSKVPRR-----FDLEVIELEPGEPTTLGGVTVTA 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370471831 543 FQtclVRHCKHAFGCALVHTSGWKVV-YSGDTMPCEALVRMGKDATLLIHEA 593
Cdd:cd07740   136 FP---VVHPSGALPLALRLEAAGRVLaYSGDTEWTDALVPLARGADLFICEC 184
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 388-658 2.50e-16

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 79.55  E-value: 2.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 388 EIIFLGTGSAIPM----------------KIRNVSATLVNiSPDTSLLLDCGEGtfgqlCRHYGDQVDRVLGTLAAVFVS 451
Cdd:COG1235     2 KVTFLGSGSSGGVpqigcdcpvcastdprYGRTRSSILVE-ADGTRLLIDAGPD-----LREQLLRLGLDPSKIDAILLT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 452 HLHADHHTGLPSIllqRERALAslgKPLHpllVVAPNQLKAWLQQYHNQCQEvlHHISMIPAKCLQEGAEISspaverlI 531
Cdd:COG1235    76 HEHADHIAGLDDL---RPRYGP---NPIP---VYATPGTLEALERRFPYLFA--PYPGKLEFHEIEPGEPFE-------I 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 532 SSLlrtcdleEFQTCLVRH-CKHAFGCaLVHTSGWKVVYSGDT-MPCEALVRMGKDATLLIHEATLEDGleeeavEKTHS 609
Cdd:COG1235   138 GGL-------TVTPFPVPHdAGDPVGY-RIEDGGKKLAYATDTgYIPEEVLELLRGADLLILDATYDDP------EPGHL 203

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370471831 610 TTSQAISVGMRMNAEFIMLNHFSQRYAKVPLF-----SPNFSEKVGVAFDHMKV 658
Cdd:COG1235   204 SNEEALELLARLGPKRLVLTHLSPDNNDHELDydeleAALLPAGVEVAYDGMEI 257
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 1-74 1.19e-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: 61.13  E-value: 1.19e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370471831   1 MQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPK-CVLSGPPQLEKYLEAIKIFSGPLKGIELAVRPH 74
Cdd:cd16272    41 LLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRKKpLTIYGPKGIKEFLEKLLNFPVEILPLGFPLEIE 115
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 418-631 3.04e-06

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: 48.46  E-value: 3.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 418 LLLDCGEGTFGQLcRHYGDQVDRVLGTLAAVFVSHLHADHHTGLPSIllqRERALASLGKPLHPLLVVAPN-QLKAWLQQ 496
Cdd:pfam12706   3 ILIDPGPDLRQQA-LPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDL---REGRPRPLYAPLGVLAHLRRNfPYLFLLEH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 497 YHNQCQEV-----------LHHISMIPAkclQEGAEISSPAVERLISSLlrtcdleefqtclvrhckhafgcaLVHTSGW 565
Cdd:pfam12706  79 YGVRVHEIdwgesftvgdgGLTVTATPA---RHGSPRGLDPNPGDTLGF------------------------RIEGPGK 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370471831 566 KVVYSGDTMPCEALV--RMGkDATLLIHEATLEDglEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHF 631
Cdd:pfam12706 132 RVYYAGDTGYFPDEIgeRLG-GADLLLLDGGAWR--DDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 389-590 8.72e-06

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: 8.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 389 IIFLGTGSAipmkiRNVSATLVNIS-------PDTSLLLDCGEGTFGQLCRHYGDQVDrvlgtLAAVFVSHLHADHHTGL 461
Cdd:cd07741     1 IIFLGTGGG-----RFVVITQLRASggiwielNGKNIHIDPGPGALVRMCRPKLDPTK-----LDAIILSHRHLDHSNDA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 462 PSILlqreRALASLGKPlHPLLVVAPNQ--------LKAWLQQYhnqCQEVLHhismipakcLQEGAEISSPaverliss 533
Cdd:cd07741    71 NVLI----EAMTEGGFK-KRGTLLAPEDalngepvvLLYYHRRK---LEEIEI---------LEEGDEYELG-------- 125

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370471831 534 llrtcDLEEFQTCLVRHCKHAFGcALVHTSGWKVVYSGDTMPCEALVRMGKDATLLI 590
Cdd:cd07741   126 -----GIKIEATRHKHSDPTTYG-FIFRTSDKKIGYISDTRYFEELIEYYSNCDVLI 176
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 406-597 1.01e-05

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 46.78  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831  406 SATLVnISPDTSLLLDCGEGT----FGQLCRHYGDQVDrvlgtlaAVFVSHLHADHHTGLPSILlqreralaslgkPLHP 481
Cdd:smart00849   1 NSYLV-RDDGGAILIDTGPGEaedlLAELKKLGPKKID-------AIILTHGHPDHIGGLPELL------------EAPG 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831  482 LLVVAPNQLKAWLQQYHNQCQEVLHHI-SMIPAKCLQEGAEIsspaverlissllrtcDLEEFQTCLVRHCKHAFGCALV 560
Cdd:smart00849  61 APVYAPEGTAELLKDLLALLGELGAEAePAPPDRTLKDGDEL----------------DLGGGELEVIHTPGHTPGSIVL 124

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1370471831  561 HTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLED 597
Cdd:smart00849 125 YLPEGKILFTGDLLFAGGDGRTLVDGGDAAASDALES 161
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 1-26 9.18e-05

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: 41.04  E-value: 9.18e-05
                          10        20
                  ....*....|....*....|....*..
gi 1370471831   1 MQEHKLKVARLDNIFLTRMH-WSNVGG 26
Cdd:pfam13691  37 LNEQKVRLSKLEDIFLTGKVsWSNIGG 63
PRK02126 PRK02126
ribonuclease Z; Provisional
 562-636 3.99e-04

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 43.37  E-value: 3.99e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370471831 562 TSGWKVVYSGDTMP----CEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRYA 636
Cdd:PRK02126  240 EPGQKIGYVTDIGYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQ 318
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 413-465 1.20e-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: 40.59  E-value: 1.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370471831 413 SPDTSLLLDCGEGtfgqlCRHYGDQVDRVLGTLAAVFVSHL-----HADHHTGLPSIL 465
Cdd:cd07722    25 TGKRRILIDTGEG-----RPSYIPLLKSVLDSEGNATISDIllthwHHDHVGGLPDVL 77
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 407-465 2.46e-03

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: 40.23  E-value: 2.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370471831 407 ATLVNISPDTSLLLDCGEgtfgqlcRHYGDQVDRVL---------GTLAAVFVSHLHADHHTGLPSIL 465
Cdd:COG2333    13 AILIRTPDGKTILIDTGP-------RPSFDAGERVVlpylralgiRRLDLLVLTHPDADHIGGLAAVL 73
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 388-457 3.15e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 39.38  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370471831 388 EIIFLGTGSA--IPM---------------KIRNVSAtLVNIsPDTSLLLDCGEgTF-GQLCRHYGDQVDrvlgtlaAVF 449
Cdd:cd16279     2 KLTFLGTGTSsgVPVigcdcgvcdssdpknRRLRSSI-LIET-GGKNILIDTGP-DFrQQALRAGIRKLD-------AVL 71


                  ....*...
gi 1370471831 450 VSHLHADH 457
Cdd:cd16279    72 LTHAHADH 79
 
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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