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Conserved domains on  [gi|51011089|ref|NP_001003503|]
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zinc phosphodiesterase ELAC protein 1 [Danio rerio]

Protein Classification

ribonuclease Z( domain architecture ID 10021201)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 4-364 1.54e-113

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: 332.65  E-value: 1.54e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089     4 DVTFLGTGSAYPSPHRGASALVLRTEGENWLFDCGEGTQIQLMKSTLRAGKISKVFISHLHGDHLFGLPGLLCTISLNLN 83
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLNGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089    84 PQPdqpppcVDIYGPRGLRLFIRVALQLSGSQLLFPYAVHELqpsdeqcpeegrlspalttasetlhpqeRPGRTVHpdp 163
Cdd:TIGR02651  81 KEP------LTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEI----------------------------EEGGLVF--- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   164 dtdcyhliDDKQFVVKAFKLFHRVPSFGFSVEERERPGRLNTDLLKELGLKPGPLYGRLKNGQSVTLDSGRVLTAGEVLE 243
Cdd:TIGR02651 124 --------EDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDREKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLG 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   244 PPLKGRKVCVFGDcSAPLgEGFKRACYGADVLVHEATLENGQQEKAVEHGHSTPGMAAAVALTCEAKTLVLHHFSQRYkp 323
Cdd:TIGR02651 196 PPRKGRKIAYTGD-TRPC-EEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY-- 271

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 51011089   324 enlrrdddeDDVSELKRQAELVLQgsrtDVILAEDFLTLPV 364
Cdd:TIGR02651 272 ---------SDEEELLEEAKKIFP----NTYIAEDFMEIEI 299
 
Name Accession Description Interval E-value
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 4-364 1.54e-113

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: 332.65  E-value: 1.54e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089     4 DVTFLGTGSAYPSPHRGASALVLRTEGENWLFDCGEGTQIQLMKSTLRAGKISKVFISHLHGDHLFGLPGLLCTISLNLN 83
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLNGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089    84 PQPdqpppcVDIYGPRGLRLFIRVALQLSGSQLLFPYAVHELqpsdeqcpeegrlspalttasetlhpqeRPGRTVHpdp 163
Cdd:TIGR02651  81 KEP------LTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEI----------------------------EEGGLVF--- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   164 dtdcyhliDDKQFVVKAFKLFHRVPSFGFSVEERERPGRLNTDLLKELGLKPGPLYGRLKNGQSVTLDSGRVLTAGEVLE 243
Cdd:TIGR02651 124 --------EDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDREKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLG 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   244 PPLKGRKVCVFGDcSAPLgEGFKRACYGADVLVHEATLENGQQEKAVEHGHSTPGMAAAVALTCEAKTLVLHHFSQRYkp 323
Cdd:TIGR02651 196 PPRKGRKIAYTGD-TRPC-EEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY-- 271

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 51011089   324 enlrrdddeDDVSELKRQAELVLQgsrtDVILAEDFLTLPV 364
Cdd:TIGR02651 272 ---------SDEEELLEEAKKIFP----NTYIAEDFMEIEI 299
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 5-363 5.13e-107

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: 314.00  E-value: 5.13e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   5 VTFLGTGSAYPSPHRGASALVLRTEGENWLFDCGEGTQIQLMKSTLRAGKISKVFISHLHGDHLFGLPGLLCTISLNLNP 84
Cdd:cd07717   1 LTFLGTGSAVPTPERNLSSIALRLEGELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGRT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089  85 QPdqpppcVDIYGPRGLRLFIRVALQLSGSQLLFPYAVHELQPsdeqcpeegrlspalttasetlhpqerpgrtvhpdpd 164
Cdd:cd07717  81 EP------LTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEP------------------------------------- 117

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089 165 tDCYHLIDDKQFVVKAFKLFHRVPSFGFSVEErerpgrlntdllkelglkpgplygrlkngqsvtldsgrvltagevlep 244
Cdd:cd07717 118 -DPGLVFEDDGFTVTAFPLDHRVPCFGYRFEE------------------------------------------------ 148

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089 245 plkGRKVCVFGDCSAPlgEGFKRACYGADVLVHEATLENGQQEKAVEHGHSTPGMAAAVALTCEAKTLVLHHFSQRYKpe 324
Cdd:cd07717 149 ---GRKIAYLGDTRPC--EGLVELAKGADLLIHEATFLDDDAEKAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARYK-- 221

                       330       340       350
                ....*....|....*....|....*....|....*....
gi 51011089 325 nlrrdddedDVSELKRQAELVlqgsRTDVILAEDFLTLP 363
Cdd:cd07717 222 ---------DPEELLKEARAV----FPNTILAEDFMTIE 247
PRK00055 PRK00055
ribonuclease Z; Reviewed
 3-364 1.17e-98

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 293.63  E-value: 1.17e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089    3 MDVTFLGTGSAYPSPHRGASALVLRTEGENWLFDCGEGTQIQLMKSTLRAGKISKVFISHLHGDHLFGLPGLLCTISLNL 82
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   83 NPQPdqpppcVDIYGPRGLRLFIRVALQLSGSqllfpyavhelqpsdeqcpeegrlspalttasetlhpqerpgrtvhpd 162
Cdd:PRK00055  82 RTEP------LTIYGPKGIKEFVETLLRASGS------------------------------------------------ 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089  163 pdtdcyhliddkqfvvkafklfhrvpsFGFSVEERERPGRLNTDLLKELGLKPGPLYGRLKNGQSVTLDSGRVLTAGEVL 242
Cdd:PRK00055 108 ---------------------------LGYRIAEKDKPGKLDAEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVL 160

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089  243 EPPLKGRKVCVFGDcSAPLgEGFKRACYGADVLVHEATLENGQQEKAVEHGHSTPGMAAAVALTCEAKTLVLHHFSQRYK 322
Cdd:PRK00055 161 GPPRKGRKVAYCGD-TRPC-EALVELAKGADLLVHEATFGDEDEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYT 238

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 51011089  323 PenlrrdddedDVSELKRQAELVLQgsrtDVILAEDFLTLPV 364
Cdd:PRK00055 239 G----------DPEELLKEAREIFP----NTELAEDLMRVEV 266
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
3-364 6.86e-77

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 237.40  E-value: 6.86e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   3 MDVTFLGTGSAYPSPHRGASALVLRTEGENWLFDCGEGTQIQLMKSTLRAGKISKVFISHLHGDHLFGLPGLLCTISLNL 82
Cdd:COG1234   1 MKLTFLGTGGAVPTPGRATSSYLLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089  83 NPQPdqpppcVDIYGPRGLRLFIRVALQLSGSQLLFPYAVHELQPSDEqcpeegrlspalttasetlhpqerpgrtvhpd 162
Cdd:COG1234  81 REKP------LTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPGEV-------------------------------- 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089 163 pdtdcyhlIDDKQFVVKAFKLFHRVPSFGFSVEErerpgrlntdllkelglkpgplygrlkngqsvtldsgrvltagevl 242
Cdd:COG1234 123 --------FEIGGFTVTAFPLDHPVPAYGYRFEE---------------------------------------------- 148

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089 243 epplKGRKVCVFGDCSAPlgEGFKRACYGADVLVHEATLENGQQEKAVEHGHSTPGMAAAVALTCEAKTLVLHHFSQRYk 322
Cdd:COG1234 149 ----PGRSLVYSGDTRPC--EALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRY- 221

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 51011089 323 penlrrdddeDDVSELKRQAELVLQGsrtDVILAEDFLTLPV 364
Cdd:COG1234 222 ----------DDPEELLAEARAVFPG---PVELAEDGMVIEL 250
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 22-130 1.21e-09

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: 56.79  E-value: 1.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089     22 SALVLRTEGENWLFDCGEGTQIQLMKSTLRAG--KISKVFISHLHGDHLFGLPGLLCTislnlnpqpdqppPCVDIYGPR 99
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGpkKIDAIILTHGHPDHIGGLPELLEA-------------PGAPVYAPE 67

                           90       100       110
                   ....*....|....*....|....*....|.
gi 51011089    100 GLRLFIRVALQLSGSQLLFPYAVHELQPSDE 130
Cdd:smart00849  68 GTAELLKDLLALLGELGAEAEPAPPDRTLKD 98
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 34-317 9.50e-07

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 48.85  E-value: 9.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089    34 LFDCGEGTQIQLMK----STLRAGKISKVFISHLHGDHLFGLPGLLctislnlnpqPDQPPPcvdIYGPRGLRLFIRVAL 109
Cdd:pfam12706   4 LIDPGPDLRQQALPalqpGRLRDDPIDAVLLTHDHYDHLAGLLDLR----------EGRPRP---LYAPLGVLAHLRRNF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   110 QLSGSQLLFPYAVHELQPSDEQCPEEGRLSpalttasetlhpqerpgrtvhpdpdtdcyhliddkqfvVKAFKLFHRVPs 189
Cdd:pfam12706  71 PYLFLLEHYGVRVHEIDWGESFTVGDGGLT--------------------------------------VTATPARHGSP- 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   190 fgfsveerERPGRLNTDllkelglkpgplygrlkngqsvtldsgrvlTAGEVLEPPlkGRKVCVFGDCsAPLGEGFKRAC 269
Cdd:pfam12706 112 --------RGLDPNPGD------------------------------TLGFRIEGP--GKRVYYAGDT-GYFPDEIGERL 150

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 51011089   270 YGADVLVHEATLENgqQEKAVEHGHSTPGMAAAVALTCEAKTLVLHHF 317
Cdd:pfam12706 151 GGADLLLLDGGAWR--DDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
 
Name Accession Description Interval E-value
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 4-364 1.54e-113

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: 332.65  E-value: 1.54e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089     4 DVTFLGTGSAYPSPHRGASALVLRTEGENWLFDCGEGTQIQLMKSTLRAGKISKVFISHLHGDHLFGLPGLLCTISLNLN 83
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLNGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089    84 PQPdqpppcVDIYGPRGLRLFIRVALQLSGSQLLFPYAVHELqpsdeqcpeegrlspalttasetlhpqeRPGRTVHpdp 163
Cdd:TIGR02651  81 KEP------LTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEI----------------------------EEGGLVF--- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   164 dtdcyhliDDKQFVVKAFKLFHRVPSFGFSVEERERPGRLNTDLLKELGLKPGPLYGRLKNGQSVTLDSGRVLTAGEVLE 243
Cdd:TIGR02651 124 --------EDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDREKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLG 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   244 PPLKGRKVCVFGDcSAPLgEGFKRACYGADVLVHEATLENGQQEKAVEHGHSTPGMAAAVALTCEAKTLVLHHFSQRYkp 323
Cdd:TIGR02651 196 PPRKGRKIAYTGD-TRPC-EEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY-- 271

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 51011089   324 enlrrdddeDDVSELKRQAELVLQgsrtDVILAEDFLTLPV 364
Cdd:TIGR02651 272 ---------SDEEELLEEAKKIFP----NTYIAEDFMEIEI 299
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 5-363 5.13e-107

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: 314.00  E-value: 5.13e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   5 VTFLGTGSAYPSPHRGASALVLRTEGENWLFDCGEGTQIQLMKSTLRAGKISKVFISHLHGDHLFGLPGLLCTISLNLNP 84
Cdd:cd07717   1 LTFLGTGSAVPTPERNLSSIALRLEGELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGRT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089  85 QPdqpppcVDIYGPRGLRLFIRVALQLSGSQLLFPYAVHELQPsdeqcpeegrlspalttasetlhpqerpgrtvhpdpd 164
Cdd:cd07717  81 EP------LTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEP------------------------------------- 117

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089 165 tDCYHLIDDKQFVVKAFKLFHRVPSFGFSVEErerpgrlntdllkelglkpgplygrlkngqsvtldsgrvltagevlep 244
Cdd:cd07717 118 -DPGLVFEDDGFTVTAFPLDHRVPCFGYRFEE------------------------------------------------ 148

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089 245 plkGRKVCVFGDCSAPlgEGFKRACYGADVLVHEATLENGQQEKAVEHGHSTPGMAAAVALTCEAKTLVLHHFSQRYKpe 324
Cdd:cd07717 149 ---GRKIAYLGDTRPC--EGLVELAKGADLLIHEATFLDDDAEKAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARYK-- 221

                       330       340       350
                ....*....|....*....|....*....|....*....
gi 51011089 325 nlrrdddedDVSELKRQAELVlqgsRTDVILAEDFLTLP 363
Cdd:cd07717 222 ---------DPEELLKEARAV----FPNTILAEDFMTIE 247
PRK00055 PRK00055
ribonuclease Z; Reviewed
 3-364 1.17e-98

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 293.63  E-value: 1.17e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089    3 MDVTFLGTGSAYPSPHRGASALVLRTEGENWLFDCGEGTQIQLMKSTLRAGKISKVFISHLHGDHLFGLPGLLCTISLNL 82
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   83 NPQPdqpppcVDIYGPRGLRLFIRVALQLSGSqllfpyavhelqpsdeqcpeegrlspalttasetlhpqerpgrtvhpd 162
Cdd:PRK00055  82 RTEP------LTIYGPKGIKEFVETLLRASGS------------------------------------------------ 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089  163 pdtdcyhliddkqfvvkafklfhrvpsFGFSVEERERPGRLNTDLLKELGLKPGPLYGRLKNGQSVTLDSGRVLTAGEVL 242
Cdd:PRK00055 108 ---------------------------LGYRIAEKDKPGKLDAEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVL 160

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089  243 EPPLKGRKVCVFGDcSAPLgEGFKRACYGADVLVHEATLENGQQEKAVEHGHSTPGMAAAVALTCEAKTLVLHHFSQRYK 322
Cdd:PRK00055 161 GPPRKGRKVAYCGD-TRPC-EALVELAKGADLLVHEATFGDEDEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYT 238

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 51011089  323 PenlrrdddedDVSELKRQAELVLQgsrtDVILAEDFLTLPV 364
Cdd:PRK00055 239 G----------DPEELLKEAREIFP----NTELAEDLMRVEV 266
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
3-364 6.86e-77

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 237.40  E-value: 6.86e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   3 MDVTFLGTGSAYPSPHRGASALVLRTEGENWLFDCGEGTQIQLMKSTLRAGKISKVFISHLHGDHLFGLPGLLCTISLNL 82
Cdd:COG1234   1 MKLTFLGTGGAVPTPGRATSSYLLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089  83 NPQPdqpppcVDIYGPRGLRLFIRVALQLSGSQLLFPYAVHELQPSDEqcpeegrlspalttasetlhpqerpgrtvhpd 162
Cdd:COG1234  81 REKP------LTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPGEV-------------------------------- 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089 163 pdtdcyhlIDDKQFVVKAFKLFHRVPSFGFSVEErerpgrlntdllkelglkpgplygrlkngqsvtldsgrvltagevl 242
Cdd:COG1234 123 --------FEIGGFTVTAFPLDHPVPAYGYRFEE---------------------------------------------- 148

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089 243 epplKGRKVCVFGDCSAPlgEGFKRACYGADVLVHEATLENGQQEKAVEHGHSTPGMAAAVALTCEAKTLVLHHFSQRYk 322
Cdd:COG1234 149 ----PGRSLVYSGDTRPC--EALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRY- 221

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 51011089 323 penlrrdddeDDVSELKRQAELVLQGsrtDVILAEDFLTLPV 364
Cdd:COG1234 222 ----------DDPEELLAEARAVFPG---PVELAEDGMVIEL 250
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 5-279 4.30e-35

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: 126.99  E-value: 4.30e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   5 VTFLGTGSAYPSPHRGASALVLRTEGENWLFDCGEGTQIQLMKSTLRAGKISKVFISHLHGDHLFGLPGLLCTISLNLNP 84
Cdd:cd16272   1 LTFLGTGGAVPSLTRNTSSYLLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089  85 QPdqpppcVDIYGPRGLRLFIRVALQ--LSGSQLLFPYAVHELQPSDEQcpeegrlspalttasetlhpqerpgrtvhpd 162
Cdd:cd16272  81 KP------LTIYGPKGIKEFLEKLLNfpVEILPLGFPLEIEELEEGGEV------------------------------- 123

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089 163 pdtdcyhlIDDKQFVVKAFKLFHRVPSFGFSVEErerpgrlntdllkelglkpgplygrlkngqsvtldsgrvltagevl 242
Cdd:cd16272 124 --------LELGDLKVEAFPVKHSVESLGYRIEA---------------------------------------------- 149

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 51011089 243 epplKGRKVCVFGDCSAplGEGFKRACYGADVLVHEA 279
Cdd:cd16272 150 ----EGKSIVYSGDTGP--CENLVELAKGADLLIHEC 180
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 5-280 3.73e-26

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: 103.78  E-value: 3.73e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   5 VTFLGTGSAYPSPHRGASALVLRTEGENW-LFDCGEGTQIQL--------MKSTLRagKISKVFISHLHGDHLFGLPGLL 75
Cdd:cd07718   1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSiLLDCGEGTLGQLrrhygpeeADEVLR--NLKCIFISHLHADHHLGLIRLL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089  76 CTISlNLNPQPDQPPPCVdiyGPRGLRLFIRVALQLSGSQLLFPYAVHELQPSDEQCPEEGRLSPALTTASETLHPQErp 155
Cdd:cd07718  79 AERK-KLFKPPSPPLYVV---APRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKS-- 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089 156 grtvhpdpdtdcyhliddkqfvVKAFKLFHRVPSFGFSVEERErpgrlntdllkelglkpgplygrlkngqsvtldsgrv 235
Cdd:cd07718 153 ----------------------IETVPVIHCPDAYGIVLTHED------------------------------------- 173

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 51011089 236 ltagevlepplkGRKVcVF-GDCSaPLgEGFKRACYGADVLVHEAT 280
Cdd:cd07718 174 ------------GWKI-VYsGDTR-PC-EALVEAGKGADLLIHEAT 204
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 5-111 1.56e-24

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: 99.13  E-value: 1.56e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   5 VTFLGTGSAYPSPHRGASALVLRTEGENWLFDCGEGTQIQLMKSTLRAGKISKVFISHLHGDHLFGLPGLlctisLNLNP 84
Cdd:cd07719   2 VTLLGTGGPIPDPDRAGPSTLVVVGGRVYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPAL-----LLTAW 76

                        90       100
                ....*....|....*....|....*..
gi 51011089  85 QPDQPPPcVDIYGPRGLRLFIRVALQL 111
Cdd:cd07719  77 LAGRKTP-LPVYGPPGTRALVDGLLAA 102
PRK02126 PRK02126
ribonuclease Z; Provisional
 26-328 3.58e-22

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 95.75  E-value: 3.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   26 LRTEGENWLFDCGEGTQiqLMKSTLRagKISKVFISHLHGDHLFGLPGLLctiSLNLnpqpDQPPPcVDIYGPRGlrlFI 105
Cdd:PRK02126  23 FLFERRALLFDLGDLHH--LPPRELL--RISHIFVSHTHMDHFIGFDRLL---RHCL----GRPRR-LRLFGPPG---FA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089  106 R-VALQLSGS--QLLFPYA----VHELQPSDeqcpeeGRLSPALTTASETLHPQERPGRTVHPDPdtdcyhLIDDKQFVV 178
Cdd:PRK02126  88 DqVEHKLAGYtwNLVENYPttfrVHEVELHD------GRIRRALFSCRRAFAREAEEELSLPDGV------LLDEPWFRV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089  179 KAFKLFHRVPSFGFSVEERERPGrLNTDLLKELGLKPGPLYGRLKNG---------------QSVTLDSGRVLTAGEVLE 243
Cdd:PRK02126 156 RAAFLDHGIPCLAFALEEKAHIN-IDKNRLAELGLPPGPWLRELKHAvlrgepddtpirvlwRDGGGEHERVRPLGELKE 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089  244 PPLK---GRKVCVFGDCsAPLGEGFKR---ACYGADVLVHEATLENGQQEKAVEHGHSTPGMAAAVALTCEAKTLVLHHF 317
Cdd:PRK02126 235 RVLRiepGQKIGYVTDI-GYTEENLARiveLAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHF 313

                        330
                 ....*....|...
gi 51011089  318 SQRY--KPENLRR 328
Cdd:PRK02126 314 SPRYqgRGAELYR 326
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 3-364 8.28e-22

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 93.42  E-value: 8.28e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   3 MDVTFLGTGSAYPSPH----------------RGASALVLRTEGENWLFDCGEGTQIQLMKSTLRAGKISKVFISHLHGD 66
Cdd:COG1235   1 MKVTFLGSGSSGGVPQigcdcpvcastdprygRTRSSILVEADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTHEHAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089  67 HLFGLPGLLctislnlnpqPDQPPPCVDIYGPRGLRLFIRVAlqlsgsqllFPYAVHELQPsdeqcpeegrlspalttas 146
Cdd:COG1235  81 HIAGLDDLR----------PRYGPNPIPVYATPGTLEALERR---------FPYLFAPYPG------------------- 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089 147 eTLHPQE-RPGRTVHpdpdtdcyhlIDDkqFVVKAFKLFH-RVPSFGFSVEErerpgrlntdllkelglkpgplygrlkn 224
Cdd:COG1235 123 -KLEFHEiEPGEPFE----------IGG--LTVTPFPVPHdAGDPVGYRIED---------------------------- 161

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089 225 gqsvtldsgrvltagevlepplKGRKVCVFGDCsAPLGEGFKRACYGADVLVHEATLENGqqekavEHGHSTPGMAAAVA 304
Cdd:COG1235 162 ----------------------GGKKLAYATDT-GYIPEEVLELLRGADLLILDATYDDP------EPGHLSNEEALELL 212

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089 305 LTCEAKTLVLHHFSQRYkpenlrrDDDEDDVSELKRQAElvlqgsRTDVILAEDFLTLPV 364
Cdd:COG1235 213 ARLGPKRLVLTHLSPDN-------NDHELDYDELEAALL------PAGVEVAYDGMEIEL 259
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 6-151 2.96e-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: 2.96e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   6 TFLGTGSAYPSPHRGASALVLRTEGENWLFDCGEGTQIQLMKSTLRAGKISKVFISHLHGDHLFGLPGLLctISLNLNPQ 85
Cdd:cd07740   1 TFLGSGDAFGSGGRLNTCFHVASEAGRFLIDCGASSLIALKRAGIDPNAIDAIFITHLHGDHFGGLPFFL--LDAQFVAK 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51011089  86 PDQPPPcvdIYGPRGLRLFIRVALQL--SGSQLL---FPYAVHELQPSDEQcpEEGRLSPaltTASETLHP 151
Cdd:cd07740  79 RTRPLT---IAGPPGLRERLRRAMEAlfPGSSKVprrFDLEVIELEPGEPT--TLGGVTV---TAFPVVHP 141
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 5-153 3.49e-13

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: 67.08  E-value: 3.49e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   5 VTFLGTGSAYPSPHRGASALVLRTEGENWLFDCGEGTQIQLMKStLRAGKISKVFISHLHGDHLFGLPGLLCTISLNLNP 84
Cdd:cd07716   2 LTVLGCSGSYPGPGGACSGYLLEADGFRILLDCGSGVLSRLQRY-IDPEDLDAVVLSHLHPDHCADLGVLQYARRYHPRG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51011089  85 QPDQPPPcvdIYGPRGLRLFIRVALQLSGSqllfpYAVHELQPSDEQcpeegRLSPALTTASETLHPQE 153
Cdd:cd07716  81 ARKPPLP---LYGPAGPAERLAALYGLEDV-----FDFHPIEPGEPL-----EIGPFTITFFRTVHPVP 136
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 22-130 1.21e-09

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: 56.79  E-value: 1.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089     22 SALVLRTEGENWLFDCGEGTQIQLMKSTLRAG--KISKVFISHLHGDHLFGLPGLLCTislnlnpqpdqppPCVDIYGPR 99
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGpkKIDAIILTHGHPDHIGGLPELLEA-------------PGAPVYAPE 67

                           90       100       110
                   ....*....|....*....|....*....|.
gi 51011089    100 GLRLFIRVALQLSGSQLLFPYAVHELQPSDE 130
Cdd:smart00849  68 GTAELLKDLLALLGELGAEAEPAPPDRTLKD 98
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 3-99 4.53e-08

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: 52.48  E-value: 4.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   3 MDVTFLGTGSAYPSP----------------HRGASALVLRTEGENWLFDCGEGTQIQLmkstLRAG--KISKVFISHLH 64
Cdd:cd16279   1 MKLTFLGTGTSSGVPvigcdcgvcdssdpknRRLRSSILIETGGKNILIDTGPDFRQQA----LRAGirKLDAVLLTHAH 76

                        90       100       110
                ....*....|....*....|....*....|....*
gi 51011089  65 GDHLFGLPGLLctiSLNLNPQpdqppPCVDIYGPR 99
Cdd:cd16279  77 ADHIHGLDDLR---PFNRLQQ-----RPIPVYASE 103
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 34-317 9.50e-07

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 48.85  E-value: 9.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089    34 LFDCGEGTQIQLMK----STLRAGKISKVFISHLHGDHLFGLPGLLctislnlnpqPDQPPPcvdIYGPRGLRLFIRVAL 109
Cdd:pfam12706   4 LIDPGPDLRQQALPalqpGRLRDDPIDAVLLTHDHYDHLAGLLDLR----------EGRPRP---LYAPLGVLAHLRRNF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   110 QLSGSQLLFPYAVHELQPSDEQCPEEGRLSpalttasetlhpqerpgrtvhpdpdtdcyhliddkqfvVKAFKLFHRVPs 189
Cdd:pfam12706  71 PYLFLLEHYGVRVHEIDWGESFTVGDGGLT--------------------------------------VTATPARHGSP- 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   190 fgfsveerERPGRLNTDllkelglkpgplygrlkngqsvtldsgrvlTAGEVLEPPlkGRKVCVFGDCsAPLGEGFKRAC 269
Cdd:pfam12706 112 --------RGLDPNPGD------------------------------TLGFRIEGP--GKRVYYAGDT-GYFPDEIGERL 150

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 51011089   270 YGADVLVHEATLENgqQEKAVEHGHSTPGMAAAVALTCEAKTLVLHHF 317
Cdd:pfam12706 151 GGADLLLLDGGAWR--DDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
19-75 2.82e-06

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 47.36  E-value: 2.82e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51011089    19 RGASALVLRTEGENWLFDCGEGTQIQLMKSTLRAG----KISKVFISHLHGDHLFGLPGLL 75
Cdd:pfam00753   4 GQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGlgpkDIDAVILTHGHFDHIGGLGELA 64
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 22-71 3.34e-06

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. 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: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 47.93  E-value: 3.34e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 51011089  22 SALVLRTEGENWLFDCGEGTQI-----QLMKSTLRAG----KISKVFISHLHGDHLFGL 71
Cdd:cd07720  50 NAFLVRTGGRLILVDTGAGGLFgptagKLLANLAAAGidpeDIDDVLLTHLHPDHIGGL 108
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 21-103 8.98e-06

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


Pssm-ID: 293854 [Multi-domain]  Cd Length: 175  Bit Score: 45.72  E-value: 8.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089  21 ASALVLRTEGENWLFDCGEGTQIQLMKSTLRAGKISKVFISHLHGDHLFGLPGLLCTISLNLNPQ-----PDQPPPcvDI 95
Cdd:cd16296  12 GAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKcvlsgPNKQSP--DK 89


                ....*...
gi 51011089  96 YGPRGLRL 103
Cdd:cd16296  90 IGVRRQIL 97
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 3-71 1.44e-05

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. 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: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 45.31  E-value: 1.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   3 MDVTFLGTGSA------------------YPSPHRGASALVLRTEGENWLFDCGegtqiqLMKSTLR--AGKISKVFISH 62
Cdd:cd07736   1 MKLTFLGTGDAggvpvygcdcsacqrarqDPSYRRRPCSALIEVDGERILLDAG------LTDLAERfpPGSIDAILLTH 74


                ....*....
gi 51011089  63 LHGDHLFGL 71
Cdd:cd07736  75 FHMDHVQGL 83
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 15-64 5.76e-05

tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related structurally to the Lactamase_B family members. tRNase Z is the endonuclease that is involved in tRNA 3'-end maturation through removal of the 3'-trailer sequences from tRNA precursors. The fission yeast Schizosaccharomyces pombe contains two candidate tRNase Zs encoded by two essential genes. The first, Swiss:Q10155, is targeted to the nucleus and has an SV40 nuclear localization signal at its N-terminus, consisting of four consecutive arginine and lysine residues between residues 208 and 211 (KKRK) that is critical for the NLS function. The second, Swiss:P87168, is targeted to the mitochondria, with an N-terminal mitochondrial targeting signal within the first 38 residues.


Pssm-ID: 404562 [Multi-domain]  Cd Length: 63  Bit Score: 40.65  E-value: 5.76e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 51011089    15 PSPHRGASALVLRTEGENWLF-DCGEGTQIQLMKSTLRAGKISKVFISHLH 64
Cdd:pfam13691   6 PTADTPGPLLLLHFDSKRYLFgNVGEGTQRALNEQKVRLSKLEDIFLTGKV 56
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 33-86 7.56e-05

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: 42.91  E-value: 7.56e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 51011089  33 WLFDCGEGTQ--IQLMKSTLRAGK---ISKVFISHLHGDHLFGLPGLLctiSLNLNPQP 86
Cdd:cd07722  30 ILIDTGEGRPsyIPLLKSVLDSEGnatISDILLTHWHHDHVGGLPDVL---DLLRGPSP 85
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 3-75 9.87e-05

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: 43.31  E-value: 9.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   3 MDVTFLGTGsaypsphRGASALVLRTEGENWLFDCGEGTQIQLMKSTLRA-------GKISKVFISHLHGDHLFGLPGLL 75
Cdd:COG2333   1 LRVTFLDVG-------QGDAILIRTPDGKTILIDTGPRPSFDAGERVVLPylralgiRRLDLLVLTHPDADHIGGLAAVL 73
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 24-75 1.20e-04

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


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 42.66  E-value: 1.20e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 51011089  24 LVLRTEGENWLFDCGEGTQIQLMKSTLRAG-KISKVFISHLHGDHLFGLPGLL 75
Cdd:cd06262  14 LVSDEEGEAILIDPGAGALEKILEAIEELGlKIKAILLTHGHFDHIGGLAELK 66
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 20-75 1.75e-04

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. 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: 293799  Cd Length: 269  Bit Score: 42.61  E-value: 1.75e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089  20 GASALVlRTEGENWLFDCGEGTQI----QLMKSTLRagKISKVFISHLHGDHLFGLPGLL 75
Cdd:cd07713  20 GLSLLI-ETEGKKILFDTGQSGVLlhnaKKLGIDLS--DIDAVVLSHGHYDHTGGLKALL 76
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 3-74 1.86e-04

RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 43.25  E-value: 1.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   3 MDVTFLG-----TGSAYpsphrgasalVLRTEGENWLFDCG---EGTQIQLMKSTLRAGKISKVFISHLHGDHLFGLPGL 74
Cdd:COG1236   1 MKLTFLGaagevTGSCY----------LLETGGTRILIDCGlfqGGKERNWPPFPFRPSDVDAVVLTHAHLDHSGALPLL 70
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 14-74 3.80e-04

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 41.21  E-value: 3.80e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51011089  14 YPSPHRGASALVLRTEGENWLFDCG-EGTQIQLMKSTLRA--GKISKVFISHLHGDHLFGLPGL 74
Cdd:COG0491   8 TPGAGLGVNSYLIVGGDGAVLIDTGlGPADAEALLAALAAlgLDIKAVLLTHLHPDHVGGLAAL 71
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 6-199 6.19e-04

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. 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: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 40.56  E-value: 6.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089   6 TFLGT-GSaYPSPHRGA-------SALVLRTEGENWLFDCGEGtqIQLMKSTLRAGKISK---VFISHLHGDHLFGLPgl 74
Cdd:cd07715   1 RFWGVrGS-IPVPGPDTvryggntSCVEVRAGGELLILDAGTG--IRELGNELMKEGPPGeahLLLSHTHWDHIQGFP-- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089  75 lctislNLNP--QPDQpppCVDIYGPRGLRLFIRVAL--QLSGSqlLFPyavhelqpsdeqcpeegrLSPALTTASETLH 150
Cdd:cd07715  76 ------FFAPayDPGN---RIHIYGPHKDGGSLEEVLrrQMSPP--YFP------------------VPLEELLAAIEFH 126

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 51011089 151 PQErPGRTVHPDPdtdcyhliddkqFVVKAFKLFHRVPSFGFSVEERER 199
Cdd:cd07715 127 DLE-PGEPFSIGG------------VTVTTIPLNHPGGALGYRIEEDGK 162
PRK14866 PRK14866
hypothetical protein; Provisional
 142-241 7.36e-04

hypothetical protein; Provisional


Pssm-ID: 237840  Cd Length: 451  Bit Score: 41.52  E-value: 7.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089  142 LTTASETLhpqeRPGRTVHPDPDTDCY-HLIDDkqfVVKAFKL-FHRVPSFGFSVEERERpgRLNTDLLKELGLKPGPLY 219
Cdd:PRK14866 344 LTTGGGTR----LGGFIAFEAADSDIReDLVDL---CVKVLKEkYDSVYRGDNELVIRKE--RFDPELARKLGVPEGPAF 414

                         90       100
                 ....*....|....*....|..
gi 51011089  220 GRLKNGQSVTLDsGRVLTAGEV 241
Cdd:PRK14866 415 GKLAAGQPVEVD-GETITPEMV 435
PRK02113 PRK02113
MBL fold metallo-hydrolase;
3-74 7.99e-04

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 40.54  E-value: 7.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51011089    3 MDVTFLGTGSAYPSPHRG-----------------ASALVLrTEGENWLFDCGEGTQIQLMksTLRAGKISKVFISHLHG 65
Cdd:PRK02113   1 MKIRILGSGTSTGVPEIGctcpvctskdprdnrlrTSALVE-TEGARILIDCGPDFREQML--RLPFGKIDAVLITHEHY 77


                 ....*....
gi 51011089   66 DHLFGLPGL 74
Cdd:PRK02113  78 DHVGGLDDL 86
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 5-67 2.06e-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: 39.10  E-value: 2.06e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51011089   5 VTFLGTGSA---YPSPHRGASALVLRTEGENWLFDCGEGTQIQLMKSTLRAGKISKVFISHLHGDH 67
Cdd:cd07741   1 IIFLGTGGGrfvVITQLRASGGIWIELNGKNIHIDPGPGALVRMCRPKLDPTKLDAIILSHRHLDH 66
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 23-75 2.73e-03

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. 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: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 38.27  E-value: 2.73e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 51011089  23 ALVLRTEGENWLFDCGEGTQI--QLMKSTLRA---GKISKVFISHLHGDHLFGLPGLL 75
Cdd:cd07731  12 AILIQTPGKTILIDTGPRDSFgeDVVVPYLKArgiKKLDYLILTHPDADHIGGLDAVL 69
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 18-75 7.29e-03

Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. 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: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 37.31  E-value: 7.29e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51011089  18 HRGASALVLRTEGENWLFDCG-----EGTQIQLMKSTLRAGKISKVFISHLHGDHLFGLPGLL 75
Cdd:cd07734   8 EVGRSCFLVEFKGRTVLLDCGmnpgkEDPEACLPQFELLPPEIDAILISHFHLDHCGALPYLF 70
 
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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