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Conserved domains on  [gi|1958656769|ref|XP_038941246|]
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zinc phosphodiesterase ELAC protein 2 isoform X1 [Rattus norvegicus]

Protein Classification

ribonuclease Z( domain architecture ID 10869915)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 111-316 1.52e-107

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: 316.80  E-value: 1.52e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 111 IVFLGTGSAIPMKIRNVSSTLVNLSPDKSVLLDCGEGTFGQLCRHYGQQ-IDRVLCNLTAVFVSHLHADHHTGLLNILLQ 189
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 190 REHALAslgKPFQPLLVVAPTQLRAWLQQYHNQCQEILHHISMIPAKCLQKGAEVPSPPVERLISLLLETCDLQEFQTCL 269
Cdd:cd07718    81 RKKLFK---PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKSIETVP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958656769 270 VRHCKHAFGCALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEAT 316
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; ...
 286-358 9.05e-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: 41.05  E-value: 9.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656769 286 GWKVVYSGDTMP----CEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAIGVGMRMNAEFIMLNHFSQRYA 358
Cdd:PRK02126  242 GQKIGYVTDIGYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQ 318
 
Name Accession Description Interval E-value
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 111-316 1.52e-107

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: 316.80  E-value: 1.52e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 111 IVFLGTGSAIPMKIRNVSSTLVNLSPDKSVLLDCGEGTFGQLCRHYGQQ-IDRVLCNLTAVFVSHLHADHHTGLLNILLQ 189
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 190 REHALAslgKPFQPLLVVAPTQLRAWLQQYHNQCQEILHHISMIPAKCLQKGAEVPSPPVERLISLLLETCDLQEFQTCL 269
Cdd:cd07718    81 RKKLFK---PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKSIETVP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958656769 270 VRHCKHAFGCALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEAT 316
Cdd:cd07718   158 VIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
110-380 1.45e-49

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 169.22  E-value: 1.45e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 110 EIVFLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHygqQIDrvLCNLTAVFVSHLHADHHTGLLNILLQ 189
Cdd:COG1234     2 KLTFLGTGGAVPTPGRATSSYLLE-AGGERLLIDCGEGTQRQLLRA---GLD--PRDIDAIFITHLHGDHIAGLPGLLST 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 190 RehalaSLGKPFQPLLVVAPTQLRAWLQQYHNQCQEILH-HISMIPakcLQKGAEVPSPPVErlisllletcdlqeFQTC 268
Cdd:COG1234    76 R-----SLAGREKPLTIYGPPGTKEFLEALLKASGTDLDfPLEFHE---IEPGEVFEIGGFT--------------VTAF 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 269 LVRHCKHAFGcALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAIGVGMRMNAEFI 348
Cdd:COG1234   134 PLDHPVPAYG-YRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVKRL 212

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958656769 349 MLNHFSQRYAKIPLF----SPDFNEKVGIAFDHMKV 380
Cdd:COG1234   213 VLTHFSPRYDDPEELlaeaRAVFPGPVELAEDGMVI 248
PRK00055 PRK00055
ribonuclease Z; Reviewed
 110-357 2.96e-42

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 150.72  E-value: 2.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 110 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRVlcnltavFVSHLHADHHTGLLNI 186
Cdd:PRK00055    3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQL-LKTGikpRKIDKI-------FITHLHGDHIFGLPGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 187 LLQRehalaSLGKPFQPLLVVAPtqlrAWLQQYHNQCQEILHHIS----------MIPAKCLQKGAEVPSPPVERLisll 256
Cdd:PRK00055   74 LSTR-----SLSGRTEPLTIYGP----KGIKEFVETLLRASGSLGyriaekdkpgKLDAEKLKALGVPPGPLFGKL---- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 257 letcdlQEFQTCLV---RHCKHAFGCALVHSsGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTT 333
Cdd:PRK00055  141 ------KRGEDVTLedgRIINPADVLGPPRK-GRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEELAKEYGHSTA 213

                         250       260
                  ....*....|....*....|....
gi 1958656769 334 SQAIGVGMRMNAEFIMLNHFSQRY 357
Cdd:PRK00055  214 RQAAEIAKEAGVKRLILTHFSPRY 237
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 110-357 1.55e-34

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: 130.80  E-value: 1.55e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 110 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRVlcnltavFVSHLHADHHTGLLNI 186
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-NGELWLFDCGEGTQRQM-LRSGispMKIDRI-------FITHLHGDHILGLPGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 187 LLQRehalaSLGKPFQPLLVVAPtqlrawlqqyhnqcQEILHHISMIpakcLQKGAEVPSPPVErlISLLLETCDLQEF- 265
Cdd:TIGR02651  72 LSTM-----SFQGRKEPLTIYGP--------------PGIKEFIETS----LRVSYTYLNYPIK--IHEIEEGGLVFEDd 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 266 ----QTCLVRHCKHAFGCALV-------------------------------------------------HSSGWKVVYS 292
Cdd:TIGR02651 127 gfkvEAFPLDHSIPSLGYRFEekdrpgkfdrekakelgippgplygklkrgetvtlidgriidpedvlgpPRKGRKIAYT 206

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656769 293 GDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAIGVGMRMNAEFIMLNHFSQRY 357
Cdd:TIGR02651 207 GDTRPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY 271
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 140-353 2.17e-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: 48.07  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 140 VLLDCGEGTFGQL------CRHYGQQIDrvlcnltAVFVSHLHADHHTGLLNIllqrehalaslgKPFQPLLVVAP---- 209
Cdd:pfam12706   3 ILIDPGPDLRQQAlpalqpGRLRDDPID-------AVLLTHDHYDHLAGLLDL------------REGRPRPLYAPlgvl 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 210 TQLRAW------LQQYHNQCQEI-----------LHHISMIPAKclQKGAEVPSPPVERLISLLLETcdlqefqtclvrh 272
Cdd:pfam12706  64 AHLRRNfpylflLEHYGVRVHEIdwgesftvgdgGLTVTATPAR--HGSPRGLDPNPGDTLGFRIEG------------- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 273 ckhafgcalvhsSGWKVVYSGDTMPCEALV-QMGKDATLLIHEATLEDglEEEAVEKTHSTTSQAIGVGMRMNAEFIMLN 351
Cdd:pfam12706 129 ------------PGKRVYYAGDTGYFPDEIgERLGGADLLLLDGGAWR--DDEMIHMGHMTPEEAVEAAADLGARRKVLI 194


                  ..
gi 1958656769 352 HF 353
Cdd:pfam12706 195 HI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 128-319 6.01e-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: 46.39  E-value: 6.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769  128 SSTLVNlSPDKSVLLDCGEGTFGQLCRHYGQQIDRvlcNLTAVFVSHLHADhHTGLLNILLQREHAlaslgkpfqplLVV 207
Cdd:smart00849   1 NSYLVR-DDGGAILIDTGPGEAEDLLAELKKLGPK---KIDAIILTHGHPD-HIGGLPELLEAPGA-----------PVY 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769  208 APTQLRAWLQQYHNQCQEILHHI-SMIPAKCLQKGAEVpsppverlisllletcDLQEFQTCLVRHCKHAFGCALVHSSG 286
Cdd:smart00849  65 APEGTAELLKDLLALLGELGAEAePAPPDRTLKDGDEL----------------DLGGGELEVIHTPGHTPGSIVLYLPE 128

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1958656769  287 WKVVYSGDTMPCEALVQMGKDATLLIHEATLED 319
Cdd:smart00849 129 GKILFTGDLLFAGGDGRTLVDGGDAAASDALES 161
PRK02126 PRK02126
ribonuclease Z; Provisional
 286-358 9.05e-04

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 41.05  E-value: 9.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656769 286 GWKVVYSGDTMP----CEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAIGVGMRMNAEFIMLNHFSQRYA 358
Cdd:PRK02126  242 GQKIGYVTDIGYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQ 318
 
Name Accession Description Interval E-value
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 111-316 1.52e-107

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: 316.80  E-value: 1.52e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 111 IVFLGTGSAIPMKIRNVSSTLVNLSPDKSVLLDCGEGTFGQLCRHYGQQ-IDRVLCNLTAVFVSHLHADHHTGLLNILLQ 189
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 190 REHALAslgKPFQPLLVVAPTQLRAWLQQYHNQCQEILHHISMIPAKCLQKGAEVPSPPVERLISLLLETCDLQEFQTCL 269
Cdd:cd07718    81 RKKLFK---PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKSIETVP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958656769 270 VRHCKHAFGCALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEAT 316
Cdd:cd07718   158 VIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
110-380 1.45e-49

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 169.22  E-value: 1.45e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 110 EIVFLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHygqQIDrvLCNLTAVFVSHLHADHHTGLLNILLQ 189
Cdd:COG1234     2 KLTFLGTGGAVPTPGRATSSYLLE-AGGERLLIDCGEGTQRQLLRA---GLD--PRDIDAIFITHLHGDHIAGLPGLLST 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 190 RehalaSLGKPFQPLLVVAPTQLRAWLQQYHNQCQEILH-HISMIPakcLQKGAEVPSPPVErlisllletcdlqeFQTC 268
Cdd:COG1234    76 R-----SLAGREKPLTIYGPPGTKEFLEALLKASGTDLDfPLEFHE---IEPGEVFEIGGFT--------------VTAF 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 269 LVRHCKHAFGcALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAIGVGMRMNAEFI 348
Cdd:COG1234   134 PLDHPVPAYG-YRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVKRL 212

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958656769 349 MLNHFSQRYAKIPLF----SPDFNEKVGIAFDHMKV 380
Cdd:COG1234   213 VLTHFSPRYDDPEELlaeaRAVFPGPVELAEDGMVI 248
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 111-357 3.80e-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: 162.62  E-value: 3.80e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 111 IVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYGqqidRVLCNLTAVFVSHLHADHHTGLLNILlqr 190
Cdd:cd07717     1 LTFLGTGSAVPTPERNLSSIALRL-EGELWLFDCGEGTQRQL-LRAG----LSPSKIDRIFITHLHGDHILGLPGLL--- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 191 ehALASLGKPFQPLLVVAPTQLRAWLQQYHNQCQ-----EILHHismipakclqkgaEVPSPPVErlislLLETCDLQeF 265
Cdd:cd07717    72 --STMSLLGRTEPLTIYGPKGLKEFLETLLRLSAsrlpyPIEVH-------------ELEPDPGL-----VFEDDGFT-V 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 266 QTCLVRHCKHAFGCALVhsSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAIGVGMRMNA 345
Cdd:cd07717   131 TAFPLDHRVPCFGYRFE--EGRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKAKETGHSTAKQAAEIAKKAGV 208

                         250
                  ....*....|..
gi 1958656769 346 EFIMLNHFSQRY 357
Cdd:cd07717   209 KKLVLTHFSARY 220
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 111-315 2.12e-42

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: 148.18  E-value: 2.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 111 IVFLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHyGQQIDRvlcnLTAVFVSHLHADHHTGLLNILLQR 190
Cdd:cd16272     1 LTFLGTGGAVPSLTRNTSSYLLE-TGGTRILLDCGEGTVYRLLKA-GVDPDK----LDAIFLSHFHLDHIGGLPTLLFAR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 191 EhalasLGKPFQPLLVVAPTQLRAWLQQYHNQCQEILHHismipakclqkgaevPSPPVERLISLLLETCDLQEF--QTC 268
Cdd:cd16272    75 R-----YGGRKKPLTIYGPKGIKEFLEKLLNFPVEILPL---------------GFPLEIEELEEGGEVLELGDLkvEAF 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958656769 269 LVRHCKHAFGCALvHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEA 315
Cdd:cd16272   135 PVKHSVESLGYRI-EAEGKSIVYSGDTGPCENLVELAKGADLLIHEC 180
PRK00055 PRK00055
ribonuclease Z; Reviewed
 110-357 2.96e-42

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 150.72  E-value: 2.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 110 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRVlcnltavFVSHLHADHHTGLLNI 186
Cdd:PRK00055    3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQL-LKTGikpRKIDKI-------FITHLHGDHIFGLPGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 187 LLQRehalaSLGKPFQPLLVVAPtqlrAWLQQYHNQCQEILHHIS----------MIPAKCLQKGAEVPSPPVERLisll 256
Cdd:PRK00055   74 LSTR-----SLSGRTEPLTIYGP----KGIKEFVETLLRASGSLGyriaekdkpgKLDAEKLKALGVPPGPLFGKL---- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 257 letcdlQEFQTCLV---RHCKHAFGCALVHSsGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTT 333
Cdd:PRK00055  141 ------KRGEDVTLedgRIINPADVLGPPRK-GRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEELAKEYGHSTA 213

                         250       260
                  ....*....|....*....|....
gi 1958656769 334 SQAIGVGMRMNAEFIMLNHFSQRY 357
Cdd:PRK00055  214 RQAAEIAKEAGVKRLILTHFSPRY 237
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 110-357 1.55e-34

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: 130.80  E-value: 1.55e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 110 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRVlcnltavFVSHLHADHHTGLLNI 186
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-NGELWLFDCGEGTQRQM-LRSGispMKIDRI-------FITHLHGDHILGLPGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 187 LLQRehalaSLGKPFQPLLVVAPtqlrawlqqyhnqcQEILHHISMIpakcLQKGAEVPSPPVErlISLLLETCDLQEF- 265
Cdd:TIGR02651  72 LSTM-----SFQGRKEPLTIYGP--------------PGIKEFIETS----LRVSYTYLNYPIK--IHEIEEGGLVFEDd 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 266 ----QTCLVRHCKHAFGCALV-------------------------------------------------HSSGWKVVYS 292
Cdd:TIGR02651 127 gfkvEAFPLDHSIPSLGYRFEekdrpgkfdrekakelgippgplygklkrgetvtlidgriidpedvlgpPRKGRKIAYT 206

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656769 293 GDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAIGVGMRMNAEFIMLNHFSQRY 357
Cdd:TIGR02651 207 GDTRPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY 271
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 110-313 5.20e-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: 96.05  E-value: 5.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 110 EIVFLGTGSAIPMKIRNVSSTLVnLSPDKSVLLDCGEGTFGQLCRHyGQQIDRvlcnLTAVFVSHLHADHHTGLLNILLQ 189
Cdd:cd07719     1 RVTLLGTGGPIPDPDRAGPSTLV-VVGGRVYLVDAGSGVVRRLAQA-GLPLGD----LDAVFLTHLHSDHVADLPALLLT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 190 REHALASlgkpfQPLLVVAPTQLRAW----LQQYHnqcQEILHHISMIPAKCLQKGA-----EVPSPPVerlislLLETC 260
Cdd:cd07719    75 AWLAGRK-----TPLPVYGPPGTRALvdglLAAYA---LDIDYRARIGDEGRPDPGAlvevhEIAAGGV------VYEDD 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656769 261 DLQeFQTCLVRH--CKHAFgcAL-VHSSGWKVVYSGDTMPCEALVQMGKDATLLIH 313
Cdd:cd07719   141 GVK-VTAFLVDHgpVPPAL--AYrFDTPGRSVVFSGDTGPSENLIELAKGADLLVH 193
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 113-315 3.95e-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: 82.31  E-value: 3.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 113 FLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRhygQQIDRVlcNLTAVFVSHLHADHHTGLLNILLQREH 192
Cdd:cd07740     2 FLGSGDAFGSGGRLNTCFHVA-SEAGRFLIDCGASSLIALKR---AGIDPN--AIDAIFITHLHGDHFGGLPFFLLDAQF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 193 ALaslgKPFQPLLVVAPTQLRAWLQQyhnqCQEILH-HISMIPAKclqkgAEVPSPPVERLISLLLETCDLQEFQtclVR 271
Cdd:cd07740    76 VA----KRTRPLTIAGPPGLRERLRR----AMEALFpGSSKVPRR-----FDLEVIELEPGEPTTLGGVTVTAFP---VV 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958656769 272 HCKHAFGCALVHSSGWKVV-YSGDTMPCEALVQMGKDATLLIHEA 315
Cdd:cd07740   140 HPSGALPLALRLEAAGRVLaYSGDTEWTDALVPLARGADLFICEC 184
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 128-315 5.86e-18

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: 81.33  E-value: 5.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 128 SSTLVNlSPDKSVLLDCGEGTFGQLCRHygqqIDrvLCNLTAVFVSHLHADHHTGLlnILLQREHALASLGKPFQPLLVV 207
Cdd:cd07716    19 SGYLLE-ADGFRILLDCGSGVLSRLQRY----ID--PEDLDAVVLSHLHPDHCADL--GVLQYARRYHPRGARKPPLPLY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 208 APTQLRAWLQQ-YHNQCQEILHHIsmipakclqkgaEVPSPpverlisllLETCDLqEFQTCLVRHCKHAFGCALVHSSG 286
Cdd:cd07716    90 GPAGPAERLAAlYGLEDVFDFHPI------------EPGEP---------LEIGPF-TITFFRTVHPVPCYAMRIEDGGK 147

                         170       180
                  ....*....|....*....|....*....
gi 1958656769 287 wKVVYSGDTMPCEALVQMGKDATLLIHEA 315
Cdd:cd07716   148 -VLVYTGDTGYCDELVEFARGADLLLCEA 175
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 110-380 9.04e-15

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 74.16  E-value: 9.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 110 EIVFLGTGSAIPM----------------KIRNVSSTLVNlSPDKSVLLDCGEGtFGQLCRHYGQQIDRvlcnLTAVFVS 173
Cdd:COG1235     2 KVTFLGSGSSGGVpqigcdcpvcastdprYGRTRSSILVE-ADGTRLLIDAGPD-LREQLLRLGLDPSK----IDAILLT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 174 HLHADHHTGLLNIllqREHALAslgkpfQPLLVVAPTQLRAWLQQYHNQCQEilHHISMIPAKCLQKGAEVpsppverli 253
Cdd:COG1235    76 HEHADHIAGLDDL---RPRYGP------NPIPVYATPGTLEALERRFPYLFA--PYPGKLEFHEIEPGEPF--------- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 254 slllETCDLqEFQTCLVRH-CKHAFGCaLVHSSGWKVVYSGDT-MPCEALVQMGKDATLLIHEATLEDGleeeavEKTHS 331
Cdd:COG1235   136 ----EIGGL-TVTPFPVPHdAGDPVGY-RIEDGGKKLAYATDTgYIPEEVLELLRGADLLILDATYDDP------EPGHL 203

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958656769 332 TTSQAIGVGMRMNAEFIMLNHFSQRYAKIPLF-----SPDFNEKVGIAFDHMKV 380
Cdd:COG1235   204 SNEEALELLARLGPKRLVLTHLSPDNNDHELDydeleAALLPAGVEVAYDGMEI 257
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 140-353 2.17e-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: 48.07  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 140 VLLDCGEGTFGQL------CRHYGQQIDrvlcnltAVFVSHLHADHHTGLLNIllqrehalaslgKPFQPLLVVAP---- 209
Cdd:pfam12706   3 ILIDPGPDLRQQAlpalqpGRLRDDPID-------AVLLTHDHYDHLAGLLDL------------REGRPRPLYAPlgvl 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 210 TQLRAW------LQQYHNQCQEI-----------LHHISMIPAKclQKGAEVPSPPVERLISLLLETcdlqefqtclvrh 272
Cdd:pfam12706  64 AHLRRNfpylflLEHYGVRVHEIdwgesftvgdgGLTVTATPAR--HGSPRGLDPNPGDTLGFRIEG------------- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 273 ckhafgcalvhsSGWKVVYSGDTMPCEALV-QMGKDATLLIHEATLEDglEEEAVEKTHSTTSQAIGVGMRMNAEFIMLN 351
Cdd:pfam12706 129 ------------PGKRVYYAGDTGYFPDEIgERLGGADLLLLDGGAWR--DDEMIHMGHMTPEEAVEAAADLGARRKVLI 194


                  ..
gi 1958656769 352 HF 353
Cdd:pfam12706 195 HI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 128-319 6.01e-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: 46.39  E-value: 6.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769  128 SSTLVNlSPDKSVLLDCGEGTFGQLCRHYGQQIDRvlcNLTAVFVSHLHADhHTGLLNILLQREHAlaslgkpfqplLVV 207
Cdd:smart00849   1 NSYLVR-DDGGAILIDTGPGEAEDLLAELKKLGPK---KIDAIILTHGHPD-HIGGLPELLEAPGA-----------PVY 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769  208 APTQLRAWLQQYHNQCQEILHHI-SMIPAKCLQKGAEVpsppverlisllletcDLQEFQTCLVRHCKHAFGCALVHSSG 286
Cdd:smart00849  65 APEGTAELLKDLLALLGELGAEAePAPPDRTLKDGDEL----------------DLGGGELEVIHTPGHTPGSIVLYLPE 128

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1958656769  287 WKVVYSGDTMPCEALVQMGKDATLLIHEATLED 319
Cdd:smart00849 129 GKILFTGDLLFAGGDGRTLVDGGDAAASDALES 161
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
125-295 3.03e-05

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 44.67  E-value: 3.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 125 RNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHYGQQIDRVLcNLTAVFVSHLHADhHTGLLNILLQRehalaslgkpFQPL 204
Cdd:pfam00753   4 GQVNSYLIE-GGGGAVLIDTGGSAEAALLLLLAALGLGPK-DIDAVILTHGHFD-HIGGLGELAEA----------TDVP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 205 LVVAPTQLRAWLQQYHNQCQEILHHISMIPakclqkgaeVPSPPVERLISLLLETCDLQEFqtcLVRHCK-HAFGCALVH 283
Cdd:pfam00753  71 VIVVAEEARELLDEELGLAASRLGLPGPPV---------VPLPPDVVLEEGDGILGGGLGL---LVTHGPgHGPGHVVVY 138

                         170
                  ....*....|..
gi 1958656769 284 SSGWKVVYSGDT 295
Cdd:pfam00753 139 YGGGKVLFTGDL 150
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 121-190 4.77e-04

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: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 41.33  E-value: 4.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958656769 121 PMKIRNVSSTLVnLSPDKSVLLDCgegtfgQLCRHYGQQ----IDRVLCNLTAVFVSHLHADHHTGlLNILLQR 190
Cdd:cd07739    10 EISSFPVTSTLI-YGETEAVLVDA------QFTRADAERladwIKASGKTLTTIYITHGHPDHYFG-LEVLLEA 75
PRK02126 PRK02126
ribonuclease Z; Provisional
 286-358 9.05e-04

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 41.05  E-value: 9.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958656769 286 GWKVVYSGDTMP----CEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAIGVGMRMNAEFIMLNHFSQRYA 358
Cdd:PRK02126  242 GQKIGYVTDIGYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQ 318
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 110-179 9.99e-04

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: 40.15  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 110 EIVFLGTGSA--IPM-----------KIRNV---SSTLVNlSPDKSVLLDCGEgTF-GQLCRHYGQQIDrvlcnltAVFV 172
Cdd:cd16279     2 KLTFLGTGTSsgVPVigcdcgvcdssDPKNRrlrSSILIE-TGGKNILIDTGP-DFrQQALRAGIRKLD-------AVLL 72


                  ....*..
gi 1958656769 173 SHLHADH 179
Cdd:cd16279    73 THAHADH 79
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 111-179 1.61e-03

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: 39.87  E-value: 1.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656769 111 IVFLGTGSA--IPMK-IRNVSSTLVNLsPDKSVLLDCGEGTFGQLCRHygqQIDRVlcNLTAVFVSHLHADH 179
Cdd:cd07741     1 IIFLGTGGGrfVVITqLRASGGIWIEL-NGKNIHIDPGPGALVRMCRP---KLDPT--KLDAIILSHRHLDH 66
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 131-300 1.84e-03

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


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 39.19  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 131 LVNLSPDKSVLLDCGEGTFGQLCRHygqqIDRVLCNLTAVFVSHLHADhHTGLLNILLQREHALASLGKPFQPLLVVAPT 210
Cdd:cd06262    14 LVSDEEGEAILIDPGAGALEKILEA----IEELGLKIKAILLTHGHFD-HIGGLAELKEAPGAPVYIHEADAELLEDPEL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 211 QLRAWLqqyhnqcqeilhhismipakclqkGAEVPSPPVERLIS----LLLETCDLQefqtclVRHCK-HAFGCALVHSS 285
Cdd:cd06262    89 NLAFFG------------------------GGPLPPPEPDILLEdgdtIELGGLELE------VIHTPgHTPGSVCFYIE 138

                         170
                  ....*....|....*
gi 1958656769 286 GWKVVYSGDTMPCEA 300
Cdd:cd06262   139 EEGVLFTGDTLFAGS 153
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 111-184 3.71e-03

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 38.59  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656769 111 IVFLG-----TGSAIpmkirnvsstLVNLsPDKSVLLDCG-----EGTFGQLCRHYGQQIDRvlcnLTAVFVSHLHADhH 180
Cdd:cd16295     1 LTFLGaarevTGSCY----------LLET-GGKRILLDCGlfqggKELEELNNEPFPFDPKE----IDAVILTHAHLD-H 64


                  ....
gi 1958656769 181 TGLL 184
Cdd:cd16295    65 SGRL 68
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 129-187 6.36e-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: 38.30  E-value: 6.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656769 129 STLVNLSPDKSVLLDCGEGTFGQLCRHY------GQQIDRvlcnLTAVFVSHLHADHHTGLLNIL 187
Cdd:COG2333    13 AILIRTPDGKTILIDTGPRPSFDAGERVvlpylrALGIRR----LDLLVLTHPDADHIGGLAAVL 73
 
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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