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Conserved domains on  [gi|260166619|ref|NP_001159434|]
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zinc phosphodiesterase ELAC protein 2 isoform 3 [Homo sapiens]

Protein Classification

zinc phosphodiesterase ELAC protein 2( domain architecture ID 10888841)

zinc phosphodiesterase ELAC protein 2 is involved in tRNA maturation by catalyzing endonucleolytic cleavage and removing extra 3' nucleotides from tRNA precursors, generating 3' termini of tRNAs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 60-271 7.55e-108

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: 326.91  E-value: 7.55e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  60 LQVVAAGSRDSGAALYVFSEFNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLS 139
Cdd:cd16296    1 LQVVAAGSRDMGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 140 GPPQlekyleaikifsgplkgielavRPHSApeyedetmtvyqipiHSVSQRRGVRDSSLVVAFICKLHLKRGNFLVLKA 219
Cdd:cd16296   81 GPNK----------------------QSPDK---------------IGVRRQILERDPSLVVAFICKLHLKKGNFLVLKA 123

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 260166619 220 KEMGLPVGTAAIAPIIAAVKDGKSITHEGREILAEELCTPPDPGAAFVVVEC 271
Cdd:cd16296  124 KELGLPVGTAAIAPIIAAVKDGKSITFEGREILAEELCTPPDPGIVFIVVEC 175
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 443-648 5.25e-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: 315.26  E-value: 5.25e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 443 IIFLGTGSAIPMKIRNVSATLVNISPDTSLLLDCGEGTFGQLCRHYGDQ-VDRVLGTLAAVFVSHLHADHHTGLPSILLQ 521
Cdd:cd07718    1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 522 RERALAslgKPLHPLLVVAPNQLKAWLQQYHNQCQEVLHHISMIPAKCLQEGAEISSPAVERLISSLLRTCDLEEFQTCL 601
Cdd:cd07718   81 RKKLFK---PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKSIETVP 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 260166619 602 VRHCKHAFGCALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEAT 648
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; ...
 616-690 4.59e-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: 42.98  E-value: 4.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260166619 616 TSGWKVVYSGDTMP----CEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRYA 690
Cdd:PRK02126 240 EPGQKIGYVTDIGYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQ 318
 
Name Accession Description Interval E-value
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 60-271 7.55e-108

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: 326.91  E-value: 7.55e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  60 LQVVAAGSRDSGAALYVFSEFNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLS 139
Cdd:cd16296    1 LQVVAAGSRDMGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 140 GPPQlekyleaikifsgplkgielavRPHSApeyedetmtvyqipiHSVSQRRGVRDSSLVVAFICKLHLKRGNFLVLKA 219
Cdd:cd16296   81 GPNK----------------------QSPDK---------------IGVRRQILERDPSLVVAFICKLHLKKGNFLVLKA 123

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 260166619 220 KEMGLPVGTAAIAPIIAAVKDGKSITHEGREILAEELCTPPDPGAAFVVVEC 271
Cdd:cd16296  124 KELGLPVGTAAIAPIIAAVKDGKSITFEGREILAEELCTPPDPGIVFIVVEC 175
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 443-648 5.25e-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: 315.26  E-value: 5.25e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 443 IIFLGTGSAIPMKIRNVSATLVNISPDTSLLLDCGEGTFGQLCRHYGDQ-VDRVLGTLAAVFVSHLHADHHTGLPSILLQ 521
Cdd:cd07718    1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 522 RERALAslgKPLHPLLVVAPNQLKAWLQQYHNQCQEVLHHISMIPAKCLQEGAEISSPAVERLISSLLRTCDLEEFQTCL 601
Cdd:cd07718   81 RKKLFK---PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKSIETVP 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 260166619 602 VRHCKHAFGCALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEAT 648
Cdd:cd07718  158 VIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
442-712 5.33e-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: 5.33e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 442 EIIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLCRHYGDqvdrvLGTLAAVFVSHLHADHHTGLPSILLQ 521
Cdd:COG1234    2 KLTFLGTGGAVPTPGRATSSYLLEA-GGERLLIDCGEGTQRQLLRAGLD-----PRDIDAIFITHLHGDHIAGLPGLLST 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 522 ReralaSLGKPLHPLLVVAPNQLKAWLQQYHNQCQEVLH-HISMIPakcLQEGAEIsspaverlissllrtcDLEEFQ-- 598
Cdd:COG1234   76 R-----SLAGREKPLTIYGPPGTKEFLEALLKASGTDLDfPLEFHE---IEPGEVF----------------EIGGFTvt 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 599 TCLVRHCKHAFGcALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAE 678
Cdd:COG1234  132 AFPLDHPVPAYG-YRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVK 210

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 260166619 679 FIMLNHFSQRYAKVPLF----SPNFSEKVGVAFDHMKV 712
Cdd:COG1234  211 RLVLTHFSPRYDDPEELlaeaRAVFPGPVELAEDGMVI 248
PRK00055 PRK00055
ribonuclease Z; Reviewed
 442-689 4.24e-40

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 148.79  E-value: 4.24e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 442 EIIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLcRHYG---DQVDRvlgtlaaVFVSHLHADHHTGLPSI 518
Cdd:PRK00055   3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQL-LKTGikpRKIDK-------IFITHLHGDHIFGLPGL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 519 LLQReralaSLGKPLHPLLVVAPnqlkAWLQQYHNQCQEVLHHIS----------MIPAKCLQEGAEISSPAVERLISSl 588
Cdd:PRK00055  74 LSTR-----SLSGRTEPLTIYGP----KGIKEFVETLLRASGSLGyriaekdkpgKLDAEKLKALGVPPGPLFGKLKRG- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 589 lrtcdlEEFQTCLVRHCKHAFGCALVHTsGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQA 668
Cdd:PRK00055 144 ------EDVTLEDGRIINPADVLGPPRK-GRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEELAKEYGHSTARQA 216

                        250       260
                 ....*....|....*....|.
gi 260166619 669 ISVGMRMNAEFIMLNHFSQRY 689
Cdd:PRK00055 217 AEIAKEAGVKRLILTHFSPRY 237
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 442-689 5.94e-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: 129.26  E-value: 5.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  442 EIIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLcRHYG---DQVDRVlgtlaavFVSHLHADHHTGLPSI 518
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-NGELWLFDCGEGTQRQM-LRSGispMKIDRI-------FITHLHGDHILGLPGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  519 LLQReralaSLGKPLHPLLVVAPNQLKAWLQqyhNQCQEVLHHISMIPakclqEGAEISSPAVERlissllrtcDLEEFQ 598
Cdd:TIGR02651  72 LSTM-----SFQGRKEPLTIYGPPGIKEFIE---TSLRVSYTYLNYPI-----KIHEIEEGGLVF---------EDDGFK 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  599 --TCLVRHCKHAFGCALV-------------------------------------------------HTSGWKVVYSGDT 627
Cdd:TIGR02651 130 veAFPLDHSIPSLGYRFEekdrpgkfdrekakelgippgplygklkrgetvtlidgriidpedvlgpPRKGRKIAYTGDT 209

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260166619  628 MPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRY 689
Cdd:TIGR02651 210 RPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY 271
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 61-120 2.82e-18

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: 79.17  E-value: 2.82e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260166619   61 QVVAAGSRDS-GAALYVFSEFNRYLF-NCGEGVQRLMQEHKLKVARLDNIFLTRMH-WSNVGG 120
Cdd:pfam13691   1 QVVTTPTADTpGPLLLLHFDSKRYLFgNVGEGTQRALNEQKVRLSKLEDIFLTGKVsWSNIGG 63
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
50-188 9.41e-14

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 71.76  E-value: 9.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  50 GCSGGpntvylqvVAAGSRDSGAALYVFSEFnRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLK 129
Cdd:COG1234    7 GTGGA--------VPTPGRATSSYLLEAGGE-RLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRS 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260166619 130 ETGLPK-CVLSGPPQLEKYLEAIKIFSGPLKGIELAVRPHSAPE-YEDETMTVYQIPI-HSV 188
Cdd:COG1234   78 LAGREKpLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPGEvFEIGGFTVTAFPLdHPV 139
PRK00055 PRK00055
ribonuclease Z; Reviewed
 83-298 1.96e-10

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 62.12  E-value: 1.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  83 YLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCV-LSGPPQLEKYLEAIKIFSGPLkGi 161
Cdd:PRK00055  32 FLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSGRTEPLtIYGPKGIKEFVETLLRASGSL-G- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 162 elavrphsapeyedetmtvYQIpihsvsqrrgvrdsslvvaficKLHLKRGNFLVLKAKEMGLPVGTaaiapIIAAVKDG 241
Cdd:PRK00055 110 -------------------YRI----------------------AEKDKPGKLDAEKLKALGVPPGP-----LFGKLKRG 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260166619 242 KSITHE-GREILAEELCTPPDPGAAFVVV----ECPD-ESFIQP----ICEnATFqryqGKADAPVA 298
Cdd:PRK00055 144 EDVTLEdGRIINPADVLGPPRKGRKVAYCgdtrPCEAlVELAKGadllVHE-ATF----GDEDEELA 205
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 472-685 2.50e-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: 48.85  E-value: 2.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  472 LLLDCGEGTFGQLcRHYGDQVDRVLGTLAAVFVSHLHADHHTGLPSIllqRERALASLGKPLHPLLVVAPN-QLKAWLQQ 550
Cdd:pfam12706   3 ILIDPGPDLRQQA-LPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDL---REGRPRPLYAPLGVLAHLRRNfPYLFLLEH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  551 YHNQCQEV-----------LHHISMIPAkclQEGAEISSPAVERLISSLlrtcdleefqtclvrhckhafgcaLVHTSGW 619
Cdd:pfam12706  79 YGVRVHEIdwgesftvgdgGLTVTATPA---RHGSPRGLDPNPGDTLGF------------------------RIEGPGK 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260166619  620 KVVYSGDTMPCEALV--RMGkDATLLIHEATLEDglEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHF 685
Cdd:pfam12706 132 RVYYAGDTGYFPDEIgeRLG-GADLLLLDGGAWR--DDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 460-651 5.77e-06

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 47.55  E-value: 5.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619   460 SATLVnISPDTSLLLDCGEGT----FGQLCRHYGDQVDrvlgtlaAVFVSHLHADHHTGLPSILlqreralaslgkPLHP 535
Cdd:smart00849   1 NSYLV-RDDGGAILIDTGPGEaedlLAELKKLGPKKID-------AIILTHGHPDHIGGLPELL------------EAPG 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619   536 LLVVAPNQLKAWLQQYHNQCQEVLHHI-SMIPAKCLQEGAEIsspaverlissllrtcDLEEFQTCLVRHCKHAFGCALV 614
Cdd:smart00849  61 APVYAPEGTAELLKDLLALLGELGAEAePAPPDRTLKDGDEL----------------DLGGGELEVIHTPGHTPGSIVL 124

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 260166619   615 HTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLED 651
Cdd:smart00849 125 YLPEGKILFTGDLLFAGGDGRTLVDGGDAAASDALES 161
PRK02126 PRK02126
ribonuclease Z; Provisional
 616-690 4.59e-04

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 42.98  E-value: 4.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260166619 616 TSGWKVVYSGDTMP----CEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRYA 690
Cdd:PRK02126 240 EPGQKIGYVTDIGYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQ 318
 
Name Accession Description Interval E-value
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 60-271 7.55e-108

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: 326.91  E-value: 7.55e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  60 LQVVAAGSRDSGAALYVFSEFNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLS 139
Cdd:cd16296    1 LQVVAAGSRDMGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 140 GPPQlekyleaikifsgplkgielavRPHSApeyedetmtvyqipiHSVSQRRGVRDSSLVVAFICKLHLKRGNFLVLKA 219
Cdd:cd16296   81 GPNK----------------------QSPDK---------------IGVRRQILERDPSLVVAFICKLHLKKGNFLVLKA 123

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 260166619 220 KEMGLPVGTAAIAPIIAAVKDGKSITHEGREILAEELCTPPDPGAAFVVVEC 271
Cdd:cd16296  124 KELGLPVGTAAIAPIIAAVKDGKSITFEGREILAEELCTPPDPGIVFIVVEC 175
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 443-648 5.25e-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: 315.26  E-value: 5.25e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 443 IIFLGTGSAIPMKIRNVSATLVNISPDTSLLLDCGEGTFGQLCRHYGDQ-VDRVLGTLAAVFVSHLHADHHTGLPSILLQ 521
Cdd:cd07718    1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 522 RERALAslgKPLHPLLVVAPNQLKAWLQQYHNQCQEVLHHISMIPAKCLQEGAEISSPAVERLISSLLRTCDLEEFQTCL 601
Cdd:cd07718   81 RKKLFK---PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKSIETVP 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 260166619 602 VRHCKHAFGCALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEAT 648
Cdd:cd07718  158 VIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
442-712 5.33e-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: 5.33e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 442 EIIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLCRHYGDqvdrvLGTLAAVFVSHLHADHHTGLPSILLQ 521
Cdd:COG1234    2 KLTFLGTGGAVPTPGRATSSYLLEA-GGERLLIDCGEGTQRQLLRAGLD-----PRDIDAIFITHLHGDHIAGLPGLLST 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 522 ReralaSLGKPLHPLLVVAPNQLKAWLQQYHNQCQEVLH-HISMIPakcLQEGAEIsspaverlissllrtcDLEEFQ-- 598
Cdd:COG1234   76 R-----SLAGREKPLTIYGPPGTKEFLEALLKASGTDLDfPLEFHE---IEPGEVF----------------EIGGFTvt 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 599 TCLVRHCKHAFGcALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAE 678
Cdd:COG1234  132 AFPLDHPVPAYG-YRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVK 210

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 260166619 679 FIMLNHFSQRYAKVPLF----SPNFSEKVGVAFDHMKV 712
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 ...
 443-689 5.90e-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: 170.32  E-value: 5.90e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 443 IIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLcRHYGdqvdRVLGTLAAVFVSHLHADHHTGLPSiLLQR 522
Cdd:cd07717    1 LTFLGTGSAVPTPERNLSSIALRL-EGELWLFDCGEGTQRQL-LRAG----LSPSKIDRIFITHLHGDHILGLPG-LLST 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 523 eralASLGKPLHPLLVVAPNQLKAWLQQYHNQCQEVLhhismipakclqeGAEIsspAVERLISSLLRTCDLEEFQ--TC 600
Cdd:cd07717   74 ----MSLLGRTEPLTIYGPKGLKEFLETLLRLSASRL-------------PYPI---EVHELEPDPGLVFEDDGFTvtAF 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 601 LVRHCKHAFGCALvhTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFI 680
Cdd:cd07717  134 PLDHRVPCFGYRF--EEGRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKAKETGHSTAKQAAEIAKKAGVKKL 211


                 ....*....
gi 260166619 681 MLNHFSQRY 689
Cdd:cd07717  212 VLTHFSARY 220
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 443-647 5.58e-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: 156.65  E-value: 5.58e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 443 IIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLCRHYGDqvdrvLGTLAAVFVSHLHADHHTGLPSILLQR 522
Cdd:cd16272    1 LTFLGTGGAVPSLTRNTSSYLLET-GGTRILLDCGEGTVYRLLKAGVD-----PDKLDAIFLSHFHLDHIGGLPTLLFAR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 523 EralasLGKPLHPLLVVAPNQLKAWLQQYHNQCQEVLHHISMIpakclqEGAEISSPAVERLISSLlrtcdleEFQTCLV 602
Cdd:cd16272   75 R-----YGGRKKPLTIYGPKGIKEFLEKLLNFPVEILPLGFPL------EIEELEEGGEVLELGDL-------KVEAFPV 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 260166619 603 RHCKHAFGCALVHTsGWKVVYSGDTMPCEALVRMGKDATLLIHEA 647
Cdd:cd16272  137 KHSVESLGYRIEAE-GKSIVYSGDTGPCENLVELAKGADLLIHEC 180
PRK00055 PRK00055
ribonuclease Z; Reviewed
 442-689 4.24e-40

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 148.79  E-value: 4.24e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 442 EIIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLcRHYG---DQVDRvlgtlaaVFVSHLHADHHTGLPSI 518
Cdd:PRK00055   3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQL-LKTGikpRKIDK-------IFITHLHGDHIFGLPGL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 519 LLQReralaSLGKPLHPLLVVAPnqlkAWLQQYHNQCQEVLHHIS----------MIPAKCLQEGAEISSPAVERLISSl 588
Cdd:PRK00055  74 LSTR-----SLSGRTEPLTIYGP----KGIKEFVETLLRASGSLGyriaekdkpgKLDAEKLKALGVPPGPLFGKLKRG- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 589 lrtcdlEEFQTCLVRHCKHAFGCALVHTsGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQA 668
Cdd:PRK00055 144 ------EDVTLEDGRIINPADVLGPPRK-GRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEELAKEYGHSTARQA 216

                        250       260
                 ....*....|....*....|.
gi 260166619 669 ISVGMRMNAEFIMLNHFSQRY 689
Cdd:PRK00055 217 AEIAKEAGVKRLILTHFSPRY 237
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 442-689 5.94e-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: 129.26  E-value: 5.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  442 EIIFLGTGSAIPMKIRNVSATLVNIsPDTSLLLDCGEGTFGQLcRHYG---DQVDRVlgtlaavFVSHLHADHHTGLPSI 518
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-NGELWLFDCGEGTQRQM-LRSGispMKIDRI-------FITHLHGDHILGLPGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  519 LLQReralaSLGKPLHPLLVVAPNQLKAWLQqyhNQCQEVLHHISMIPakclqEGAEISSPAVERlissllrtcDLEEFQ 598
Cdd:TIGR02651  72 LSTM-----SFQGRKEPLTIYGPPGIKEFIE---TSLRVSYTYLNYPI-----KIHEIEEGGLVF---------EDDGFK 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  599 --TCLVRHCKHAFGCALV-------------------------------------------------HTSGWKVVYSGDT 627
Cdd:TIGR02651 130 veAFPLDHSIPSLGYRFEekdrpgkfdrekakelgippgplygklkrgetvtlidgriidpedvlgpPRKGRKIAYTGDT 209

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260166619  628 MPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRY 689
Cdd:TIGR02651 210 RPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY 271
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 442-645 4.08e-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: 4.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 442 EIIFLGTGSAIPMKIRNVSATLVnISPDTSLLLDCGEGTFGQLCrhygdQVDRVLGTLAAVFVSHLHADHHTGLPSILLQ 521
Cdd:cd07719    1 RVTLLGTGGPIPDPDRAGPSTLV-VVGGRVYLVDAGSGVVRRLA-----QAGLPLGDLDAVFLTHLHSDHVADLPALLLT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 522 ReralaSLGKPLHPLLVVAPNQLKAW---LQQYHNQCQEVLHHISMIPAkcLQEGA-----EISSPAVerlissllrTCD 593
Cdd:cd07719   75 A-----WLAGRKTPLPVYGPPGTRALvdgLLAAYALDIDYRARIGDEGR--PDPGAlvevhEIAAGGV---------VYE 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 260166619 594 LEEFQ--TCLVRH--CKHAFgcAL-VHTSGWKVVYSGDTMPCEALVRMGKDATLLIH 645
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 ...
 467-647 1.58e-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: 1.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 467 SPDTSLLLDCGEGTFGQLCRHygdqVDrvLGTLAAVFVSHLHADHHTGLPSilLQRERALASLGKPLHPLLVVAPNQLKA 546
Cdd:cd07716   25 ADGFRILLDCGSGVLSRLQRY----ID--PEDLDAVVLSHLHPDHCADLGV--LQYARRYHPRGARKPPLPLYGPAGPAE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 547 WLQQ-YHNQCQEVLHHISmiPAKCLQEGaeisspaverlissllrtcDLeEFQTCLVRHCKHAFGCALVHtSGWKVVYSG 625
Cdd:cd07716   97 RLAAlYGLEDVFDFHPIE--PGEPLEIG-------------------PF-TITFFRTVHPVPCYAMRIED-GGKVLVYTG 153

                        170       180
                 ....*....|....*....|..
gi 260166619 626 DTMPCEALVRMGKDATLLIHEA 647
Cdd:cd07716  154 DTGYCDELVEFARGADLLLCEA 175
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 70-271 9.47e-19

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: 84.62  E-value: 9.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  70 SGAALYVFSEFNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPK-CVLSGPPQLEKYL 148
Cdd:cd16272   16 NTSSYLLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRKKpLTIYGPKGIKEFL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 149 EAIKIFSGPLKGIELAVrphsapEYEDetmtvyqIPIHSVSQRRGvrdsSLVVAFICKLHLKRGNFLVLKAkemglpvgt 228
Cdd:cd16272   96 EKLLNFPVEILPLGFPL------EIEE-------LEEGGEVLELG----DLKVEAFPVKHSVESLGYRIEA--------- 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 260166619 229 aaiapiiaavkDGKSI-----THEGREILaeELCtppdPGAAFVVVEC 271
Cdd:cd16272  150 -----------EGKSIvysgdTGPCENLV--ELA----KGADLLIHEC 180
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 61-120 2.82e-18

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: 79.17  E-value: 2.82e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 260166619   61 QVVAAGSRDS-GAALYVFSEFNRYLF-NCGEGVQRLMQEHKLKVARLDNIFLTRMH-WSNVGG 120
Cdd:pfam13691   1 QVVTTPTADTpGPLLLLHFDSKRYLFgNVGEGTQRALNEQKVRLSKLEDIFLTGKVsWSNIGG 63
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 444-647 3.92e-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: 83.08  E-value: 3.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 444 IFLGTGSAIPMKIRNVSATLVNiSPDTSLLLDCGEGTFGQLCRhYGdqVDRVlgTLAAVFVSHLHADHHTGLPSILL--- 520
Cdd:cd07740    1 TFLGSGDAFGSGGRLNTCFHVA-SEAGRFLIDCGASSLIALKR-AG--IDPN--AIDAIFITHLHGDHFGGLPFFLLdaq 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 521 ---QRERalaslgkplhPLLVVAPNQLKAWLQQyhnqCQEVLH-HISMIPAKclqegAEISSPAVERLISSLLRTCDLEE 596
Cdd:cd07740   75 fvaKRTR----------PLTIAGPPGLRERLRR----AMEALFpGSSKVPRR-----FDLEVIELEPGEPTTLGGVTVTA 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 260166619 597 FQtclVRHCKHAFGCALVHTSGWKVV-YSGDTMPCEALVRMGKDATLLIHEA 647
Cdd:cd07740  136 FP---VVHPSGALPLALRLEAAGRVLaYSGDTEWTDALVPLARGADLFICEC 184
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 442-712 2.13e-16

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 79.94  E-value: 2.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 442 EIIFLGTGSAIPM----------------KIRNVSATLVNiSPDTSLLLDCGEGtfgqlCRHYGDQVDRVLGTLAAVFVS 505
Cdd:COG1235    2 KVTFLGSGSSGGVpqigcdcpvcastdprYGRTRSSILVE-ADGTRLLIDAGPD-----LREQLLRLGLDPSKIDAILLT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 506 HLHADHHTGLPSIllqRERALAslgKPLHpllVVAPNQLKAWLQQYHNQCQEvlHHISMIPAKCLQEGAEISspaverlI 585
Cdd:COG1235   76 HEHADHIAGLDDL---RPRYGP---NPIP---VYATPGTLEALERRFPYLFA--PYPGKLEFHEIEPGEPFE-------I 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 586 SSLlrtcdleEFQTCLVRH-CKHAFGCaLVHTSGWKVVYSGDT-MPCEALVRMGKDATLLIHEATLEDGleeeavEKTHS 663
Cdd:COG1235  138 GGL-------TVTPFPVPHdAGDPVGY-RIEDGGKKLAYATDTgYIPEEVLELLRGADLLILDATYDDP------EPGHL 203

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 260166619 664 TTSQAISVGMRMNAEFIMLNHFSQRYAKVPLF-----SPNFSEKVGVAFDHMKV 712
Cdd:COG1235  204 SNEEALELLARLGPKRLVLTHLSPDNNDHELDydeleAALLPAGVEVAYDGMEI 257
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 81-188 1.05e-14

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: 74.41  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  81 NRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCV-LSGPPQLEKYLEAIKIFSGPLK 159
Cdd:cd07717   27 ELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGRTEPLtIYGPKGLKEFLETLLRLSASRL 106

                         90       100       110
                 ....*....|....*....|....*....|...
gi 260166619 160 GIELAVRPHSAPE---YEDETMTVYQIPI-HSV 188
Cdd:cd07717  107 PYPIEVHELEPDPglvFEDDGFTVTAFPLdHRV 139
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
50-188 9.41e-14

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 71.76  E-value: 9.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  50 GCSGGpntvylqvVAAGSRDSGAALYVFSEFnRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLK 129
Cdd:COG1234    7 GTGGA--------VPTPGRATSSYLLEAGGE-RLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRS 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260166619 130 ETGLPK-CVLSGPPQLEKYLEAIKIFSGPLKGIELAVRPHSAPE-YEDETMTVYQIPI-HSV 188
Cdd:COG1234   78 LAGREKpLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPGEvFEIGGFTVTAFPLdHPV 139
PRK00055 PRK00055
ribonuclease Z; Reviewed
 83-298 1.96e-10

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 62.12  E-value: 1.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  83 YLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCV-LSGPPQLEKYLEAIKIFSGPLkGi 161
Cdd:PRK00055  32 FLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSGRTEPLtIYGPKGIKEFVETLLRASGSL-G- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 162 elavrphsapeyedetmtvYQIpihsvsqrrgvrdsslvvaficKLHLKRGNFLVLKAKEMGLPVGTaaiapIIAAVKDG 241
Cdd:PRK00055 110 -------------------YRI----------------------AEKDKPGKLDAEKLKALGVPPGP-----LFGKLKRG 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260166619 242 KSITHE-GREILAEELCTPPDPGAAFVVV----ECPD-ESFIQP----ICEnATFqryqGKADAPVA 298
Cdd:PRK00055 144 EDVTLEdGRIINPADVLGPPRKGRKVAYCgdtrPCEAlVELAKGadllVHE-ATF----GDEDEELA 205
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 472-685 2.50e-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: 48.85  E-value: 2.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  472 LLLDCGEGTFGQLcRHYGDQVDRVLGTLAAVFVSHLHADHHTGLPSIllqRERALASLGKPLHPLLVVAPN-QLKAWLQQ 550
Cdd:pfam12706   3 ILIDPGPDLRQQA-LPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDL---REGRPRPLYAPLGVLAHLRRNfPYLFLLEH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  551 YHNQCQEV-----------LHHISMIPAkclQEGAEISSPAVERLISSLlrtcdleefqtclvrhckhafgcaLVHTSGW 619
Cdd:pfam12706  79 YGVRVHEIdwgesftvgdgGLTVTATPA---RHGSPRGLDPNPGDTLGF------------------------RIEGPGK 131

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260166619  620 KVVYSGDTMPCEALV--RMGkDATLLIHEATLEDglEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHF 685
Cdd:pfam12706 132 RVYYAGDTGYFPDEIgeRLG-GADLLLLDGGAWR--DDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 460-651 5.77e-06

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 47.55  E-value: 5.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619   460 SATLVnISPDTSLLLDCGEGT----FGQLCRHYGDQVDrvlgtlaAVFVSHLHADHHTGLPSILlqreralaslgkPLHP 535
Cdd:smart00849   1 NSYLV-RDDGGAILIDTGPGEaedlLAELKKLGPKKID-------AIILTHGHPDHIGGLPELL------------EAPG 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619   536 LLVVAPNQLKAWLQQYHNQCQEVLHHI-SMIPAKCLQEGAEIsspaverlissllrtcDLEEFQTCLVRHCKHAFGCALV 614
Cdd:smart00849  61 APVYAPEGTAELLKDLLALLGELGAEAePAPPDRTLKDGDEL----------------DLGGGELEVIHTPGHTPGSIVL 124

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 260166619   615 HTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLED 651
Cdd:smart00849 125 YLPEGKILFTGDLLFAGGDGRTLVDGGDAAASDALES 161
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 443-644 9.49e-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: 9.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 443 IIFLGTGSAipmkiRNVSATLVNIS-------PDTSLLLDCGEGTFGQLCRHYGDQVDrvlgtLAAVFVSHLHADHHTGL 515
Cdd:cd07741    1 IIFLGTGGG-----RFVVITQLRASggiwielNGKNIHIDPGPGALVRMCRPKLDPTK-----LDAIILSHRHLDHSNDA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 516 PSILlqreRALASLGKPlHPLLVVAPNQ--------LKAWLQQYhnqCQEVLHhismipakcLQEGAEISSPaverliss 587
Cdd:cd07741   71 NVLI----EAMTEGGFK-KRGTLLAPEDalngepvvLLYYHRRK---LEEIEI---------LEEGDEYELG-------- 125

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 260166619 588 llrtcDLEEFQTCLVRHCKHAFGcALVHTSGWKVVYSGDTMPCEALVRMGKDATLLI 644
Cdd:cd07741  126 -----GIKIEATRHKHSDPTTYG-FIFRTSDKKIGYISDTRYFEELIEYYSNCDVLI 176
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 52-180 1.37e-04

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: 43.66  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619  52 SGGPntvylqvVAAGSRdSGAALYVFSEFNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKET 131
Cdd:cd07719    7 TGGP-------IPDPDR-AGPSTLVVVGGRVYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLLTAWLA 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260166619 132 GLPKCV-LSGPPQLEKYLEAI------------KIFSGPLKGIELAVRPH----SAPEYEDETMTV 180
Cdd:cd07719   79 GRKTPLpVYGPPGTRALVDGLlaayaldidyraRIGDEGRPDPGALVEVHeiaaGGVVYEDDGVKV 144
PRK02126 PRK02126
ribonuclease Z; Provisional
 616-690 4.59e-04

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 42.98  E-value: 4.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260166619 616 TSGWKVVYSGDTMP----CEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRYA 690
Cdd:PRK02126 240 EPGQKIGYVTDIGYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQ 318
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 467-519 1.05e-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: 40.98  E-value: 1.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 260166619 467 SPDTSLLLDCGEGtfgqlCRHYGDQVDRVLGTLAAVFVSHL-----HADHHTGLPSIL 519
Cdd:cd07722   25 TGKRRILIDTGEG-----RPSYIPLLKSVLDSEGNATISDIllthwHHDHVGGLPDVL 77
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 461-519 2.51e-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: 2.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260166619 461 ATLVNISPDTSLLLDCGEgtfgqlcRHYGDQVDRVL---------GTLAAVFVSHLHADHHTGLPSIL 519
Cdd:COG2333   13 AILIRTPDGKTILIDTGP-------RPSFDAGERVVlpylralgiRRLDLLVLTHPDADHIGGLAAVL 73
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 442-511 3.46e-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: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260166619 442 EIIFLGTGSA--IPM---------------KIRNVSAtLVNIsPDTSLLLDCGEgTF-GQLCRHYGDQVDrvlgtlaAVF 503
Cdd:cd16279    2 KLTFLGTGTSsgVPVigcdcgvcdssdpknRRLRSSI-LIET-GGKNILIDTGP-DFrQQALRAGIRKLD-------AVL 71


                 ....*...
gi 260166619 504 VSHLHADH 511
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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