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Conserved domains on  [gi|1907082873|ref|XP_036012824|]
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zinc phosphodiesterase ELAC protein 2 isoform X4 [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 ...
 111-321 1.29e-105

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: 312.56  E-value: 1.29e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 111 IVFLGTGSAIPMKIRNVSSTLVNLSPDKSVLLDCGEGTFGQLCRHYGQQ-IDRVLCSLTAVFVSHLHADHHTGLLNILLQ 189
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 190 REHALRsffqaslgKPFQPLLVVAPTQLRAWLQQYHNHCQEILHHVSMIPAKCLQKGAEVSNTTLERLISLLLETCDLEE 269
Cdd:cd07718    81 RKKLFK--------PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKS 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907082873 270 FQTCLVRHCKHAFGCALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEAT 321
Cdd:cd07718   153 IETVPVIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 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 ...
 111-321 1.29e-105

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: 312.56  E-value: 1.29e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 111 IVFLGTGSAIPMKIRNVSSTLVNLSPDKSVLLDCGEGTFGQLCRHYGQQ-IDRVLCSLTAVFVSHLHADHHTGLLNILLQ 189
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 190 REHALRsffqaslgKPFQPLLVVAPTQLRAWLQQYHNHCQEILHHVSMIPAKCLQKGAEVSNTTLERLISLLLETCDLEE 269
Cdd:cd07718    81 RKKLFK--------PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKS 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907082873 270 FQTCLVRHCKHAFGCALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEAT 321
Cdd:cd07718   153 IETVPVIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
110-385 8.81e-50

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 169.99  E-value: 8.81e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 110 EIVFLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHygqQIDrvLCSLTAVFVSHLHADHHTGLLNILLQ 189
Cdd:COG1234     2 KLTFLGTGGAVPTPGRATSSYLLE-AGGERLLIDCGEGTQRQLLRA---GLD--PRDIDAIFITHLHGDHIAGLPGLLST 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 190 REHALRSffqaslgkpfQPLLVVAPTQLRAWLQQYHNHCQEILH-HVSMIPakcLQKGaevsnttlerlislllETCDLE 268
Cdd:COG1234    76 RSLAGRE----------KPLTIYGPPGTKEFLEALLKASGTDLDfPLEFHE---IEPG----------------EVFEIG 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 269 EFQ--TCLVRHCKHAFGcALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGM 346
Cdd:COG1234   127 GFTvtAFPLDHPVPAYG-YRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAA 205

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907082873 347 RMNAEFIMLNHFSQRYAKIPLF----SPDFNEKVGIAFDHMKV 385
Cdd:COG1234   206 EAGVKRLVLTHFSPRYDDPEELlaeaRAVFPGPVELAEDGMVI 248
PRK00055 PRK00055
ribonuclease Z; Reviewed
 110-362 2.06e-41

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 148.40  E-value: 2.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 110 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRvlcsltaVFVSHLHADHHTGLLNI 186
Cdd:PRK00055    3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQL-LKTGikpRKIDK-------IFITHLHGDHIFGLPGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 187 LLQ-----REHALRSFFQASLGKPFQPLLVVAPTqlRAWLqqyhnhcqeILHH------------VSMIPAKC----LQK 245
Cdd:PRK00055   74 LSTrslsgRTEPLTIYGPKGIKEFVETLLRASGS--LGYR---------IAEKdkpgkldaeklkALGVPPGPlfgkLKR 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 246 GAEVsntTLE--RLISLlletcdleefqTCLVRhckhafgcalVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLE 323
Cdd:PRK00055  143 GEDV---TLEdgRIINP-----------ADVLG----------PPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFG 198

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907082873 324 DGLEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHFSQRY 362
Cdd:PRK00055  199 DEDEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRY 237
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 110-362 3.40e-35

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: 132.73  E-value: 3.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 110 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRVlcsltavFVSHLHADHHTGLLNI 186
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-NGELWLFDCGEGTQRQM-LRSGispMKIDRI-------FITHLHGDHILGLPGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 187 L-----LQREHAL--------RSFFQASLG-----KPFQPLLV-VAPTQLRAWLQQYHNHCQEILHHV-SM--------- 237
Cdd:TIGR02651  72 LstmsfQGRKEPLtiygppgiKEFIETSLRvsytyLNYPIKIHeIEEGGLVFEDDGFKVEAFPLDHSIpSLgyrfeekdr 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 238 -------------IPA----KCLQKGAEVsnTTLERlislllETCDLEEFqTCLVRHckhafgcalvhssGWKVVYSGDT 300
Cdd:TIGR02651 152 pgkfdrekakelgIPPgplyGKLKRGETV--TLIDG------RIIDPEDV-LGPPRK-------------GRKIAYTGDT 209

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082873 301 MPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHFSQRY 362
Cdd:TIGR02651 210 RPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY 271
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 128-324 2.04e-05

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 44.85  E-value: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873  128 SSTLVNlSPDKSVLLDCGEGTFGQLCRHYGQQIDRvlcSLTAVFVSHLHADhHTGLLNILLQREHAlrsffqaslgkpfq 207
Cdd:smart00849   1 NSYLVR-DDGGAILIDTGPGEAEDLLAELKKLGPK---KIDAIILTHGHPD-HIGGLPELLEAPGA-------------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873  208 plLVVAPTQLRAWLQQYHNHCQEILHHV-SMIPAKCLQKGAEVsnttlerlisllletcDLEEFQTCLVRHCKHAFGCAL 286
Cdd:smart00849  62 --PVYAPEGTAELLKDLLALLGELGAEAePAPPDRTLKDGDEL----------------DLGGGELEVIHTPGHTPGSIV 123

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1907082873  287 VHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLED 324
Cdd:smart00849 124 LYLPEGKILFTGDLLFAGGDGRTLVDGGDAAASDALES 161
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 140-358 2.99e-05

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 44.99  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 140 VLLDCGEGTFGQLCR--HYGQQIDRvlcSLTAVFVSHLHADHHTGLLNIllqREHALRSFFqASLG--------KPFQPL 209
Cdd:pfam12706   3 ILIDPGPDLRQQALPalQPGRLRDD---PIDAVLLTHDHYDHLAGLLDL---REGRPRPLY-APLGvlahlrrnFPYLFL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 210 LVVAPTQLR--AWLQQYHNHCQEIlhHVSMIPAKclQKGAEVSNTTLERLISLLLETcdleefqtclvrhckhafgcalv 287
Cdd:pfam12706  76 LEHYGVRVHeiDWGESFTVGDGGL--TVTATPAR--HGSPRGLDPNPGDTLGFRIEG----------------------- 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082873 288 hsSGWKVVYSGDTMPCEALV-QMGKDATLLIHEATLEDglEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHF 358
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 ...
 111-321 1.29e-105

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: 312.56  E-value: 1.29e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 111 IVFLGTGSAIPMKIRNVSSTLVNLSPDKSVLLDCGEGTFGQLCRHYGQQ-IDRVLCSLTAVFVSHLHADHHTGLLNILLQ 189
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 190 REHALRsffqaslgKPFQPLLVVAPTQLRAWLQQYHNHCQEILHHVSMIPAKCLQKGAEVSNTTLERLISLLLETCDLEE 269
Cdd:cd07718    81 RKKLFK--------PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKS 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907082873 270 FQTCLVRHCKHAFGCALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEAT 321
Cdd:cd07718   153 IETVPVIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
110-385 8.81e-50

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 169.99  E-value: 8.81e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 110 EIVFLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHygqQIDrvLCSLTAVFVSHLHADHHTGLLNILLQ 189
Cdd:COG1234     2 KLTFLGTGGAVPTPGRATSSYLLE-AGGERLLIDCGEGTQRQLLRA---GLD--PRDIDAIFITHLHGDHIAGLPGLLST 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 190 REHALRSffqaslgkpfQPLLVVAPTQLRAWLQQYHNHCQEILH-HVSMIPakcLQKGaevsnttlerlislllETCDLE 268
Cdd:COG1234    76 RSLAGRE----------KPLTIYGPPGTKEFLEALLKASGTDLDfPLEFHE---IEPG----------------EVFEIG 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 269 EFQ--TCLVRHCKHAFGcALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGM 346
Cdd:COG1234   127 GFTvtAFPLDHPVPAYG-YRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAA 205

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907082873 347 RMNAEFIMLNHFSQRYAKIPLF----SPDFNEKVGIAFDHMKV 385
Cdd:COG1234   206 EAGVKRLVLTHFSPRYDDPEELlaeaRAVFPGPVELAEDGMVI 248
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 111-362 1.15e-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: 164.54  E-value: 1.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 111 IVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYGqqidRVLCSLTAVFVSHLHADHHTGLLNiLLQR 190
Cdd:cd07717     1 LTFLGTGSAVPTPERNLSSIALRL-EGELWLFDCGEGTQRQL-LRAG----LSPSKIDRIFITHLHGDHILGLPG-LLST 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 191 ehalrsffqASLGKPFQPLLVVAPTQLRAWLQQYHNHCQEILhhvsmipakclqkGAEVSNTTLERLISLLLETCDLEeF 270
Cdd:cd07717    74 ---------MSLLGRTEPLTIYGPKGLKEFLETLLRLSASRL-------------PYPIEVHELEPDPGLVFEDDGFT-V 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 271 QTCLVRHCKHAFGCALVhsSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGMRMNA 350
Cdd:cd07717   131 TAFPLDHRVPCFGYRFE--EGRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKAKETGHSTAKQAAEIAKKAGV 208

                         250
                  ....*....|..
gi 1907082873 351 EFIMLNHFSQRY 362
Cdd:cd07717   209 KKLVLTHFSARY 220
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 111-320 1.65e-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: 1.65e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 111 IVFLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHyGQQIDRvlcsLTAVFVSHLHADHHTGLLNILLQR 190
Cdd:cd16272     1 LTFLGTGGAVPSLTRNTSSYLLE-TGGTRILLDCGEGTVYRLLKA-GVDPDK----LDAIFLSHFHLDHIGGLPTLLFAR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 191 EHALRSffqaslgkpfQPLLVVAPTQLRAWLQQYHNHCQEILHHVSmipakclqkgaevsnTTLERLISLLLETCDLEEF 270
Cdd:cd16272    75 RYGGRK----------KPLTIYGPKGIKEFLEKLLNFPVEILPLGF---------------PLEIEELEEGGEVLELGDL 129

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907082873 271 --QTCLVRHCKHAFGCALvHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEA 320
Cdd:cd16272   130 kvEAFPVKHSVESLGYRI-EAEGKSIVYSGDTGPCENLVELAKGADLLIHEC 180
PRK00055 PRK00055
ribonuclease Z; Reviewed
 110-362 2.06e-41

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 148.40  E-value: 2.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 110 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRvlcsltaVFVSHLHADHHTGLLNI 186
Cdd:PRK00055    3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQL-LKTGikpRKIDK-------IFITHLHGDHIFGLPGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 187 LLQ-----REHALRSFFQASLGKPFQPLLVVAPTqlRAWLqqyhnhcqeILHH------------VSMIPAKC----LQK 245
Cdd:PRK00055   74 LSTrslsgRTEPLTIYGPKGIKEFVETLLRASGS--LGYR---------IAEKdkpgkldaeklkALGVPPGPlfgkLKR 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 246 GAEVsntTLE--RLISLlletcdleefqTCLVRhckhafgcalVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLE 323
Cdd:PRK00055  143 GEDV---TLEdgRIINP-----------ADVLG----------PPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFG 198

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1907082873 324 DGLEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHFSQRY 362
Cdd:PRK00055  199 DEDEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRY 237
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 110-362 3.40e-35

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: 132.73  E-value: 3.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 110 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRVlcsltavFVSHLHADHHTGLLNI 186
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-NGELWLFDCGEGTQRQM-LRSGispMKIDRI-------FITHLHGDHILGLPGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 187 L-----LQREHAL--------RSFFQASLG-----KPFQPLLV-VAPTQLRAWLQQYHNHCQEILHHV-SM--------- 237
Cdd:TIGR02651  72 LstmsfQGRKEPLtiygppgiKEFIETSLRvsytyLNYPIKIHeIEEGGLVFEDDGFKVEAFPLDHSIpSLgyrfeekdr 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 238 -------------IPA----KCLQKGAEVsnTTLERlislllETCDLEEFqTCLVRHckhafgcalvhssGWKVVYSGDT 300
Cdd:TIGR02651 152 pgkfdrekakelgIPPgplyGKLKRGETV--TLIDG------RIIDPEDV-LGPPRK-------------GRKIAYTGDT 209

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082873 301 MPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHFSQRY 362
Cdd:TIGR02651 210 RPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY 271
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 110-318 1.76e-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: 97.20  E-value: 1.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 110 EIVFLGTGSAIPMKIRNVSSTLVnLSPDKSVLLDCGEGTFGQLCRHyGQQIDRvlcsLTAVFVSHLHADHHTGLLNILLQ 189
Cdd:cd07719     1 RVTLLGTGGPIPDPDRAGPSTLV-VVGGRVYLVDAGSGVVRRLAQA-GLPLGD----LDAVFLTHLHSDHVADLPALLLT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 190 REHALRSffqaslgkpfQPLLVVAPTQLRAWLQQY-HNHCQEILHHVSMIPAKCLQKGAEVSNTTlerlISLLLETCDLE 268
Cdd:cd07719    75 AWLAGRK----------TPLPVYGPPGTRALVDGLlAAYALDIDYRARIGDEGRPDPGALVEVHE----IAAGGVVYEDD 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907082873 269 EFQ--TCLVRH--CKHAFgcAL-VHSSGWKVVYSGDTMPCEALVQMGKDATLLIH 318
Cdd:cd07719   141 GVKvtAFLVDHgpVPPAL--AYrFDTPGRSVVFSGDTGPSENLIELAKGADLLVH 193
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 113-320 5.02e-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: 81.92  E-value: 5.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 113 FLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRhygQQIDRVlcSLTAVFVSHLHADHHTGLLNILLQREH 192
Cdd:cd07740     2 FLGSGDAFGSGGRLNTCFHVA-SEAGRFLIDCGASSLIALKR---AGIDPN--AIDAIFITHLHGDHFGGLPFFLLDAQF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 193 -ALRSffqaslgkpfQPLLVVAPTQLRAWLQQyhnhCQEilhhvSMIPAkclqkgaevSNTTLERL-ISLLL----ETCD 266
Cdd:cd07740    76 vAKRT----------RPLTIAGPPGLRERLRR----AME-----ALFPG---------SSKVPRRFdLEVIElepgEPTT 127

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082873 267 LEEF--QTCLVRHCKHAFGCALVHSSGWKVV-YSGDTMPCEALVQMGKDATLLIHEA 320
Cdd:cd07740   128 LGGVtvTAFPVVHPSGALPLALRLEAAGRVLaYSGDTEWTDALVPLARGADLFICEC 184
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 128-320 8.93e-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: 80.56  E-value: 8.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 128 SSTLVNlSPDKSVLLDCGEGTFGQLCRHygqqIDrvLCSLTAVFVSHLHADH---HTGLLnillqreHALRSffqASLGK 204
Cdd:cd07716    19 SGYLLE-ADGFRILLDCGSGVLSRLQRY----ID--PEDLDAVVLSHLHPDHcadLGVLQ-------YARRY---HPRGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 205 PFQPLLVVAPTQlrawlqqyhnhcqeilhhvsmiPAKCLQKGAEVSNTTLERLISlllETCDLE----EFQTCLVRHCKH 280
Cdd:cd07716    82 RKPPLPLYGPAG----------------------PAERLAALYGLEDVFDFHPIE---PGEPLEigpfTITFFRTVHPVP 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907082873 281 AFGCALVHSSGwKVVYSGDTMPCEALVQMGKDATLLIHEA 320
Cdd:cd07716   137 CYAMRIEDGGK-VLVYTGDTGYCDELVEFARGADLLLCEA 175
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 110-385 9.85e-16

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 76.86  E-value: 9.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 110 EIVFLGTGSAIPM----------------KIRNVSSTLVNlSPDKSVLLDCGEGtFGQLCRHYGQQIDRvlcsLTAVFVS 173
Cdd:COG1235     2 KVTFLGSGSSGGVpqigcdcpvcastdprYGRTRSSILVE-ADGTRLLIDAGPD-LREQLLRLGLDPSK----IDAILLT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 174 HLHADHHTGLLNillqrehaLRSFFQAslgkpfQPLLVVAP----TQLRAWLQQYHNHCQEILHHVSMIPAKClqkgaev 249
Cdd:COG1235    76 HEHADHIAGLDD--------LRPRYGP------NPIPVYATpgtlEALERRFPYLFAPYPGKLEFHEIEPGEP------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 250 snttlerlisllLETCDLeEFQTCLVRH-CKHAFGCaLVHSSGWKVVYSGDT-MPCEALVQMGKDATLLIHEATLEDGle 327
Cdd:COG1235   135 ------------FEIGGL-TVTPFPVPHdAGDPVGY-RIEDGGKKLAYATDTgYIPEEVLELLRGADLLILDATYDDP-- 198

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082873 328 eeavEKTHSTTSQAINVGMRMNAEFIMLNHFSQRYAKIPLF-----SPDFNEKVGIAFDHMKV 385
Cdd:COG1235   199 ----EPGHLSNEEALELLARLGPKRLVLTHLSPDNNDHELDydeleAALLPAGVEVAYDGMEI 257
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 128-324 2.04e-05

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 44.85  E-value: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873  128 SSTLVNlSPDKSVLLDCGEGTFGQLCRHYGQQIDRvlcSLTAVFVSHLHADhHTGLLNILLQREHAlrsffqaslgkpfq 207
Cdd:smart00849   1 NSYLVR-DDGGAILIDTGPGEAEDLLAELKKLGPK---KIDAIILTHGHPD-HIGGLPELLEAPGA-------------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873  208 plLVVAPTQLRAWLQQYHNHCQEILHHV-SMIPAKCLQKGAEVsnttlerlisllletcDLEEFQTCLVRHCKHAFGCAL 286
Cdd:smart00849  62 --PVYAPEGTAELLKDLLALLGELGAEAePAPPDRTLKDGDEL----------------DLGGGELEVIHTPGHTPGSIV 123

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1907082873  287 VHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLED 324
Cdd:smart00849 124 LYLPEGKILFTGDLLFAGGDGRTLVDGGDAAASDALES 161
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 140-358 2.99e-05

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 44.99  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 140 VLLDCGEGTFGQLCR--HYGQQIDRvlcSLTAVFVSHLHADHHTGLLNIllqREHALRSFFqASLG--------KPFQPL 209
Cdd:pfam12706   3 ILIDPGPDLRQQALPalQPGRLRDD---PIDAVLLTHDHYDHLAGLLDL---REGRPRPLY-APLGvlahlrrnFPYLFL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 210 LVVAPTQLR--AWLQQYHNHCQEIlhHVSMIPAKclQKGAEVSNTTLERLISLLLETcdleefqtclvrhckhafgcalv 287
Cdd:pfam12706  76 LEHYGVRVHeiDWGESFTVGDGGL--TVTATPAR--HGSPRGLDPNPGDTLGFRIEG----------------------- 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082873 288 hsSGWKVVYSGDTMPCEALV-QMGKDATLLIHEATLEDglEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHF 358
Cdd:pfam12706 129 --PGKRVYYAGDTGYFPDEIgERLGGADLLLLDGGAWR--DDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK02126 PRK02126
ribonuclease Z; Provisional
 138-363 1.64e-04

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 43.75  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 138 KSVLLDCGegtfgqlcrhygqQID----RVLCSLTAVFVSHLHADHHTG---LLNILLQREHALRSF------------F 198
Cdd:PRK02126   28 RALLFDLG-------------DLHhlppRELLRISHIFVSHTHMDHFIGfdrLLRHCLGRPRRLRLFgppgfadqvehkL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 199 QA---SLGKPFQPLLVVAPTQLRAW-LQQYHNHCQE----------------------------ILHHvsMIP--AKCLQ 244
Cdd:PRK02126   95 AGytwNLVENYPTTFRVHEVELHDGrIRRALFSCRRafareaeeelslpdgvlldepwfrvraaFLDH--GIPclAFALE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 245 KGAEVsNTTLERLISLLLETCD-LEEFQTCL---------VRHCKHAFGC-------------ALVHSS-GWKVVYSGDT 300
Cdd:PRK02126  173 EKAHI-NIDKNRLAELGLPPGPwLRELKHAVlrgepddtpIRVLWRDGGGehervrplgelkeRVLRIEpGQKIGYVTDI 251

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082873 301 MP----CEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHFSQRYA 363
Cdd:PRK02126  252 GYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQ 318
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
125-190 2.68e-04

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 41.97  E-value: 2.68e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082873 125 RNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHY---GQQIDRVlcslTAVFVSHLHADhHTGLLNILLQR 190
Cdd:pfam00753   4 GQVNSYLIE-GGGGAVLIDTGGSAEAALLLLLaalGLGPKDI----DAVILTHGHFD-HIGGLGELAEA 66
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 110-179 1.18e-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: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 110 EIVFLGTGSA--IPM-----------KIRNV---SSTLVNlSPDKSVLLDCGEgTF-GQLCRHYGQQIDrvlcsltAVFV 172
Cdd:cd16279     2 KLTFLGTGTSsgVPVigcdcgvcdssDPKNRrlrSSILIE-TGGKNILIDTGP-DFrQQALRAGIRKLD-------AVLL 72


                  ....*..
gi 1907082873 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 1.73e-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: 1.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082873 111 IVFLGTGSA--IPMK-IRNVSSTLVNLsPDKSVLLDCGEGTFGQLCRHygqQIDRVlcSLTAVFVSHLHADH 179
Cdd:cd07741     1 IIFLGTGGGrfVVITqLRASGGIWIEL-NGKNIHIDPGPGALVRMCRP---KLDPT--KLDAIILSHRHLDH 66
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 135-187 2.24e-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: 2.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082873 135 SPDKSVLLDCGEGtfgqlCRHYGQQIDRVL-----CSLTAVFVSHLHADHHTGLLNIL 187
Cdd:cd07722    25 TGKRRILIDTGEG-----RPSYIPLLKSVLdsegnATISDILLTHWHHDHVGGLPDVL 77
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 111-184 2.29e-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: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082873 111 IVFLG-----TGSAIpmkirnvsstLVNLsPDKSVLLDCG-----EGTFGQLCRHYGQQIDrvlcSLTAVFVSHLHADhH 180
Cdd:cd16295     1 LTFLGaarevTGSCY----------LLET-GGKRILLDCGlfqggKELEELNNEPFPFDPK----EIDAVILTHAHLD-H 64


                  ....
gi 1907082873 181 TGLL 184
Cdd:cd16295    65 SGRL 68
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 121-190 2.98e-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: 2.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082873 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 6.58e-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: 6.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082873 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 7.98e-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: 7.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907082873 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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