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Conserved domains on  [gi|1386806290|ref|NP_001349913|]
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zinc phosphodiesterase ELAC protein 2 isoform 4 [Mus musculus]

Protein Classification

RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold domain-containing protein( domain architecture ID 10869912)

RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold domain-containing protein

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 1.21e-106

Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme; this eukaryotic subgroup includes short forms (ELAC1) and the C-terminus of long forms including human ELAC2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


:

Pssm-ID: 293804 [Multi-domain]  Cd Length: 204  Bit Score: 314.49  E-value: 1.21e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 111 IVFLGTGSAIPMKIRNVSSTLVNLSPDKSVLLDCGEGTFGQLCRHYGQQ-IDRVLCSLTAVFVSHLHADHHTGLLNILLQ 189
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 190 REHALAslgKPFQPLLVVAPTQLRAWLQQYHNHCQEILHHVSMIPAKCLQKGAEVSNTTLERLISLLLETCDLEEFQTCL 269
Cdd:cd07718    81 RKKLFK---PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKSIETVP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1386806290 270 VRHCKHAFGCALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEAT 316
Cdd:cd07718   158 VIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
 
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 1.21e-106

Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme; this eukaryotic subgroup includes short forms (ELAC1) and the C-terminus of long forms including human ELAC2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293804 [Multi-domain]  Cd Length: 204  Bit Score: 314.49  E-value: 1.21e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 111 IVFLGTGSAIPMKIRNVSSTLVNLSPDKSVLLDCGEGTFGQLCRHYGQQ-IDRVLCSLTAVFVSHLHADHHTGLLNILLQ 189
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 190 REHALAslgKPFQPLLVVAPTQLRAWLQQYHNHCQEILHHVSMIPAKCLQKGAEVSNTTLERLISLLLETCDLEEFQTCL 269
Cdd:cd07718    81 RKKLFK---PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKSIETVP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1386806290 270 VRHCKHAFGCALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEAT 316
Cdd:cd07718   158 VIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
110-380 2.99e-50

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 171.15  E-value: 2.99e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 110 EIVFLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHygqQIDrvLCSLTAVFVSHLHADHHTGLLNILLQ 189
Cdd:COG1234     2 KLTFLGTGGAVPTPGRATSSYLLE-AGGERLLIDCGEGTQRQLLRA---GLD--PRDIDAIFITHLHGDHIAGLPGLLST 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 190 RehalaSLGKPFQPLLVVAPTQLRAWLQQYHNHCQEILH-HVSMIPakcLQKGaevsnttlerlislllETCDLEEFQ-- 266
Cdd:COG1234    76 R-----SLAGREKPLTIYGPPGTKEFLEALLKASGTDLDfPLEFHE---IEPG----------------EVFEIGGFTvt 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 267 TCLVRHCKHAFGcALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGMRMNAE 346
Cdd:COG1234   132 AFPLDHPVPAYG-YRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVK 210

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1386806290 347 FIMLNHFSQRYAKIPLF----SPDFNEKVGIAFDHMKV 380
Cdd:COG1234   211 RLVLTHFSPRYDDPEELlaeaRAVFPGPVELAEDGMVI 248
PRK00055 PRK00055
ribonuclease Z; Reviewed
 110-357 1.32e-40

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 146.09  E-value: 1.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 110 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRVlcsltavFVSHLHADHHTGLLNI 186
Cdd:PRK00055    3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQL-LKTGikpRKIDKI-------FITHLHGDHIFGLPGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 187 LLQ-----REHAL-----ASLGKPFQPLLVVA------------PTQLRAWLQQYHNhcqeilhhvsmIPAKC----LQK 240
Cdd:PRK00055   74 LSTrslsgRTEPLtiygpKGIKEFVETLLRASgslgyriaekdkPGKLDAEKLKALG-----------VPPGPlfgkLKR 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 241 GAEVsntTLE--RLISLlletcdleefqTCLVRhckhafgcalVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLE 318
Cdd:PRK00055  143 GEDV---TLEdgRIINP-----------ADVLG----------PPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFG 198

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1386806290 319 DGLEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHFSQRY 357
Cdd:PRK00055  199 DEDEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRY 237
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 110-357 1.25e-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: 1.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 110 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRVlcsltavFVSHLHADHHTGLLNI 186
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-NGELWLFDCGEGTQRQM-LRSGispMKIDRI-------FITHLHGDHILGLPGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 187 LLQRehalaSLGKPFQPLLVVAP--------TQLRAWlqqYHN-----HCQEI------------------LHHVsmIPA 235
Cdd:TIGR02651  72 LSTM-----SFQGRKEPLTIYGPpgikefieTSLRVS---YTYlnypiKIHEIeegglvfeddgfkveafpLDHS--IPS 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 236 ------------------------------KCLQKGAEVsnTTLERlislllETCDLEEFqTCLVRHckhafgcalvhss 285
Cdd:TIGR02651 142 lgyrfeekdrpgkfdrekakelgippgplyGKLKRGETV--TLIDG------RIIDPEDV-LGPPRK------------- 199

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386806290 286 GWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHFSQRY 357
Cdd:TIGR02651 200 GRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY 271
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 128-319 5.36e-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: 46.78  E-value: 5.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290  128 SSTLVNlSPDKSVLLDCGEGTFGQLCRHYGQQIDRvlcSLTAVFVSHLHADhHTGLLNILLQREHAlaslgkpfqplLVV 207
Cdd:smart00849   1 NSYLVR-DDGGAILIDTGPGEAEDLLAELKKLGPK---KIDAIILTHGHPD-HIGGLPELLEAPGA-----------PVY 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290  208 APTQLRAWLQQYHNHCQEILHHV-SMIPAKCLQKGAEVsnttlerlisllletcDLEEFQTCLVRHCKHAFGCALVHSSG 286
Cdd:smart00849  65 APEGTAELLKDLLALLGELGAEAePAPPDRTLKDGDEL----------------DLGGGELEVIHTPGHTPGSIVLYLPE 128

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1386806290  287 WKVVYSGDTMPCEALVQMGKDATLLIHEATLED 319
Cdd:smart00849 129 GKILFTGDLLFAGGDGRTLVDGGDAAASDALES 161
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 140-353 1.21e-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: 45.76  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 140 VLLDCGEGTFGQLCR--HYGQQIDRvlcSLTAVFVSHLHADHHTGLLNIllqrehalaslgKPFQPLLVVAP----TQLR 213
Cdd:pfam12706   3 ILIDPGPDLRQQALPalQPGRLRDD---PIDAVLLTHDHYDHLAGLLDL------------REGRPRPLYAPlgvlAHLR 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 214 AW------LQQYHNHCQEI-----------LHHVSMIPAKclQKGAEVSNTTLERLISLLLETcdleefqtclvrhckha 276
Cdd:pfam12706  68 RNfpylflLEHYGVRVHEIdwgesftvgdgGLTVTATPAR--HGSPRGLDPNPGDTLGFRIEG----------------- 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386806290 277 fgcalvhsSGWKVVYSGDTMPCEALV-QMGKDATLLIHEATLEDglEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHF 353
Cdd:pfam12706 129 --------PGKRVYYAGDTGYFPDEIgERLGGADLLLLDGGAWR--DDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
 
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 1.21e-106

Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme; this eukaryotic subgroup includes short forms (ELAC1) and the C-terminus of long forms including human ELAC2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293804 [Multi-domain]  Cd Length: 204  Bit Score: 314.49  E-value: 1.21e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 111 IVFLGTGSAIPMKIRNVSSTLVNLSPDKSVLLDCGEGTFGQLCRHYGQQ-IDRVLCSLTAVFVSHLHADHHTGLLNILLQ 189
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 190 REHALAslgKPFQPLLVVAPTQLRAWLQQYHNHCQEILHHVSMIPAKCLQKGAEVSNTTLERLISLLLETCDLEEFQTCL 269
Cdd:cd07718    81 RKKLFK---PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKSIETVP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1386806290 270 VRHCKHAFGCALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEAT 316
Cdd:cd07718   158 VIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
110-380 2.99e-50

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 171.15  E-value: 2.99e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 110 EIVFLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHygqQIDrvLCSLTAVFVSHLHADHHTGLLNILLQ 189
Cdd:COG1234     2 KLTFLGTGGAVPTPGRATSSYLLE-AGGERLLIDCGEGTQRQLLRA---GLD--PRDIDAIFITHLHGDHIAGLPGLLST 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 190 RehalaSLGKPFQPLLVVAPTQLRAWLQQYHNHCQEILH-HVSMIPakcLQKGaevsnttlerlislllETCDLEEFQ-- 266
Cdd:COG1234    76 R-----SLAGREKPLTIYGPPGTKEFLEALLKASGTDLDfPLEFHE---IEPG----------------EVFEIGGFTvt 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 267 TCLVRHCKHAFGcALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGMRMNAE 346
Cdd:COG1234   132 AFPLDHPVPAYG-YRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVK 210

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1386806290 347 FIMLNHFSQRYAKIPLF----SPDFNEKVGIAFDHMKV 380
Cdd:COG1234   211 RLVLTHFSPRYDDPEELlaeaRAVFPGPVELAEDGMVI 248
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 111-357 1.67e-48

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


Pssm-ID: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 166.47  E-value: 1.67e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 111 IVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYGqqidRVLCSLTAVFVSHLHADHHTGLLNILlqr 190
Cdd:cd07717     1 LTFLGTGSAVPTPERNLSSIALRL-EGELWLFDCGEGTQRQL-LRAG----LSPSKIDRIFITHLHGDHILGLPGLL--- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 191 ehALASLGKPFQPLLVVAPTQLRAWLQQYHNHCQEILhhvsmipakclqkGAEVSNTTLERLISLLLETCDLEeFQTCLV 270
Cdd:cd07717    72 --STMSLLGRTEPLTIYGPKGLKEFLETLLRLSASRL-------------PYPIEVHELEPDPGLVFEDDGFT-VTAFPL 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 271 RHCKHAFGCALVhsSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGMRMNAEFIML 350
Cdd:cd07717   136 DHRVPCFGYRFE--EGRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKAKETGHSTAKQAAEIAKKAGVKKLVL 213


                  ....*..
gi 1386806290 351 NHFSQRY 357
Cdd:cd07717   214 THFSARY 220
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 111-315 1.31e-41

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: 145.87  E-value: 1.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 111 IVFLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHyGQQIDRvlcsLTAVFVSHLHADHHTGLLNILLQR 190
Cdd:cd16272     1 LTFLGTGGAVPSLTRNTSSYLLE-TGGTRILLDCGEGTVYRLLKA-GVDPDK----LDAIFLSHFHLDHIGGLPTLLFAR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 191 EhalasLGKPFQPLLVVAPTQLRAWLQQYHNHCQEILHHVSmipakclqkgaevsnTTLERLISLLLETCDLEEF--QTC 268
Cdd:cd16272    75 R-----YGGRKKPLTIYGPKGIKEFLEKLLNFPVEILPLGF---------------PLEIEELEEGGEVLELGDLkvEAF 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1386806290 269 LVRHCKHAFGCALvHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEA 315
Cdd:cd16272   135 PVKHSVESLGYRI-EAEGKSIVYSGDTGPCENLVELAKGADLLIHEC 180
PRK00055 PRK00055
ribonuclease Z; Reviewed
 110-357 1.32e-40

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 146.09  E-value: 1.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 110 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRVlcsltavFVSHLHADHHTGLLNI 186
Cdd:PRK00055    3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQL-LKTGikpRKIDKI-------FITHLHGDHIFGLPGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 187 LLQ-----REHAL-----ASLGKPFQPLLVVA------------PTQLRAWLQQYHNhcqeilhhvsmIPAKC----LQK 240
Cdd:PRK00055   74 LSTrslsgRTEPLtiygpKGIKEFVETLLRASgslgyriaekdkPGKLDAEKLKALG-----------VPPGPlfgkLKR 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 241 GAEVsntTLE--RLISLlletcdleefqTCLVRhckhafgcalVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLE 318
Cdd:PRK00055  143 GEDV---TLEdgRIINP-----------ADVLG----------PPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFG 198

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1386806290 319 DGLEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHFSQRY 357
Cdd:PRK00055  199 DEDEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRY 237
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 110-357 1.25e-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: 1.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 110 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRVlcsltavFVSHLHADHHTGLLNI 186
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-NGELWLFDCGEGTQRQM-LRSGispMKIDRI-------FITHLHGDHILGLPGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 187 LLQRehalaSLGKPFQPLLVVAP--------TQLRAWlqqYHN-----HCQEI------------------LHHVsmIPA 235
Cdd:TIGR02651  72 LSTM-----SFQGRKEPLTIYGPpgikefieTSLRVS---YTYlnypiKIHEIeegglvfeddgfkveafpLDHS--IPS 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 236 ------------------------------KCLQKGAEVsnTTLERlislllETCDLEEFqTCLVRHckhafgcalvhss 285
Cdd:TIGR02651 142 lgyrfeekdrpgkfdrekakelgippgplyGKLKRGETV--TLIDG------RIIDPEDV-LGPPRK------------- 199

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386806290 286 GWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHFSQRY 357
Cdd:TIGR02651 200 GRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY 271
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 110-313 1.50e-23

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 97.59  E-value: 1.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 110 EIVFLGTGSAIPMKIRNVSSTLVnLSPDKSVLLDCGEGTFGQLCRHyGQQIDRvlcsLTAVFVSHLHADHHTGLLNILLQ 189
Cdd:cd07719     1 RVTLLGTGGPIPDPDRAGPSTLV-VVGGRVYLVDAGSGVVRRLAQA-GLPLGD----LDAVFLTHLHSDHVADLPALLLT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 190 REHALASlgkpfQPLLVVAPTQLRAWLQQY-HNHCQEILHHVSMIPAKCLQKGAEVSNTTlerlISLLLETCDLEEFQ-- 266
Cdd:cd07719    75 AWLAGRK-----TPLPVYGPPGTRALVDGLlAAYALDIDYRARIGDEGRPDPGALVEVHE----IAAGGVVYEDDGVKvt 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1386806290 267 TCLVRH--CKHAFgcAL-VHSSGWKVVYSGDTMPCEALVQMGKDATLLIH 313
Cdd:cd07719   146 AFLVDHgpVPPAL--AYrFDTPGRSVVFSGDTGPSENLIELAKGADLLVH 193
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 128-315 1.78e-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: 82.49  E-value: 1.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 128 SSTLVNlSPDKSVLLDCGEGTFGQLCRHygqqIDrvLCSLTAVFVSHLHADHHTGLlnILLQREHALASLGKPFQPLLVV 207
Cdd:cd07716    19 SGYLLE-ADGFRILLDCGSGVLSRLQRY----ID--PEDLDAVVLSHLHPDHCADL--GVLQYARRYHPRGARKPPLPLY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 208 APTQlrawlqqyhnhcqeilhhvsmiPAKCLQKGAEVSNTTLERLISlllETCDLE----EFQTCLVRHCKHAFGCALVH 283
Cdd:cd07716    90 GPAG----------------------PAERLAALYGLEDVFDFHPIE---PGEPLEigpfTITFFRTVHPVPCYAMRIED 144

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1386806290 284 SSGwKVVYSGDTMPCEALVQMGKDATLLIHEA 315
Cdd:cd07716   145 GGK-VLVYTGDTGYCDELVEFARGADLLLCEA 175
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 113-315 3.88e-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: 3.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 113 FLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRhygQQIDRVlcSLTAVFVSHLHADHHTGLLNILLQREH 192
Cdd:cd07740     2 FLGSGDAFGSGGRLNTCFHVA-SEAGRFLIDCGASSLIALKR---AGIDPN--AIDAIFITHLHGDHFGGLPFFLLDAQF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 193 ALaslgKPFQPLLVVAPTQLRAWLQQyhnhCQEilhhvSMIPAkclqkgaevSNTTLERL-ISLLL----ETCDLEEF-- 265
Cdd:cd07740    76 VA----KRTRPLTIAGPPGLRERLRR----AME-----ALFPG---------SSKVPRRFdLEVIElepgEPTTLGGVtv 133

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1386806290 266 QTCLVRHCKHAFGCALVHSSGWKVV-YSGDTMPCEALVQMGKDATLLIHEA 315
Cdd:cd07740   134 TAFPVVHPSGALPLALRLEAAGRVLaYSGDTEWTDALVPLARGADLFICEC 184
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 110-380 2.53e-15

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 75.70  E-value: 2.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 110 EIVFLGTGSAIPM----------------KIRNVSSTLVNlSPDKSVLLDCGEGtFGQLCRHYGQQIDRvlcsLTAVFVS 173
Cdd:COG1235     2 KVTFLGSGSSGGVpqigcdcpvcastdprYGRTRSSILVE-ADGTRLLIDAGPD-LREQLLRLGLDPSK----IDAILLT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 174 HLHADHHTGLLniLLQREHALASLgkpfqPLLVVAPT--QLRAWLQQYHNHCQEILHHVSMIPAKClqkgaevsnttler 251
Cdd:COG1235    76 HEHADHIAGLD--DLRPRYGPNPI-----PVYATPGTleALERRFPYLFAPYPGKLEFHEIEPGEP-------------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 252 lisllLETCDLeEFQTCLVRH-CKHAFGCaLVHSSGWKVVYSGDT-MPCEALVQMGKDATLLIHEATLEDGleeeavEKT 329
Cdd:COG1235   135 -----FEIGGL-TVTPFPVPHdAGDPVGY-RIEDGGKKLAYATDTgYIPEEVLELLRGADLLILDATYDDP------EPG 201

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1386806290 330 HSTTSQAINVGMRMNAEFIMLNHFSQRYAKIPLF-----SPDFNEKVGIAFDHMKV 380
Cdd:COG1235   202 HLSNEEALELLARLGPKRLVLTHLSPDNNDHELDydeleAALLPAGVEVAYDGMEI 257
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 128-319 5.36e-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: 46.78  E-value: 5.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290  128 SSTLVNlSPDKSVLLDCGEGTFGQLCRHYGQQIDRvlcSLTAVFVSHLHADhHTGLLNILLQREHAlaslgkpfqplLVV 207
Cdd:smart00849   1 NSYLVR-DDGGAILIDTGPGEAEDLLAELKKLGPK---KIDAIILTHGHPD-HIGGLPELLEAPGA-----------PVY 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290  208 APTQLRAWLQQYHNHCQEILHHV-SMIPAKCLQKGAEVsnttlerlisllletcDLEEFQTCLVRHCKHAFGCALVHSSG 286
Cdd:smart00849  65 APEGTAELLKDLLALLGELGAEAePAPPDRTLKDGDEL----------------DLGGGELEVIHTPGHTPGSIVLYLPE 128

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1386806290  287 WKVVYSGDTMPCEALVQMGKDATLLIHEATLED 319
Cdd:smart00849 129 GKILFTGDLLFAGGDGRTLVDGGDAAASDALES 161
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 140-353 1.21e-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: 45.76  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 140 VLLDCGEGTFGQLCR--HYGQQIDRvlcSLTAVFVSHLHADHHTGLLNIllqrehalaslgKPFQPLLVVAP----TQLR 213
Cdd:pfam12706   3 ILIDPGPDLRQQALPalQPGRLRDD---PIDAVLLTHDHYDHLAGLLDL------------REGRPRPLYAPlgvlAHLR 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 214 AW------LQQYHNHCQEI-----------LHHVSMIPAKclQKGAEVSNTTLERLISLLLETcdleefqtclvrhckha 276
Cdd:pfam12706  68 RNfpylflLEHYGVRVHEIdwgesftvgdgGLTVTATPAR--HGSPRGLDPNPGDTLGFRIEG----------------- 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386806290 277 fgcalvhsSGWKVVYSGDTMPCEALV-QMGKDATLLIHEATLEDglEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHF 353
Cdd:pfam12706 129 --------PGKRVYYAGDTGYFPDEIgERLGGADLLLLDGGAWR--DDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
125-295 2.19e-04

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 42.36  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 125 RNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHY---GQQIDRVlcslTAVFVSHLHADhHTGLLNILLQRehalaslgkpF 201
Cdd:pfam00753   4 GQVNSYLIE-GGGGAVLIDTGGSAEAALLLLLaalGLGPKDI----DAVILTHGHFD-HIGGLGELAEA----------T 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 202 QPLLVVAPTQLRAWLQQYHNhCQEILHHVSMIPAKCLQKGAEVSNTTLERLISLLLEtcdleefqtclVRHCK-HAFGCA 280
Cdd:pfam00753  68 DVPVIVVAEEARELLDEELG-LAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLL-----------VTHGPgHGPGHV 135

                         170
                  ....*....|....*
gi 1386806290 281 LVHSSGWKVVYSGDT 295
Cdd:pfam00753 136 VVYYGGGKVLFTGDL 150
PRK02126 PRK02126
ribonuclease Z; Provisional
 138-358 2.72e-04

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 42.98  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 138 KSVLLDCGegtfgqlcrhygqQID----RVLCSLTAVFVSHLHADHHTG---LLNILLQR----------------EHAL 194
Cdd:PRK02126   28 RALLFDLG-------------DLHhlppRELLRISHIFVSHTHMDHFIGfdrLLRHCLGRprrlrlfgppgfadqvEHKL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 195 AS----LGKPFQPLLVVAPTQLRAW-LQQYHNHCQE----------------------------ILHHvsMIP--AKCLQ 239
Cdd:PRK02126   95 AGytwnLVENYPTTFRVHEVELHDGrIRRALFSCRRafareaeeelslpdgvlldepwfrvraaFLDH--GIPclAFALE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 240 KGAEVsNTTLERLISLLLETCD-LEEFQTCL---------VRHCKHAFGC-------------ALVHSS-GWKVVYSGDT 295
Cdd:PRK02126  173 EKAHI-NIDKNRLAELGLPPGPwLRELKHAVlrgepddtpIRVLWRDGGGehervrplgelkeRVLRIEpGQKIGYVTDI 251

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1386806290 296 MP----CEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHFSQRYA 358
Cdd:PRK02126  252 GYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQ 318
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 110-179 1.15e-03

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


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 40.15  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 110 EIVFLGTGSA--IPM-----------KIRNV---SSTLVNlSPDKSVLLDCGEgTF-GQLCRHYGQQIDrvlcsltAVFV 172
Cdd:cd16279     2 KLTFLGTGTSsgVPVigcdcgvcdssDPKNRrlrSSILIE-TGGKNILIDTGP-DFrQQALRAGIRKLD-------AVLL 72


                  ....*..
gi 1386806290 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 1.67e-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: 1.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386806290 111 IVFLGTGSA--IPMK-IRNVSSTLVNLsPDKSVLLDCGEGTFGQLCRHygqQIDRVlcSLTAVFVSHLHADH 179
Cdd:cd07741     1 IIFLGTGGGrfVVITqLRASGGIWIEL-NGKNIHIDPGPGALVRMCRP---KLDPT--KLDAIILSHRHLDH 66
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 111-184 2.22e-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: 38.98  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806290 111 IVFLG-----TGSAIpmkirnvsstLVNLsPDKSVLLDCG-----EGTFGQLCRHYGQQIDrvlcSLTAVFVSHLHADhH 180
Cdd:cd16295     1 LTFLGaarevTGSCY----------LLET-GGKRILLDCGlfqggKELEELNNEPFPFDPK----EIDAVILTHAHLD-H 64


                  ....
gi 1386806290 181 TGLL 184
Cdd:cd16295    65 SGRL 68
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 135-187 2.29e-03

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 39.05  E-value: 2.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1386806290 135 SPDKSVLLDCGEGtfgqlCRHYGQQIDRVL-----CSLTAVFVSHLHADHHTGLLNIL 187
Cdd:cd07722    25 TGKRRILIDTGEG-----RPSYIPLLKSVLdsegnATISDILLTHWHHDHVGGLPDVL 77
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 121-190 2.91e-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: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 39.02  E-value: 2.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386806290 121 PMKIRNVSSTLVnLSPDKSVLLDCgegtfgQLCRHYGQQ----IDRVLCSLTAVFVSHLHADHHTGlLNILLQR 190
Cdd:cd07739    10 EISSFPVTSTLI-YGETEAVLVDA------QFTRADAERladwIKASGKTLTTIYITHGHPDHYFG-LEVLLEA 75
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 1386806290 129 STLVNLSPDKSVLLDCGEGTFGQLCRHY------GQQIDRvlcsLTAVFVSHLHADHHTGLLNIL 187
Cdd:COG2333    13 AILIRTPDGKTILIDTGPRPSFDAGERVvlpylrALGIRR----LDLLVLTHPDADHIGGLAAVL 73
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 135-183 7.73e-03

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 36.86  E-value: 7.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1386806290 135 SPDKSVLLDCGEG---TFGQLcrhygQQIDRVLCSLTAVFVSHLHADHHTGL 183
Cdd:cd07733    16 TEDGKLLIDAGLSgrkITGRL-----AEIGRDPEDIDAILVTHEHADHIKGL 62
 
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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