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Conserved domains on  [gi|145338580|ref|NP_188247|]
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tRNAse Z4 [Arabidopsis thaliana]

Protein Classification

ribonuclease Z( domain architecture ID 11224864)

ribonuclease Z family protein similar to Arabidopsis thaliana mitochondrial tRNase Z TRZ4, which displays tRNA 3'-processing endonuclease activity

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 576-829 2.37e-90

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: 285.60  E-value: 2.37e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 576 IVLLGTGSSQPSKYRNVTAIYIDLFSRGSILLDCGEGTLGQLKRRYGLEGADEAVRNLRCIWISHIHADHHTGLARILAR 655
Cdd:cd07718    1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEEADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 656 RRELLKgLAHEPAIVVGPRSLKNFLDAYQRLEDLDMEFLDCRNTtttswasvetsrpekntssgnaegslfskgslmqsi 735
Cdd:cd07718   81 RKKLFK-PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISN------------------------------------ 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 736 ykrPSSPLTDNSSALPFLKKLKKVLGEMGLEHLISFPVVHCPQAFGVSLKAAErkniagdeipGWKMVYSGDTRPCPEMV 815
Cdd:cd07718  124 ---RVSQSLPESDDPLSRDLLSNLLEELGLKSIETVPVIHCPDAYGIVLTHED----------GWKIVYSGDTRPCEALV 190

                        250
                 ....*....|....
gi 145338580 816 EASKGATVLIHEAT 829
Cdd:cd07718  191 EAGKGADLLIHEAT 204
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 132-188 1.03e-16

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: 74.93  E-value: 1.03e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145338580  132 QILGTgmDTQDTS-PSVLLFFDKQRFIF-NAGEGLQRFCTEHKIKLSKVDHIFLSRVCS 188
Cdd:pfam13691   1 QVVTT--PTADTPgPLLLLHFDSKRYLFgNVGEGTQRALNEQKVRLSKLEDIFLTGKVS 57
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 796-866 5.98e-05

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


The actual alignment was detected with superfamily member pfam12706:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 196  Bit Score: 44.99  E-value: 5.98e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145338580  796 EIPGWKMVYSGDTRPCPEMVEAS-KGATVLIHEATFEDAlvEEAVAKNHSTTKEAIKVGSSAGVYRTVLTHF 866
Cdd:pfam12706 127 EGPGKRVYYAGDTGYFPDEIGERlGGADLLLLDGGAWRD--DEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
tRNA_deacylase super family cl00716
D-aminoacyl-tRNA deacylase; Several aminoacyl-tRNA synthetases have the ability to transfer ...
 308-349 2.58e-04

D-aminoacyl-tRNA deacylase; Several aminoacyl-tRNA synthetases have the ability to transfer the D-isomer of their amino acid onto their cognate tRNA. D-aminoacyl-tRNA deacylases hydrolyse the ester bond between the polynucleotide and the D-amino acid, thereby preventing the accumulation of such mis-acylated and metabolically inactive tRNA molecules.


The actual alignment was detected with superfamily member PRK14866:

Pssm-ID: 469887  Cd Length: 451  Bit Score: 44.61  E-value: 2.58e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 145338580 308 KFDPKKAMALGLRAGPKYSYLQSGQSVKSDfkDITVHPSDVM 349
Cdd:PRK14866 397 RFDPELARKLGVPEGPAFGKLAAGQPVEVD--GETITPEMVH 436
 
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 ...
 576-829 2.37e-90

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: 285.60  E-value: 2.37e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 576 IVLLGTGSSQPSKYRNVTAIYIDLFSRGSILLDCGEGTLGQLKRRYGLEGADEAVRNLRCIWISHIHADHHTGLARILAR 655
Cdd:cd07718    1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEEADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 656 RRELLKgLAHEPAIVVGPRSLKNFLDAYQRLEDLDMEFLDCRNTtttswasvetsrpekntssgnaegslfskgslmqsi 735
Cdd:cd07718   81 RKKLFK-PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISN------------------------------------ 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 736 ykrPSSPLTDNSSALPFLKKLKKVLGEMGLEHLISFPVVHCPQAFGVSLKAAErkniagdeipGWKMVYSGDTRPCPEMV 815
Cdd:cd07718  124 ---RVSQSLPESDDPLSRDLLSNLLEELGLKSIETVPVIHCPDAYGIVLTHED----------GWKIVYSGDTRPCEALV 190

                        250
                 ....*....|....
gi 145338580 816 EASKGATVLIHEAT 829
Cdd:cd07718  191 EAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
574-894 4.38e-49

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 174.23  E-value: 4.38e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 574 MEIVLLGTGSSQPSKYRNVTAIYIDlFSRGSILLDCGEGTLGQLkRRYGLEgadeaVRNLRCIWISHIHADHHTGLARIL 653
Cdd:COG1234    1 MKLTFLGTGGAVPTPGRATSSYLLE-AGGERLLIDCGEGTQRQL-LRAGLD-----PRDIDAIFITHLHGDHIAGLPGLL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 654 ARRRelLKGLAhEPAIVVGPRSLKNFLDAYQRLEDLDMEF-LDCRNTTttswasvetsrpekntssgnaEGSLFSKGSLm 732
Cdd:COG1234   74 STRS--LAGRE-KPLTIYGPPGTKEFLEALLKASGTDLDFpLEFHEIE---------------------PGEVFEIGGF- 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 733 qsiykrpsspltdnssalpflkklkkvlgemgleHLISFPVVHCPQAFGVSLkaaerkniagdEIPGWKMVYSGDTRPCP 812
Cdd:COG1234  129 ----------------------------------TVTAFPLDHPVPAYGYRF-----------EEPGRSLVYSGDTRPCE 163

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 813 EMVEASKGATVLIHEATFEDALVEEAVAKNHSTTKEAIKVGSSAGVYRTVLTHFSQRYPKI-PVIDESHMH---NTCIAF 888
Cdd:COG1234  164 ALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDDPeELLAEARAVfpgPVELAE 243


                 ....*.
gi 145338580 889 DMMSIN 894
Cdd:COG1234  244 DGMVIE 249
PRK00055 PRK00055
ribonuclease Z; Reviewed
 574-893 1.64e-48

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 173.44  E-value: 1.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 574 MEIVLLGTGSSQPSKYRNVTAIYIDLFSRGsILLDCGEGTLGQLkRRYGLegadeAVRNLRCIWISHIHADHHTGLARIL 653
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGGEL-FLFDCGEGTQRQL-LKTGI-----KPRKIDKIFITHLHGDHIFGLPGLL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 654 ARR----REllkglahEPAIVVGPRSLKNFLDAYQRLedldmefldcrnTTTTSWASVETSRP-----EKNTSSGNAEGs 724
Cdd:PRK00055  75 STRslsgRT-------EPLTIYGPKGIKEFVETLLRA------------SGSLGYRIAEKDKPgkldaEKLKALGVPPG- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 725 lfskgslmqsiykrpsspltdnssalPFLKKLKKvlgemglehlisfpvvhcpqafGVSLKAAERKNIAGDEI-----PG 799
Cdd:PRK00055 135 --------------------------PLFGKLKR----------------------GEDVTLEDGRIINPADVlgpprKG 166

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 800 WKMVYSGDTRPCPEMVEASKGATVLIHEATFEDALVEEAVAKNHSTTKEAIKVGSSAGVYRTVLTHFSQRYPKipviDES 879
Cdd:PRK00055 167 RKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTG----DPE 242

                        330       340
                 ....*....|....*....|..
gi 145338580 880 HMH--------NTCIAFDMMSI 893
Cdd:PRK00055 243 ELLkeareifpNTELAEDLMRV 264
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 575-894 9.31e-45

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: 163.54  E-value: 9.31e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580  575 EIVLLGTGSSQPSKYRNVTAIYIDLFSRGsILLDCGEGTLGQLkRRYGLegadeAVRNLRCIWISHIHADHHTGLARILA 654
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLNGEL-WLFDCGEGTQRQM-LRSGI-----SPMKIDRIFITHLHGDHILGLPGLLS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580  655 RRrELLKGlaHEPAIVVGPRSLKNFLD----------AY-----------QRLEDLDME---FLDCRNTTTTSWASVETS 710
Cdd:TIGR02651  74 TM-SFQGR--KEPLTIYGPPGIKEFIEtslrvsytylNYpikiheieeggLVFEDDGFKveaFPLDHSIPSLGYRFEEKD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580  711 RPEKNtssgNAEGSLFskgslmqsiYKRPSSPLtdnssalpfLKKLKKvlGEmglehlisfpVVHCPQafGVSLKAAErk 790
Cdd:TIGR02651 151 RPGKF----DREKAKE---------LGIPPGPL---------YGKLKR--GE----------TVTLID--GRIIDPED-- 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580  791 nIAGDEIPGWKMVYSGDTRPCPEMVEASKGATVLIHEATFEDALVEEAVAKNHSTTKEAIKVGSSAGVYRTVLTHFSQRY 870
Cdd:TIGR02651 193 -VLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY 271

                         330       340
                  ....*....|....*....|....*..
gi 145338580  871 PKIPVIDE---SHMHNTCIAFDMMSIN 894
Cdd:TIGR02651 272 SDEEELLEeakKIFPNTYIAEDFMEIE 298
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 132-188 1.03e-16

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: 74.93  E-value: 1.03e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145338580  132 QILGTgmDTQDTS-PSVLLFFDKQRFIF-NAGEGLQRFCTEHKIKLSKVDHIFLSRVCS 188
Cdd:pfam13691   1 QVVTT--PTADTPgPLLLLHFDSKRYLFgNVGEGTQRALNEQKVRLSKLEDIFLTGKVS 57
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 131-363 8.89e-10

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: 58.81  E-value: 8.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 131 VQILGTGmdTQDTSPSVLLFFDKQRFIFNAGEGLQRFCTEHKIKLSKVDHIFLSRVCSEtagglpgllltlagigeqgls 210
Cdd:cd16296    1 LQVVAAG--SRDMGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWS--------------------- 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 211 vNVWGPSDLKYLVDAMRsfIPRAAMVhtrsfGPSLNISDSAPQIGLSKPKDDAYVlvddevvkisaillepsrleesgsk 290
Cdd:cd16296   58 -NVGGLSGMILTLKETG--LPKCVLS-----GPNKQSPDKIGVRRQILERDPSLV------------------------- 104

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145338580 291 pgetaVIYVCELPEIKGKFDPKKAMALGLRAG-----PKYSYLQSGQSVKSDFKDITVHpsDVMGPSVPGPVVLLVDC 363
Cdd:cd16296  105 -----VAFICKLHLKKGNFLVLKAKELGLPVGtaaiaPIIAAVKDGKSITFEGREILAE--ELCTPPDPGIVFIVVEC 175
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
131-184 7.75e-07

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 51.35  E-value: 7.75e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145338580 131 VQILGTG--MDTQDT-SPSVLLFFDKQRFIFNAGEGLQRFCTEHKIKLSKVDHIFLS 184
Cdd:COG1234    3 LTFLGTGgaVPTPGRaTSSYLLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFIT 59
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 796-866 5.98e-05

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: 44.99  E-value: 5.98e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145338580  796 EIPGWKMVYSGDTRPCPEMVEAS-KGATVLIHEATFEDAlvEEAVAKNHSTTKEAIKVGSSAGVYRTVLTHF 866
Cdd:pfam12706 127 EGPGKRVYYAGDTGYFPDEIGERlGGADLLLLDGGAWRD--DEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK14866 PRK14866
hypothetical protein; Provisional
 308-349 2.58e-04

hypothetical protein; Provisional


Pssm-ID: 237840  Cd Length: 451  Bit Score: 44.61  E-value: 2.58e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 145338580 308 KFDPKKAMALGLRAGPKYSYLQSGQSVKSDfkDITVHPSDVM 349
Cdd:PRK14866 397 RFDPELARKLGVPEGPAFGKLAAGQPVEVD--GETITPEMVH 436
PRK00055 PRK00055
ribonuclease Z; Reviewed
 131-355 6.55e-04

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 42.48  E-value: 6.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 131 VQILGTG--MDTQDTS-PSVLLFFDKQRFIFNAGEGLQRFCTEHKIKLSKVDHIFLSRVCSETAGGLPGLLltlAGIGEQ 207
Cdd:PRK00055   4 LTFLGTGsgVPTPTRNvSSILLRLGGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLL---STRSLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 208 GLS--VNVWGPSDLKYLVDAMRSFipraamvhTRSFGpslnisdsapqiglskpkddaYvlvddevvkisaillepsRLE 285
Cdd:PRK00055  81 GRTepLTIYGPKGIKEFVETLLRA--------SGSLG---------------------Y------------------RIA 113

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 286 EsgskpgetaviyvcelPEIKGKFDPKKAMALGLRAGPKYSYLQSGQSVKSDFKDItVHPSDVMGPSVPG 355
Cdd:PRK00055 114 E----------------KDKPGKLDAEKLKALGVPPGPLFGKLKRGEDVTLEDGRI-INPADVLGPPRKG 166
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 603-655 9.43e-04

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 41.00  E-value: 9.43e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 145338580   603 GSILLDCGEGTLGQLKRRYGLEGadeaVRNLRCIWISHIHADHHTGLARILAR 655
Cdd:smart00849  10 GAILIDTGPGEAEDLLAELKKLG----PKKIDAIILTHGHPDHIGGLPELLEA 58
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
591-666 2.13e-03

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 40.43  E-value: 2.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145338580  591 NVTAIYIDlfsRGSILLDCGEGTLGQLKRRYGLEGADeaVRNLRCIWISHIHADhHTGLARILARRRELLKGLAHE 666
Cdd:pfam00753   7 NSYLIEGG---GGAVLIDTGGSAEAALLLLLAALGLG--PKDIDAVILTHGHFD-HIGGLGELAEATDVPVIVVAE 76
 
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 ...
 576-829 2.37e-90

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: 285.60  E-value: 2.37e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 576 IVLLGTGSSQPSKYRNVTAIYIDLFSRGSILLDCGEGTLGQLKRRYGLEGADEAVRNLRCIWISHIHADHHTGLARILAR 655
Cdd:cd07718    1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEEADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 656 RRELLKgLAHEPAIVVGPRSLKNFLDAYQRLEDLDMEFLDCRNTtttswasvetsrpekntssgnaegslfskgslmqsi 735
Cdd:cd07718   81 RKKLFK-PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISN------------------------------------ 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 736 ykrPSSPLTDNSSALPFLKKLKKVLGEMGLEHLISFPVVHCPQAFGVSLKAAErkniagdeipGWKMVYSGDTRPCPEMV 815
Cdd:cd07718  124 ---RVSQSLPESDDPLSRDLLSNLLEELGLKSIETVPVIHCPDAYGIVLTHED----------GWKIVYSGDTRPCEALV 190

                        250
                 ....*....|....
gi 145338580 816 EASKGATVLIHEAT 829
Cdd:cd07718  191 EAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
574-894 4.38e-49

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 174.23  E-value: 4.38e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 574 MEIVLLGTGSSQPSKYRNVTAIYIDlFSRGSILLDCGEGTLGQLkRRYGLEgadeaVRNLRCIWISHIHADHHTGLARIL 653
Cdd:COG1234    1 MKLTFLGTGGAVPTPGRATSSYLLE-AGGERLLIDCGEGTQRQL-LRAGLD-----PRDIDAIFITHLHGDHIAGLPGLL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 654 ARRRelLKGLAhEPAIVVGPRSLKNFLDAYQRLEDLDMEF-LDCRNTTttswasvetsrpekntssgnaEGSLFSKGSLm 732
Cdd:COG1234   74 STRS--LAGRE-KPLTIYGPPGTKEFLEALLKASGTDLDFpLEFHEIE---------------------PGEVFEIGGF- 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 733 qsiykrpsspltdnssalpflkklkkvlgemgleHLISFPVVHCPQAFGVSLkaaerkniagdEIPGWKMVYSGDTRPCP 812
Cdd:COG1234  129 ----------------------------------TVTAFPLDHPVPAYGYRF-----------EEPGRSLVYSGDTRPCE 163

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 813 EMVEASKGATVLIHEATFEDALVEEAVAKNHSTTKEAIKVGSSAGVYRTVLTHFSQRYPKI-PVIDESHMH---NTCIAF 888
Cdd:COG1234  164 ALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDDPeELLAEARAVfpgPVELAE 243


                 ....*.
gi 145338580 889 DMMSIN 894
Cdd:COG1234  244 DGMVIE 249
PRK00055 PRK00055
ribonuclease Z; Reviewed
 574-893 1.64e-48

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 173.44  E-value: 1.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 574 MEIVLLGTGSSQPSKYRNVTAIYIDLFSRGsILLDCGEGTLGQLkRRYGLegadeAVRNLRCIWISHIHADHHTGLARIL 653
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGGEL-FLFDCGEGTQRQL-LKTGI-----KPRKIDKIFITHLHGDHIFGLPGLL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 654 ARR----REllkglahEPAIVVGPRSLKNFLDAYQRLedldmefldcrnTTTTSWASVETSRP-----EKNTSSGNAEGs 724
Cdd:PRK00055  75 STRslsgRT-------EPLTIYGPKGIKEFVETLLRA------------SGSLGYRIAEKDKPgkldaEKLKALGVPPG- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 725 lfskgslmqsiykrpsspltdnssalPFLKKLKKvlgemglehlisfpvvhcpqafGVSLKAAERKNIAGDEI-----PG 799
Cdd:PRK00055 135 --------------------------PLFGKLKR----------------------GEDVTLEDGRIINPADVlgpprKG 166

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 800 WKMVYSGDTRPCPEMVEASKGATVLIHEATFEDALVEEAVAKNHSTTKEAIKVGSSAGVYRTVLTHFSQRYPKipviDES 879
Cdd:PRK00055 167 RKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYTG----DPE 242

                        330       340
                 ....*....|....*....|..
gi 145338580 880 HMH--------NTCIAFDMMSI 893
Cdd:PRK00055 243 ELLkeareifpNTELAEDLMRV 264
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 576-893 1.09e-47

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: 1.09e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 576 IVLLGTGSSQPSKYRNVTAIYIDLFSRGsILLDCGEGTLGQLkRRYGLegadeAVRNLRCIWISHIHADHHTGLARILAR 655
Cdd:cd07717    1 LTFLGTGSAVPTPERNLSSIALRLEGEL-WLFDCGEGTQRQL-LRAGL-----SPSKIDRIFITHLHGDHILGLPGLLST 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 656 RrellkGLAH--EPAIVVGPRSLKNFLDAYQRLEDLDMEFldcrnttTTSWASVETSrpekntssgnaEGSLFSKGSLmq 733
Cdd:cd07717   74 M-----SLLGrtEPLTIYGPKGLKEFLETLLRLSASRLPY-------PIEVHELEPD-----------PGLVFEDDGF-- 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 734 siykrpsspltdnssalpflkklkkvlgemgleHLISFPVVHCPQAFGVSLKaaERKniagdeipgwKMVYSGDTRPCPE 813
Cdd:cd07717  129 ---------------------------------TVTAFPLDHRVPCFGYRFE--EGR----------KIAYLGDTRPCEG 163

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 814 MVEASKGATVLIHEATFEDALVEEAVAKNHSTTKEAIKVGSSAGVYRTVLTHFSQRYPKI-PVIDE--SHMHNTCIAFDM 890
Cdd:cd07717  164 LVELAKGADLLIHEATFLDDDAEKAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARYKDPeELLKEarAVFPNTILAEDF 243


                 ...
gi 145338580 891 MSI 893
Cdd:cd07717  244 MTI 246
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 575-894 9.31e-45

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: 163.54  E-value: 9.31e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580  575 EIVLLGTGSSQPSKYRNVTAIYIDLFSRGsILLDCGEGTLGQLkRRYGLegadeAVRNLRCIWISHIHADHHTGLARILA 654
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLNGEL-WLFDCGEGTQRQM-LRSGI-----SPMKIDRIFITHLHGDHILGLPGLLS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580  655 RRrELLKGlaHEPAIVVGPRSLKNFLD----------AY-----------QRLEDLDME---FLDCRNTTTTSWASVETS 710
Cdd:TIGR02651  74 TM-SFQGR--KEPLTIYGPPGIKEFIEtslrvsytylNYpikiheieeggLVFEDDGFKveaFPLDHSIPSLGYRFEEKD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580  711 RPEKNtssgNAEGSLFskgslmqsiYKRPSSPLtdnssalpfLKKLKKvlGEmglehlisfpVVHCPQafGVSLKAAErk 790
Cdd:TIGR02651 151 RPGKF----DREKAKE---------LGIPPGPL---------YGKLKR--GE----------TVTLID--GRIIDPED-- 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580  791 nIAGDEIPGWKMVYSGDTRPCPEMVEASKGATVLIHEATFEDALVEEAVAKNHSTTKEAIKVGSSAGVYRTVLTHFSQRY 870
Cdd:TIGR02651 193 -VLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY 271

                         330       340
                  ....*....|....*....|....*..
gi 145338580  871 PKIPVIDE---SHMHNTCIAFDMMSIN 894
Cdd:TIGR02651 272 SDEEELLEeakKIFPNTYIAEDFMEIE 298
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 576-828 1.25e-29

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: 116.21  E-value: 1.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 576 IVLLGTGSSQPSKYRNVTAIYIDLFSrGSILLDCGEGTLGQLkRRYGLegadeAVRNLRCIWISHIHADHHTGLARILAR 655
Cdd:cd16272    1 LTFLGTGGAVPSLTRNTSSYLLETGG-TRILLDCGEGTVYRL-LKAGV-----DPDKLDAIFLSHFHLDHIGGLPTLLFA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 656 RRELLKGlahEPAIVVGPRSLKNFLDAyqrledldmeFLDCRNTTTTSWASVEtsrpekntssgnaegslfskgslmqsi 735
Cdd:cd16272   74 RRYGGRK---KPLTIYGPKGIKEFLEK----------LLNFPVEILPLGFPLE--------------------------- 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 736 ykrpsspltdnssaLPFLKKLKKVLgEMGLEHLISFPVVHCPQAFGVSLkaaerkniagdEIPGWKMVYSGDTRPCPEMV 815
Cdd:cd16272  114 --------------IEELEEGGEVL-ELGDLKVEAFPVKHSVESLGYRI-----------EAEGKSIVYSGDTGPCENLV 167

                        250
                 ....*....|...
gi 145338580 816 EASKGATVLIHEA 828
Cdd:cd16272  168 ELAKGADLLIHEC 180
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 132-188 1.03e-16

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: 74.93  E-value: 1.03e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145338580  132 QILGTgmDTQDTS-PSVLLFFDKQRFIF-NAGEGLQRFCTEHKIKLSKVDHIFLSRVCS 188
Cdd:pfam13691   1 QVVTT--PTADTPgPLLLLHFDSKRYLFgNVGEGTQRALNEQKVRLSKLEDIFLTGKVS 57
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 578-843 1.16e-16

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: 79.23  E-value: 1.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 578 LLGTGSSQPSKYRNVTAIYIDlFSRGSILLDCGEGTLGQLKRrYGLEGADeavrnLRCIWISHIHADHHTGL------AR 651
Cdd:cd07740    2 FLGSGDAFGSGGRLNTCFHVA-SEAGRFLIDCGASSLIALKR-AGIDPNA-----IDAIFITHLHGDHFGGLpfflldAQ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 652 ILARRRellkglahEPAIVVGPRSLKnflDAYQRLedldMEfldcrntTTTSWASVETSRPEkntssgnaegslfskgsl 731
Cdd:cd07740   75 FVAKRT--------RPLTIAGPPGLR---ERLRRA----ME-------ALFPGSSKVPRRFD------------------ 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 732 MQSIYKRPSSPLTdnssalpflkklkkvlgeMGLEHLISFPVVHCPQAFGVSLK-AAERKNIAgdeipgwkmvYSGDTRP 810
Cdd:cd07740  115 LEVIELEPGEPTT------------------LGGVTVTAFPVVHPSGALPLALRlEAAGRVLA----------YSGDTEW 166

                        250       260       270
                 ....*....|....*....|....*....|...
gi 145338580 811 CPEMVEASKGATVLIHEATFedalVEEAVaKNH 843
Cdd:cd07740  167 TDALVPLARGADLFICECYF----FEKKV-PGH 194
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 574-893 4.05e-14

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 73.39  E-value: 4.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 574 MEIVLLGTGSSQPS---------------KY-RNVTAIYIDlFSRGSILLDCGEGTLGQLKRryglegADEAVRNLRCIW 637
Cdd:COG1235    1 MKVTFLGSGSSGGVpqigcdcpvcastdpRYgRTRSSILVE-ADGTRLLIDAGPDLREQLLR------LGLDPSKIDAIL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 638 ISHIHADHHTGLarilarrRELLKGLAHEPAIVVGPRSLKNFLDayQRLEDLDMEFLDCRNTTTTswasvetsrpeknts 717
Cdd:COG1235   74 LTHEHADHIAGL-------DDLRPRYGPNPIPVYATPGTLEALE--RRFPYLFAPYPGKLEFHEI--------------- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 718 sgnaegslfskgslmqsiykRPSSPLTdnssalpflkklkkvLGEMGLEhliSFPVVH-CPQAFGVSLkaaerkniagdE 796
Cdd:COG1235  130 --------------------EPGEPFE---------------IGGLTVT---PFPVPHdAGDPVGYRI-----------E 160

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 797 IPGWKMVYSGDT-RPCPEMVEASKGATVLIHEATFEDalvEEAvakNHSTTKEAIKVGSSAGVYRTVLTHFSQRYPKiPV 875
Cdd:COG1235  161 DGGKKLAYATDTgYIPEEVLELLRGADLLILDATYDD---PEP---GHLSNEEALELLARLGPKRLVLTHLSPDNND-HE 233

                        330       340
                 ....*....|....*....|....
gi 145338580 876 IDESHM------HNTCIAFDMMSI 893
Cdd:COG1235  234 LDYDELeaallpAGVEVAYDGMEI 257
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 575-826 2.12e-13

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: 69.85  E-value: 2.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 575 EIVLLGTGS-------SQPSkyrnvTAIYIDlfsrG-SILLDCGEGTLgqlkRRYGLEGADeaVRNLRCIWISHIHADHH 646
Cdd:cd07719    1 RVTLLGTGGpipdpdrAGPS-----TLVVVG----GrVYLVDAGSGVV----RRLAQAGLP--LGDLDAVFLTHLHSDHV 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 647 TGLARILARRrelLKGLAHEPAIVVGPRSLKNFLDAYQRLEDLDmefLDCRNttttswasvetsrpekntssGNAEGSLF 726
Cdd:cd07719   66 ADLPALLLTA---WLAGRKTPLPVYGPPGTRALVDGLLAAYALD---IDYRA--------------------RIGDEGRP 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 727 SKGSLMQSI-YKRPSSPLTDNssalpflkKLKkvlgemglehlIS-FPVVH--CPQAFG--VslkaaerkniagdEIPGW 800
Cdd:cd07719  120 DPGALVEVHeIAAGGVVYEDD--------GVK-----------VTaFLVDHgpVPPALAyrF-------------DTPGR 167

                        250       260
                 ....*....|....*....|....*.
gi 145338580 801 KMVYSGDTRPCPEMVEASKGATVLIH 826
Cdd:cd07719  168 SVVFSGDTGPSENLIELAKGADLLVH 193
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 603-828 9.59e-12

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: 64.39  E-value: 9.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 603 GSILLDCGEGTLGQLKRRYGLEGADeAVrnlrciWISHIHADH---HTGL--ARILARRREllkglAHEPAIVVGPRSLk 677
Cdd:cd07716   28 FRILLDCGSGVLSRLQRYIDPEDLD-AV------VLSHLHPDHcadLGVLqyARRYHPRGA-----RKPPLPLYGPAGP- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 678 nfLDAYQRLEDLDMEFldcrntTTTSWasvetsrpekntssgnaegslfskgslmqsiykRPSSPLTdnssalpflkklk 757
Cdd:cd07716   95 --AERLAALYGLEDVF------DFHPI---------------------------------EPGEPLE------------- 120

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145338580 758 kvLGEMGLEhliSFPVVHCPQAFGVSLKAAERKniagdeipgwkMVYSGDTRPCPEMVEASKGATVLIHEA 828
Cdd:cd07716  121 --IGPFTIT---FFRTVHPVPCYAMRIEDGGKV-----------LVYTGDTGYCDELVEFARGADLLLCEA 175
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 131-363 8.89e-10

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: 58.81  E-value: 8.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 131 VQILGTGmdTQDTSPSVLLFFDKQRFIFNAGEGLQRFCTEHKIKLSKVDHIFLSRVCSEtagglpgllltlagigeqgls 210
Cdd:cd16296    1 LQVVAAG--SRDMGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWS--------------------- 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 211 vNVWGPSDLKYLVDAMRsfIPRAAMVhtrsfGPSLNISDSAPQIGLSKPKDDAYVlvddevvkisaillepsrleesgsk 290
Cdd:cd16296   58 -NVGGLSGMILTLKETG--LPKCVLS-----GPNKQSPDKIGVRRQILERDPSLV------------------------- 104

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145338580 291 pgetaVIYVCELPEIKGKFDPKKAMALGLRAG-----PKYSYLQSGQSVKSDFKDITVHpsDVMGPSVPGPVVLLVDC 363
Cdd:cd16296  105 -----VAFICKLHLKKGNFLVLKAKELGLPVGtaaiaPIIAAVKDGKSITFEGREILAE--ELCTPPDPGIVFIVVEC 175
PRK02126 PRK02126
ribonuclease Z; Provisional
 594-870 3.60e-08

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 56.46  E-value: 3.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 594 AIYID-LFSRGSILLDCGEgtLGQLKRRyglegadeAVRNLRCIWISHIHADHHTG---LARI-LAR-RRELLKG----- 662
Cdd:PRK02126  18 GLYVDfLFERRALLFDLGD--LHHLPPR--------ELLRISHIFVSHTHMDHFIGfdrLLRHcLGRpRRLRLFGppgfa 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 663 --LAHEpaivvgprsLK----NFLDAYQ---RLEDldMEFLDCRnTTTTSWASVETSRPEKNTSSGNAEGSLFSKG---- 729
Cdd:PRK02126  88 dqVEHK---------LAgytwNLVENYPttfRVHE--VELHDGR-IRRALFSCRRAFAREAEEELSLPDGVLLDEPwfrv 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 730 ----------SLMQSIYKRPSspLTDNSSAL--------PFLKKLKKVL--GEMGLEhlisfPVVHCPQAFG----VSLK 785
Cdd:PRK02126 156 raafldhgipCLAFALEEKAH--INIDKNRLaelglppgPWLRELKHAVlrGEPDDT-----PIRVLWRDGGgeheRVRP 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 786 AAERKNIAGDEIPGWKMVYSGDTRPCPE----MVEASKGATVLIHEATFEDALVEEAVAKNHSTTKEAIKVGSSAGVYRT 861
Cdd:PRK02126 229 LGELKERVLRIEPGQKIGYVTDIGYTEEnlarIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRL 308


                 ....*....
gi 145338580 862 VLTHFSQRY 870
Cdd:PRK02126 309 LPFHFSPRY 317
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
131-184 7.75e-07

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 51.35  E-value: 7.75e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145338580 131 VQILGTG--MDTQDT-SPSVLLFFDKQRFIFNAGEGLQRFCTEHKIKLSKVDHIFLS 184
Cdd:COG1234    3 LTFLGTGgaVPTPGRaTSSYLLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFIT 59
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 796-866 5.98e-05

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: 44.99  E-value: 5.98e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145338580  796 EIPGWKMVYSGDTRPCPEMVEAS-KGATVLIHEATFEDAlvEEAVAKNHSTTKEAIKVGSSAGVYRTVLTHF 866
Cdd:pfam12706 127 EGPGKRVYYAGDTGYFPDEIGERlGGADLLLLDGGAWRD--DEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK14866 PRK14866
hypothetical protein; Provisional
 308-349 2.58e-04

hypothetical protein; Provisional


Pssm-ID: 237840  Cd Length: 451  Bit Score: 44.61  E-value: 2.58e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 145338580 308 KFDPKKAMALGLRAGPKYSYLQSGQSVKSDfkDITVHPSDVM 349
Cdd:PRK14866 397 RFDPELARKLGVPEGPAFGKLAAGQPVEVD--GETITPEMVH 436
PRK00055 PRK00055
ribonuclease Z; Reviewed
 131-355 6.55e-04

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 42.48  E-value: 6.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 131 VQILGTG--MDTQDTS-PSVLLFFDKQRFIFNAGEGLQRFCTEHKIKLSKVDHIFLSRVCSETAGGLPGLLltlAGIGEQ 207
Cdd:PRK00055   4 LTFLGTGsgVPTPTRNvSSILLRLGGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLL---STRSLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 208 GLS--VNVWGPSDLKYLVDAMRSFipraamvhTRSFGpslnisdsapqiglskpkddaYvlvddevvkisaillepsRLE 285
Cdd:PRK00055  81 GRTepLTIYGPKGIKEFVETLLRA--------SGSLG---------------------Y------------------RIA 113

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 286 EsgskpgetaviyvcelPEIKGKFDPKKAMALGLRAGPKYSYLQSGQSVKSDFKDItVHPSDVMGPSVPG 355
Cdd:PRK00055 114 E----------------KDKPGKLDAEKLKALGVPPGPLFGKLKRGEDVTLEDGRI-INPADVLGPPRKG 166
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 603-655 9.43e-04

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 41.00  E-value: 9.43e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 145338580   603 GSILLDCGEGTLGQLKRRYGLEGadeaVRNLRCIWISHIHADHHTGLARILAR 655
Cdd:smart00849  10 GAILIDTGPGEAEDLLAELKKLG----PKKIDAIILTHGHPDHIGGLPELLEA 58
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 131-184 1.51e-03

Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 40.71  E-value: 1.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145338580 131 VQILGTG--MDTQD-TSPSVLLFFDKQRFIFNAGEGLQRFCTEHKIKLSKVDHIFLS 184
Cdd:cd16272    1 LTFLGTGgaVPSLTrNTSSYLLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLS 57
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 574-645 2.03e-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: 40.53  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338580 574 MEIVLLGTGSSQ-------------PSKYRNV---TAIYIDLFSRgSILLDCG----EgtlgQLKRryglegadEAVRNL 633
Cdd:cd16279    1 MKLTFLGTGTSSgvpvigcdcgvcdSSDPKNRrlrSSILIETGGK-NILIDTGpdfrQ----QALR--------AGIRKL 67

                         90
                 ....*....|..
gi 145338580 634 RCIWISHIHADH 645
Cdd:cd16279   68 DAVLLTHAHADH 79
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
591-666 2.13e-03

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 40.43  E-value: 2.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145338580  591 NVTAIYIDlfsRGSILLDCGEGTLGQLKRRYGLEGADeaVRNLRCIWISHIHADhHTGLARILARRRELLKGLAHE 666
Cdd:pfam00753   7 NSYLIEGG---GGAVLIDTGGSAEAALLLLLAALGLG--PKDIDAVILTHGHFD-HIGGLGELAEATDVPVIVVAE 76
 
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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