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Conserved domains on  [gi|8922122|ref|NP_061166|]
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zinc phosphodiesterase ELAC protein 1 [Homo sapiens]

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 ...
 4-359 3.75e-119

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: 346.51  E-value: 3.75e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122      4 DVTFLGTGAAYPSPTRGASAVVLRCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLCTISLQSG 83
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLNGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122     84 smvsKQPIEIYGPVGLRDFIWRTMELSHTELVFHYVVHELVPTAdqcpaeelkefahvnradsppkeeqgrtilldseen 163
Cdd:TIGR02651  81 ----KEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEGG------------------------------------ 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    164 syLLFDDEQFVVKAFRLFHRIPSFGFSVVEKKRPGKLNAQKLKDLGVPPGPAYGKLKNGISVVLENGVTISPQDVLKKPI 243
Cdd:TIGR02651 121 --LVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDREKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLGPPR 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    244 VGRKICILGD---CSGVVgdggvKLCFEADLLIHEATLDDAQMDKAKEHGHSTPQMAATFAKLCRAKRLVLTHFSQRYkp 320
Cdd:TIGR02651 199 KGRKIAYTGDtrpCEEVI-----EFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY-- 271

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 8922122    321 valaregetDGIAELKKQAESVldLQEVTLAEDFMVISI 359
Cdd:TIGR02651 272 ---------SDEEELLEEAKKI--FPNTYIAEDFMEIEI 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 ...
 4-359 3.75e-119

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: 346.51  E-value: 3.75e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122      4 DVTFLGTGAAYPSPTRGASAVVLRCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLCTISLQSG 83
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLNGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122     84 smvsKQPIEIYGPVGLRDFIWRTMELSHTELVFHYVVHELVPTAdqcpaeelkefahvnradsppkeeqgrtilldseen 163
Cdd:TIGR02651  81 ----KEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEGG------------------------------------ 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    164 syLLFDDEQFVVKAFRLFHRIPSFGFSVVEKKRPGKLNAQKLKDLGVPPGPAYGKLKNGISVVLENGVTISPQDVLKKPI 243
Cdd:TIGR02651 121 --LVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDREKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLGPPR 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    244 VGRKICILGD---CSGVVgdggvKLCFEADLLIHEATLDDAQMDKAKEHGHSTPQMAATFAKLCRAKRLVLTHFSQRYkp 320
Cdd:TIGR02651 199 KGRKIAYTGDtrpCEEVI-----EFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY-- 271

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 8922122    321 valaregetDGIAELKKQAESVldLQEVTLAEDFMVISI 359
Cdd:TIGR02651 272 ---------SDEEELLEEAKKI--FPNTYIAEDFMEIEI 299
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 5-358 5.82e-117

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: 339.04  E-value: 5.82e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    5 VTFLGTGAAYPSPTRGASAVVLRCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLCTISLQSGs 84
Cdd:cd07717   1 LTFLGTGSAVPTPERNLSSIALRLEGELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGR- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   85 mvsKQPIEIYGPVGLRDFIWRTMELSHTELVFHYVVHELvptadqcpaeelkefahvnradsppkeeqgrtilldsEENS 164
Cdd:cd07717  80 ---TEPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHEL-------------------------------------EPDP 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122  165 YLLFDDEQFVVKAFRLFHRIPSFGFSVVEkkrpgklnaqklkdlgvppgpaygklkngisvvlengvtispqdvlkkpiv 244
Cdd:cd07717 120 GLVFEDDGFTVTAFPLDHRVPCFGYRFEE--------------------------------------------------- 148

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122  245 GRKICILGD---CSGVvgdggVKLCFEADLLIHEATLDDAQMDKAKEHGHSTPQMAATFAKLCRAKRLVLTHFSQRYKpv 321
Cdd:cd07717 149 GRKIAYLGDtrpCEGL-----VELAKGADLLIHEATFLDDDAEKAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARYK-- 221

                       330       340       350
                ....*....|....*....|....*....|....*..
gi 8922122  322 alaregetdGIAELKKQAESVldLQEVTLAEDFMVIS 358
Cdd:cd07717 222 ---------DPEELLKEARAV--FPNTILAEDFMTIE 247
PRK00055 PRK00055
ribonuclease Z; Reviewed
 3-360 3.24e-107

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 315.20  E-value: 3.24e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122     3 MDVTFLGTGAAYPSPTRGASAVVLRCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLCTISLQS 82
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    83 gsmvSKQPIEIYGPVGLRDFIWRTMELShtelvfhyvvhelvptadqcpaeelkefahvnradsppkeeqgrtilldsee 162
Cdd:PRK00055  82 ----RTEPLTIYGPKGIKEFVETLLRAS---------------------------------------------------- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   163 nsyllfddeqfvvkafrlfhriPSFGFSVVEKKRPGKLNAQKLKDLGVPPGPAYGKLKNGISVVLENGVTISPQDVLKKP 242
Cdd:PRK00055 106 ----------------------GSLGYRIAEKDKPGKLDAEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPP 163

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   243 IVGRKICILGD---CSGVvgdggVKLCFEADLLIHEATLDDAQMDKAKEHGHSTPQMAATFAKLCRAKRLVLTHFSQRYk 319
Cdd:PRK00055 164 RKGRKVAYCGDtrpCEAL-----VELAKGADLLVHEATFGDEDEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRY- 237

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 8922122   320 pvalaregeTDGIAELKKQAESVLDlqEVTLAEDFMVISIP 360
Cdd:PRK00055 238 ---------TGDPEELLKEAREIFP--NTELAEDLMRVEVP 267
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
3-359 4.42e-84

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 255.50  E-value: 4.42e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    3 MDVTFLGTGAAYPSPTRGASAVVLRCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLCTISLQS 82
Cdd:COG1234   1 MKLTFLGTGGAVPTPGRATSSYLLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   83 GsmvsKQPIEIYGPVGLRDFIWRTMELSHTELVFHYVVHELVPTadqcpaeelkefahvnradsppkeeqgrtilldsee 162
Cdd:COG1234  81 R----EKPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPG------------------------------------ 120

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122  163 nsyLLFDDEQFVVKAFRLFHRIPSFGFSVVEKkrpgklnaqklkdlgvppgpaygklkngisvvlengvtispqdvlkkp 242
Cdd:COG1234 121 ---EVFEIGGFTVTAFPLDHPVPAYGYRFEEP------------------------------------------------ 149

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122  243 ivGRKICILGD---CSGVvgdggVKLCFEADLLIHEATLDDAQMDKAKEHGHSTPQMAATFAKLCRAKRLVLTHFSQRYk 319
Cdd:COG1234 150 --GRSLVYSGDtrpCEAL-----VELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRY- 221

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 8922122  320 pvalaregetDGIAELKKQAESVLDlQEVTLAEDFMVISI 359
Cdd:COG1234 222 ----------DDPEELLAEARAVFP-GPVELAEDGMVIEL 250
GntH_guanitoxin NF041257
guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;
3-109 1.04e-14

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;


Pssm-ID: 469157 [Multi-domain]  Cd Length: 372  Bit Score: 74.66  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122     3 MDVTFLGTGAayPSPTRG-ASAVVL----RCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLCT 77
Cdd:NF041257  13 MRITFLGSGP--PPPRRGqANTSILvelgNGERDKFFFDIGSGSVANIIALQIPYNLLNKVFITHLHVDHYGDLPYLYPF 90

                         90       100       110
                 ....*....|....*....|....*....|..
gi 8922122    78 ISLqSGSMVskqPIEIYGPVGlrdfiwRTMEL 109
Cdd:NF041257  91 GAW-SGRWT---PLRVWGPSG------RTPEL 112
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 22-111 8.09e-12

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: 63.34  E-value: 8.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122      22 SAVVLRCEGECWLFDCGEGTQTQLMKSQLKAG--RITKIFITHLHGDHFFGLPGLLctislqsgsmvSKQPIEIYGPVGL 99
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGpkKIDAIILTHGHPDHIGGLPELL-----------EAPGAPVYAPEGT 69

                           90
                   ....*....|..
gi 8922122     100 RDFIWRTMELSH 111
Cdd:smart00849  70 AELLKDLLALLG 81
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 34-314 1.19e-08

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: 54.24  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122     34 LFDCGEGTQTQLMK----SQLKAGRITKIFITHLHGDHFFGLPGLLCTislqsgsmvskQPIEIYGPVGLRDFIWRTMEL 109
Cdd:pfam12706   4 LIDPGPDLRQQALPalqpGRLRDDPIDAVLLTHDHYDHLAGLLDLREG-----------RPRPLYAPLGVLAHLRRNFPY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    110 SHTELVFHYVVHELVPtadqcpaeelkefahvnradsppkeeqgrtilldseensyllfdDEQFVVKAFRL-FHRIPSFG 188
Cdd:pfam12706  73 LFLLEHYGVRVHEIDW--------------------------------------------GESFTVGDGGLtVTATPARH 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    189 FSvvekkrpgklnaqkLKDLGVPPGPAYGklkngisVVLENGvtispqdvlkkpivGRKICILGDCsGVVGDGGVKLCFE 268
Cdd:pfam12706 109 GS--------------PRGLDPNPGDTLG-------FRIEGP--------------GKRVYYAGDT-GYFPDEIGERLGG 152

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 8922122    269 ADLLIHEATLDDAqmDKAKEHGHSTPQMAATFAKLCRAKRLVLTHF 314
Cdd:pfam12706 153 ADLLLLDGGAWRD--DEMIHMGHMTPEEAVEAAADLGARRKVLIHI 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 ...
 4-359 3.75e-119

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: 346.51  E-value: 3.75e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122      4 DVTFLGTGAAYPSPTRGASAVVLRCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLCTISLQSG 83
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLNGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122     84 smvsKQPIEIYGPVGLRDFIWRTMELSHTELVFHYVVHELVPTAdqcpaeelkefahvnradsppkeeqgrtilldseen 163
Cdd:TIGR02651  81 ----KEPLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEEGG------------------------------------ 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    164 syLLFDDEQFVVKAFRLFHRIPSFGFSVVEKKRPGKLNAQKLKDLGVPPGPAYGKLKNGISVVLENGVTISPQDVLKKPI 243
Cdd:TIGR02651 121 --LVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDREKAKELGIPPGPLYGKLKRGETVTLIDGRIIDPEDVLGPPR 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    244 VGRKICILGD---CSGVVgdggvKLCFEADLLIHEATLDDAQMDKAKEHGHSTPQMAATFAKLCRAKRLVLTHFSQRYkp 320
Cdd:TIGR02651 199 KGRKIAYTGDtrpCEEVI-----EFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY-- 271

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 8922122    321 valaregetDGIAELKKQAESVldLQEVTLAEDFMVISI 359
Cdd:TIGR02651 272 ---------SDEEELLEEAKKI--FPNTYIAEDFMEIEI 299
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 5-358 5.82e-117

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: 339.04  E-value: 5.82e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    5 VTFLGTGAAYPSPTRGASAVVLRCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLCTISLQSGs 84
Cdd:cd07717   1 LTFLGTGSAVPTPERNLSSIALRLEGELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGR- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   85 mvsKQPIEIYGPVGLRDFIWRTMELSHTELVFHYVVHELvptadqcpaeelkefahvnradsppkeeqgrtilldsEENS 164
Cdd:cd07717  80 ---TEPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHEL-------------------------------------EPDP 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122  165 YLLFDDEQFVVKAFRLFHRIPSFGFSVVEkkrpgklnaqklkdlgvppgpaygklkngisvvlengvtispqdvlkkpiv 244
Cdd:cd07717 120 GLVFEDDGFTVTAFPLDHRVPCFGYRFEE--------------------------------------------------- 148

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122  245 GRKICILGD---CSGVvgdggVKLCFEADLLIHEATLDDAQMDKAKEHGHSTPQMAATFAKLCRAKRLVLTHFSQRYKpv 321
Cdd:cd07717 149 GRKIAYLGDtrpCEGL-----VELAKGADLLIHEATFLDDDAEKAKETGHSTAKQAAEIAKKAGVKKLVLTHFSARYK-- 221

                       330       340       350
                ....*....|....*....|....*....|....*..
gi 8922122  322 alaregetdGIAELKKQAESVldLQEVTLAEDFMVIS 358
Cdd:cd07717 222 ---------DPEELLKEARAV--FPNTILAEDFMTIE 247
PRK00055 PRK00055
ribonuclease Z; Reviewed
 3-360 3.24e-107

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 315.20  E-value: 3.24e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122     3 MDVTFLGTGAAYPSPTRGASAVVLRCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLCTISLQS 82
Cdd:PRK00055   2 MELTFLGTGSGVPTPTRNVSSILLRLGGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    83 gsmvSKQPIEIYGPVGLRDFIWRTMELShtelvfhyvvhelvptadqcpaeelkefahvnradsppkeeqgrtilldsee 162
Cdd:PRK00055  82 ----RTEPLTIYGPKGIKEFVETLLRAS---------------------------------------------------- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   163 nsyllfddeqfvvkafrlfhriPSFGFSVVEKKRPGKLNAQKLKDLGVPPGPAYGKLKNGISVVLENGVTISPQDVLKKP 242
Cdd:PRK00055 106 ----------------------GSLGYRIAEKDKPGKLDAEKLKALGVPPGPLFGKLKRGEDVTLEDGRIINPADVLGPP 163

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   243 IVGRKICILGD---CSGVvgdggVKLCFEADLLIHEATLDDAQMDKAKEHGHSTPQMAATFAKLCRAKRLVLTHFSQRYk 319
Cdd:PRK00055 164 RKGRKVAYCGDtrpCEAL-----VELAKGADLLVHEATFGDEDEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRY- 237

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 8922122   320 pvalaregeTDGIAELKKQAESVLDlqEVTLAEDFMVISIP 360
Cdd:PRK00055 238 ---------TGDPEELLKEAREIFP--NTELAEDLMRVEVP 267
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
3-359 4.42e-84

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 255.50  E-value: 4.42e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    3 MDVTFLGTGAAYPSPTRGASAVVLRCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLCTISLQS 82
Cdd:COG1234   1 MKLTFLGTGGAVPTPGRATSSYLLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   83 GsmvsKQPIEIYGPVGLRDFIWRTMELSHTELVFHYVVHELVPTadqcpaeelkefahvnradsppkeeqgrtilldsee 162
Cdd:COG1234  81 R----EKPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPG------------------------------------ 120

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122  163 nsyLLFDDEQFVVKAFRLFHRIPSFGFSVVEKkrpgklnaqklkdlgvppgpaygklkngisvvlengvtispqdvlkkp 242
Cdd:COG1234 121 ---EVFEIGGFTVTAFPLDHPVPAYGYRFEEP------------------------------------------------ 149

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122  243 ivGRKICILGD---CSGVvgdggVKLCFEADLLIHEATLDDAQMDKAKEHGHSTPQMAATFAKLCRAKRLVLTHFSQRYk 319
Cdd:COG1234 150 --GRSLVYSGDtrpCEAL-----VELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRY- 221

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 8922122  320 pvalaregetDGIAELKKQAESVLDlQEVTLAEDFMVISI 359
Cdd:COG1234 222 ----------DDPEELLAEARAVFP-GPVELAEDGMVIEL 250
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 5-276 5.60e-36

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: 128.92  E-value: 5.60e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    5 VTFLGTGAAYPSPTRGASAVVLRCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLCTISLQSGs 84
Cdd:cd16272   1 LTFLGTGGAVPSLTRNTSSYLLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGR- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   85 mvsKQPIEIYGPVGLRDFIWRTMELSHT--ELVFHYVVHELvptadqcpaeelkefahvnradsPPKEEQgrtilldsee 162
Cdd:cd16272  80 ---KKPLTIYGPKGIKEFLEKLLNFPVEilPLGFPLEIEEL-----------------------EEGGEV---------- 123

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122  163 nsyllFDDEQFVVKAFRLFHRIPSFGFsvvekkrpgklnaqklkdlgvppgpaygklkngisvVLEngvtispqdvlkkp 242
Cdd:cd16272 124 -----LELGDLKVEAFPVKHSVESLGY------------------------------------RIE-------------- 148

                       250       260       270
                ....*....|....*....|....*....|....
gi 8922122  243 IVGRKICILGDCSgvVGDGGVKLCFEADLLIHEA 276
Cdd:cd16272 149 AEGKSIVYSGDTG--PCENLVELAKGADLLIHEC 180
PRK02126 PRK02126
ribonuclease Z; Provisional
 24-326 3.02e-28

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 112.32  E-value: 3.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    24 VVLRCEGECWLFDCGEgtQTQLMKSQLKagRITKIFITHLHGDHFFGLPGLLCTIslqsgsMVSKQPIEIYGPVGLRDFI 103
Cdd:PRK02126  21 VDFLFERRALLFDLGD--LHHLPPRELL--RISHIFVSHTHMDHFIGFDRLLRHC------LGRPRRLRLFGPPGFADQV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   104 --------WRTMELSHTELVFHYVvhELVPtadqcpaEELKEFAHVNRaDSPPKEEQGRTILLDSEensylLFDDEQFVV 175
Cdd:PRK02126  91 ehklagytWNLVENYPTTFRVHEV--ELHD-------GRIRRALFSCR-RAFAREAEEELSLPDGV-----LLDEPWFRV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   176 KAFRLFHRIPSFGFSVVEKKRPGkLNAQKLKDLGVPPGPAYGKLKNGISVVLENG--VTISPQDV------------LKK 241
Cdd:PRK02126 156 RAAFLDHGIPCLAFALEEKAHIN-IDKNRLAELGLPPGPWLRELKHAVLRGEPDDtpIRVLWRDGggehervrplgeLKE 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   242 PIV----GRKICILGDCSGVVGDGG--VKLCFEADLLIHEATLDDAQMDKAKEHGHSTPQMAATFAKLCRAKRLVLTHFS 315
Cdd:PRK02126 235 RVLriepGQKIGYVTDIGYTEENLAriVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFS 314

                        330
                 ....*....|...
gi 8922122   316 QRY--KPVALARE 326
Cdd:PRK02126 315 PRYqgRGAELYRE 327
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 3-359 3.76e-28

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 110.37  E-value: 3.76e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    3 MDVTFLGTGAAYPSPT----------------RGASAVVLRCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGD 66
Cdd:COG1235   1 MKVTFLGSGSSGGVPQigcdcpvcastdprygRTRSSILVEADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTHEHAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   67 HFFGLPGLlctislqsGSMVSKQPIEIYGPVGLRDFIwrtmelshtELVFHYVVHELVPTADQCPAEELKEFAhvnrads 146
Cdd:COG1235  81 HIAGLDDL--------RPRYGPNPIPVYATPGTLEAL---------ERRFPYLFAPYPGKLEFHEIEPGEPFE------- 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122  147 ppkeeqgrtilldseensyllFDDeqFVVKAFRLFHripsfgfsvvekkrpgklnaqklkdlgvPPGPAYGklkngisVV 226
Cdd:COG1235 137 ---------------------IGG--LTVTPFPVPH----------------------------DAGDPVG-------YR 158

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122  227 LENGvtispqdvlkkpivGRKICILGDCsGVVGDGGVKLCFEADLLIHEATLDDAqmdkakEHGHSTPQMAATFAKLCRA 306
Cdd:COG1235 159 IEDG--------------GKKLAYATDT-GYIPEEVLELLRGADLLILDATYDDP------EPGHLSNEEALELLARLGP 217

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 8922122  307 KRLVLTHFSQRYKPVALAREgetdgiaelkkQAESVLDLQEVTLAEDFMVISI 359
Cdd:COG1235 218 KRLVLTHLSPDNNDHELDYD-----------ELEAALLPAGVEVAYDGMEIEL 259
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 5-192 9.55e-28

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: 107.60  E-value: 9.55e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    5 VTFLGTGAAYPSPTRGASAVVLRCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLctisLQSGS 84
Cdd:cd07719   2 VTLLGTGGPIPDPDRAGPSTLVVVGGRVYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALL----LTAWL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   85 MVSKQPIEIYGPVGLRDFiWRTMELSHTELVFHYVVHELVPTADQCPAEELKEFAhvnradsPPKeeqgrtilldseens 164
Cdd:cd07719  78 AGRKTPLPVYGPPGTRAL-VDGLLAAYALDIDYRARIGDEGRPDPGALVEVHEIA-------AGG--------------- 134

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 8922122  165 yLLFDDEQFVVKAFRLFHRI--PSFGF-------SVV 192
Cdd:cd07719 135 -VVYEDDGVKVTAFLVDHGPvpPALAYrfdtpgrSVV 170
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 5-103 3.40e-20

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: 87.22  E-value: 3.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    5 VTFLGTGAAYPSPTRGASAVVLRCEGECW-LFDCGEGTQTQLMK-----------SQLKAgritkIFITHLHGDHFFGLP 72
Cdd:cd07718   1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSiLLDCGEGTLGQLRRhygpeeadevlRNLKC-----IFISHLHADHHLGLI 75

                        90       100       110
                ....*....|....*....|....*....|.
gi 8922122   73 GLLCTISLQSGSmvSKQPIEIYGPVGLRDFI 103
Cdd:cd07718  76 RLLAERKKLFKP--PSPPLYVVAPRQLRRWL 104
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 6-110 6.79e-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: 80.77  E-value: 6.79e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    6 TFLGTGAAYPSPTRGASAvvLRCEGECWLF--DCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLCTISLQSG 83
Cdd:cd07740   1 TFLGSGDAFGSGGRLNTC--FHVASEAGRFliDCGASSLIALKRAGIDPNAIDAIFITHLHGDHFGGLPFFLLDAQFVAK 78

                        90       100
                ....*....|....*....|....*..
gi 8922122   84 smvSKQPIEIYGPVGLRDFIWRTMELS 110
Cdd:cd07740  79 ---RTRPLTIAGPPGLRERLRRAMEAL 102
GntH_guanitoxin NF041257
guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;
3-109 1.04e-14

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;


Pssm-ID: 469157 [Multi-domain]  Cd Length: 372  Bit Score: 74.66  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122     3 MDVTFLGTGAayPSPTRG-ASAVVL----RCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLCT 77
Cdd:NF041257  13 MRITFLGSGP--PPPRRGqANTSILvelgNGERDKFFFDIGSGSVANIIALQIPYNLLNKVFITHLHVDHYGDLPYLYPF 90

                         90       100       110
                 ....*....|....*....|....*....|..
gi 8922122    78 ISLqSGSMVskqPIEIYGPVGlrdfiwRTMEL 109
Cdd:NF041257  91 GAW-SGRWT---PLRVWGPSG------RTPEL 112
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 5-140 5.71e-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: 66.31  E-value: 5.71e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    5 VTFLGTGAAYPSPTRGASAVVLRCEGECWLFDCGEGTQTQLMK----SQLKAgritkIFITHLHGDHFFGLPGLLCTISL 80
Cdd:cd07716   2 LTVLGCSGSYPGPGGACSGYLLEADGFRILLDCGSGVLSRLQRyidpEDLDA-----VVLSHLHPDHCADLGVLQYARRY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   81 QSGSMVsKQPIEIYGPVGLRDFIWRTMELSHT-----------------ELVFHYVVHE--------------LVPTADQ 129
Cdd:cd07716  77 HPRGAR-KPPLPLYGPAGPAERLAALYGLEDVfdfhpiepgepleigpfTITFFRTVHPvpcyamriedggkvLVYTGDT 155

                       170
                ....*....|.
gi 8922122  130 CPAEELKEFAH 140
Cdd:cd07716 156 GYCDELVEFAR 166
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 22-111 8.09e-12

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: 63.34  E-value: 8.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122      22 SAVVLRCEGECWLFDCGEGTQTQLMKSQLKAG--RITKIFITHLHGDHFFGLPGLLctislqsgsmvSKQPIEIYGPVGL 99
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGpkKIDAIILTHGHPDHIGGLPELL-----------EAPGAPVYAPEGT 69

                           90
                   ....*....|..
gi 8922122     100 RDFIWRTMELSH 111
Cdd:smart00849  70 AELLKDLLALLG 81
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 34-314 1.19e-08

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: 54.24  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122     34 LFDCGEGTQTQLMK----SQLKAGRITKIFITHLHGDHFFGLPGLLCTislqsgsmvskQPIEIYGPVGLRDFIWRTMEL 109
Cdd:pfam12706   4 LIDPGPDLRQQALPalqpGRLRDDPIDAVLLTHDHYDHLAGLLDLREG-----------RPRPLYAPLGVLAHLRRNFPY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    110 SHTELVFHYVVHELVPtadqcpaeelkefahvnradsppkeeqgrtilldseensyllfdDEQFVVKAFRL-FHRIPSFG 188
Cdd:pfam12706  73 LFLLEHYGVRVHEIDW--------------------------------------------GESFTVGDGGLtVTATPARH 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    189 FSvvekkrpgklnaqkLKDLGVPPGPAYGklkngisVVLENGvtispqdvlkkpivGRKICILGDCsGVVGDGGVKLCFE 268
Cdd:pfam12706 109 GS--------------PRGLDPNPGDTLG-------FRIEGP--------------GKRVYYAGDT-GYFPDEIGERLGG 152

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 8922122    269 ADLLIHEATLDDAqmDKAKEHGHSTPQMAATFAKLCRAKRLVLTHF 314
Cdd:pfam12706 153 ADLLLLDGGAWRD--DEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 3-96 2.34e-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: 53.63  E-value: 2.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    3 MDVTFLGTGAAYPSPT----------------RGASAVVLRCEGECWLFDCGEGTQTQLMKSQLKagRITKIFITHLHGD 66
Cdd:cd16279   1 MKLTFLGTGTSSGVPVigcdcgvcdssdpknrRLRSSILIETGGKNILIDTGPDFRQQALRAGIR--KLDAVLLTHAHAD 78

                        90       100       110
                ....*....|....*....|....*....|
gi 8922122   67 HFFGLPGllctisLQSGSMVSKQPIEIYGP 96
Cdd:cd16279  79 HIHGLDD------LRPFNRLQQRPIPVYAS 102
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 25-75 3.19e-07

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: 49.98  E-value: 3.19e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 8922122   25 VLRCE-GECWLFDCGEGTQTQLMKSQLKAG-RITKIFITHLHGDHFFGLPGLL 75
Cdd:cd06262  14 LVSDEeGEAILIDPGAGALEKILEAIEELGlKIKAILLTHGHFDHIGGLAELK 66
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 12-74 3.39e-07

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: 50.46  E-value: 3.39e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8922122   12 AAYPSPTRGASAVVLRCEGECWLFDCG-EGTQTQLMKSQLKA--GRITKIFITHLHGDHFFGLPGL 74
Cdd:COG0491   6 GGTPGAGLGVNSYLIVGGDGAVLIDTGlGPADAEALLAALAAlgLDIKAVLLTHLHPDHVGGLAAL 71
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 3-96 5.05e-07

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: 49.54  E-value: 5.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    3 MDVTFLGTGAA------------------YPSPTRGASAVVLRCEGECWLFDCGEgtqTQLMkSQLKAGRITKIFITHLH 64
Cdd:cd07736   1 MKLTFLGTGDAggvpvygcdcsacqrarqDPSYRRRPCSALIEVDGERILLDAGL---TDLA-ERFPPGSIDAILLTHFH 76

                        90       100       110
                ....*....|....*....|....*....|..
gi 8922122   65 GDHFFGLpgllctISLQSGsmvSKQPIEIYGP 96
Cdd:cd07736  77 MDHVQGL------FHLRWG---VGDPIPVYGP 99
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
19-75 5.32e-07

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 49.67  E-value: 5.32e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8922122     19 RGASAVVLRCEGECWLFDCGEGTQTQLMKSQLKAG----RITKIFITHLHGDHFFGLPGLL 75
Cdd:pfam00753   4 GQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGlgpkDIDAVILTHGHFDHIGGLGELA 64
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 22-291 2.58e-06

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: 47.88  E-value: 2.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   22 SAVVLRCEGECWLFDCGEGTQ---TQLMKSQlKAGRITkIFITHLHGDHFFGLPglLCTISLQSGSMvskqpIEIYGPV- 97
Cdd:cd07715  24 SCVEVRAGGELLILDAGTGIRelgNELMKEG-PPGEAH-LLLSHTHWDHIQGFP--FFAPAYDPGNR-----IHIYGPHk 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   98 ---GLRDFIWRTMELSHtelvFhyvvhelvP-TADQCPAEelKEFAHVnradsppkeEQGRTILLDSeensyllfddeqF 173
Cdd:cd07715  95 dggSLEEVLRRQMSPPY----F--------PvPLEELLAA--IEFHDL---------EPGEPFSIGG------------V 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122  174 VVKAFRLFHripsfgfsvvekkrpgklnaqklkdlgvpPGPAYG-KLKNGisvvlengvtispqdvlkkpivGRKICILG 252
Cdd:cd07715 140 TVTTIPLNH-----------------------------PGGALGyRIEED----------------------GKSVVYAT 168

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 8922122  253 DCSGVVGDGG-----VKLCFEADLLIHEATLDDAQMDKAKEHGH 291
Cdd:cd07715 169 DTEHYPDDGEsdealLEFARGADLLIHDAQYTDEEYPSKRGWGH 212
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 21-78 3.51e-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: 46.87  E-value: 3.51e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 8922122   21 ASAVVLRCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLCTI 78
Cdd:cd16296  12 GAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTL 69
PRK14866 PRK14866
hypothetical protein; Provisional
 201-238 1.34e-05

hypothetical protein; Provisional


Pssm-ID: 237840  Cd Length: 451  Bit Score: 46.92  E-value: 1.34e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 8922122   201 NAQKLKDLGVPPGPAYGKLKNGISVVLEnGVTISPQDV 238
Cdd:PRK14866 399 DPELARKLGVPEGPAFGKLAAGQPVEVD-GETITPEMV 435
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 15-129 1.63e-05

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 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: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 44.98  E-value: 1.63e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   15 PSPTRGASAVVLRCEGECWLFDCGEGTQ-------TQLMKSQLKAGRITKIFITHLHGDHFfglpGLLCTISLQSGSMVS 87
Cdd:cd07725   9 PGPLGHVNVYLLRDGDETTLIDTGLATEedaealwEGLKELGLKPSDIDRVLLTHHHPDHI----GLAGKLQEKSGATVY 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 8922122   88 KQPieiYGPVGLRDFI------WRTMELS-HT--ELVFHYVVHELVPTADQ 129
Cdd:cd07725  85 ILD---VTPVKDGDKIdlgglrLKVIETPgHTpgHIVLYDEDRRELFVGDA 132
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 10-64 1.85e-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: 41.81  E-value: 1.85e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 8922122     10 TGAAYPSP-TRGASaVVLRCEGECWLF-DCGEGTQTQLMKSQLKAGRITKIFITHLH 64
Cdd:pfam13691   1 QVVTTPTAdTPGPL-LLLHFDSKRYLFgNVGEGTQRALNEQKVRLSKLEDIFLTGKV 56
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 33-94 3.27e-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: 44.06  E-value: 3.27e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8922122   33 WLFDCGEG------TQTQLMKSQLKAgRITKIFITHLHGDHFFGLPGLLctislqsgSMVSKQPIEIY 94
Cdd:cd07722  30 ILIDTGEGrpsyipLLKSVLDSEGNA-TISDILLTHWHHDHVGGLPDVL--------DLLRGPSPRVY 88
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 22-71 4.00e-05

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: 44.46  E-value: 4.00e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   22 SAVVLRCEGECWLFDCGEG-----TQTQLMKSqLKA-----GRITKIFITHLHGDHFFGL 71
Cdd:cd07720  50 NAFLVRTGGRLILVDTGAGglfgpTAGKLLAN-LAAagidpEDIDDVLLTHLHPDHIGGL 108
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 3-75 1.12e-04

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: 1.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122    3 MDVTFLGTGaaypsptRGASAVVLRCEGECWLFDCGEGTQTQLMKS----QLKAGRITKI---FITHLHGDHFFGLPGLL 75
Cdd:COG2333   1 LRVTFLDVG-------QGDAILIRTPDGKTILIDTGPRPSFDAGERvvlpYLRALGIRRLdllVLTHPDADHIGGLAAVL 73
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 54-75 1.26e-04

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 42.49  E-value: 1.26e-04
                        10        20
                ....*....|....*....|..
gi 8922122   54 RITKIFITHLHGDHFFGLPGLL 75
Cdd:cd07739  52 TLTTIYITHGHPDHYFGLEVLL 73
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 23-75 2.88e-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: 2.88e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 8922122   23 AVVLRCEGECWLFDCGEGTQT--QLMKSQLKAGRITKI---FITHLHGDHFFGLPGLL 75
Cdd:cd07731  12 AILIQTPGKTILIDTGPRDSFgeDVVVPYLKARGIKKLdylILTHPDADHIGGLDAVL 69
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 23-110 3.31e-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: 37.63  E-value: 3.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922122   23 AVVLRCEGECWLFDCGEG---TQTQLMKSQLKAGRITKIFITHLHGDHFFGLpgllctislqsGSMVSKQPIEIYGPVGl 99
Cdd:cd07733  11 CTYLETEDGKLLIDAGLSgrkITGRLAEIGRDPEDIDAILVTHEHADHIKGL-----------GVLARKYNVPIYATAG- 78

                        90
                ....*....|.
gi 8922122  100 rdfIWRTMELS 110
Cdd:cd07733  79 ---TLRAMERK 86
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 3-67 4.35e-03

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 38.63  E-value: 4.35e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8922122    3 MDVTFLGtgAAypsPTRGASAVVLRCEGECWLFDCG---EGTQTQLMKSQLKAGRITKIFITHLHGDH 67
Cdd:COG1236   1 MKLTFLG--AA---GEVTGSCYLLETGGTRILIDCGlfqGGKERNWPPFPFRPSDVDAVVLTHAHLDH 63
 
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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