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Conserved domains on  [gi|1080386478|gb|OFL73871|]
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MBL fold metallo-hydrolase [Corynebacterium sp. HMSC077C02]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11440933)

MBL fold metallo-hydrolase similar to Methanopyrus kandleri ribonuclease Z

Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-258 3.02e-73

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


:

Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 223.92  E-value: 3.02e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   1 MRLKVLGCTGSMGGPSAPASGYLIELDnGRTFVIDLGPGVLAELQKIS-DPAACD-LLLTHVHPDHTADIPGLLVWRRFH 78
Cdd:COG1234     1 MKLTFLGTGGAVPTPGRATSSYLLEAG-GERLLIDCGEGTQRQLLRAGlDPRDIDaIFITHLHGDHIAGLPGLLSTRSLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  79 PtapaSSRNL-LVGPGDIHDRIGTMCKALGSEEDANLEdtFDQVvsNPGEPLlvgggeADGGAVVTPYNMVHPVPAVGYR 157
Cdd:COG1234    80 G----REKPLtIYGPPGTKEFLEALLKASGTDLDFPLE--FHEI--EPGEVF------EIGGFTVTAFPLDHPVPAYGYR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478 158 IEADGLTIAYTGDTAWTDELVELARDADIFICEATWCSNEEG-TPPDMHLTGYEAGKAATLAGVKKLVLTHIPP-YADGE 235
Cdd:COG1234   146 FEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAElAKETGHSTAKEAAELAAEAGVKRLVLTHFSPrYDDPE 225

                         250       260
                  ....*....|....*....|...
gi 1080386478 236 EALRAAKSTFAGDVELAYLGMEL 258
Cdd:COG1234   226 ELLAEARAVFPGPVELAEDGMVI 248
 
Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-258 3.02e-73

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 223.92  E-value: 3.02e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   1 MRLKVLGCTGSMGGPSAPASGYLIELDnGRTFVIDLGPGVLAELQKIS-DPAACD-LLLTHVHPDHTADIPGLLVWRRFH 78
Cdd:COG1234     1 MKLTFLGTGGAVPTPGRATSSYLLEAG-GERLLIDCGEGTQRQLLRAGlDPRDIDaIFITHLHGDHIAGLPGLLSTRSLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  79 PtapaSSRNL-LVGPGDIHDRIGTMCKALGSEEDANLEdtFDQVvsNPGEPLlvgggeADGGAVVTPYNMVHPVPAVGYR 157
Cdd:COG1234    80 G----REKPLtIYGPPGTKEFLEALLKASGTDLDFPLE--FHEI--EPGEVF------EIGGFTVTAFPLDHPVPAYGYR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478 158 IEADGLTIAYTGDTAWTDELVELARDADIFICEATWCSNEEG-TPPDMHLTGYEAGKAATLAGVKKLVLTHIPP-YADGE 235
Cdd:COG1234   146 FEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAElAKETGHSTAKEAAELAAEAGVKRLVLTHFSPrYDDPE 225

                         250       260
                  ....*....|....*....|...
gi 1080386478 236 EALRAAKSTFAGDVELAYLGMEL 258
Cdd:COG1234   226 ELLAEARAVFPGPVELAEDGMVI 248
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 2-191 7.43e-68

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: 207.68  E-value: 7.43e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   2 RLKVLGCTGSMGGPSAPASGYLIELDNGRtFVIDLGPGVLAELQKISDPAACD-LLLTHVHPDHTADIPGLLVWRRFHPT 80
Cdd:cd07716     1 KLTVLGCSGSYPGPGGACSGYLLEADGFR-ILLDCGSGVLSRLQRYIDPEDLDaVVLSHLHPDHCADLGVLQYARRYHPR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  81 APASSRNLLVGPGDIHDRIGTMckalgseedANLEDTFDQVVSNPGEPLLVGGgeadggAVVTPYNMVHPVPAVGYRIEA 160
Cdd:cd07716    80 GARKPPLPLYGPAGPAERLAAL---------YGLEDVFDFHPIEPGEPLEIGP------FTITFFRTVHPVPCYAMRIED 144

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1080386478 161 DGLTIAYTGDTAWTDELVELARDADIFICEA 191
Cdd:cd07716   145 GGKVLVYTGDTGYCDELVEFARGADLLLCEA 175
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-258 4.88e-35

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 126.45  E-value: 4.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   1 MRLKVLGCTGSMGGPSAPASGYLIELDnGRTFVIDLGPGVLAEL--QKISdPAACD-LLLTHVHPDHTADIPGLL----V 73
Cdd:PRK00055    2 MELTFLGTGSGVPTPTRNVSSILLRLG-GELFLFDCGEGTQRQLlkTGIK-PRKIDkIFITHLHGDHIFGLPGLLstrsL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  74 WRRFHPT---APASSR----NLLVGPGDI------HDRIGTmckaLGSEEDANLEDTFDQVVSNpgepLLVGGG-EADGG 139
Cdd:PRK00055   80 SGRTEPLtiyGPKGIKefveTLLRASGSLgyriaeKDKPGK----LDAEKLKALGVPPGPLFGK----LKRGEDvTLEDG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478 140 AVVTPynmvhpvpAVGYRIEADGLTIAYTGDTAWTDELVELARDADIFICEATWCSNEEGTP-PDMHLTGYEAGKAATLA 218
Cdd:PRK00055  152 RIINP--------ADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEELAkEYGHSTARQAAEIAKEA 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1080386478 219 GVKKLVLTHI-PPYADGEEALRA-AKSTFaGDVELAYLGMEL 258
Cdd:PRK00055  224 GVKRLILTHFsPRYTGDPEELLKeAREIF-PNTELAEDLMRV 264
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 30-228 1.40e-17

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: 78.12  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  30 RTFVIDLGPGVLAELQKISDPAACD------LLLTHVHPDHTADIPGLlvwRRFHPTApassrnlLVGPGDIHDRIgtmc 103
Cdd:pfam12706   1 RRILIDPGPDLRQQALPALQPGRLRddpidaVLLTHDHYDHLAGLLDL---REGRPRP-------LYAPLGVLAHL---- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478 104 KALGSEEDANLEDTFDQVVSNPGEPLLVGggeaDGGAVVTP---------YNMVHPVPAVGYRIEADGLTIAYTGDTA-W 173
Cdd:pfam12706  67 RRNFPYLFLLEHYGVRVHEIDWGESFTVG----DGGLTVTAtparhgsprGLDPNPGDTLGFRIEGPGKRVYYAGDTGyF 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1080386478 174 TDELVELARDADIFICEATWCSNEEgtPPDM-HLTGYEAGKAATLAGVKKLVLTHI 228
Cdd:pfam12706 143 PDEIGERLGGADLLLLDGGAWRDDE--MIHMgHMTPEEAVEAAADLGARRKVLIHI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 20-185 2.33e-07

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: 49.47  E-value: 2.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   20 SGYLIElDNGRTFVIDLGPG----VLAELQKISDPAACDLLLTHVHPDHTADIPGLLvwRRFHPTapassrnlLVGPGDI 95
Cdd:smart00849   1 NSYLVR-DDGGAILIDTGPGeaedLLAELKKLGPKKIDAIILTHGHPDHIGGLPELL--EAPGAP--------VYAPEGT 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   96 HDRIGTMCKALGSEEDANLEDTFDQVVsNPGEPLLVGGGEADggavvtpynmVHPVPA-----VGYRIEADGltIAYTGD 170
Cdd:smart00849  70 AELLKDLLALLGELGAEAEPAPPDRTL-KDGDELDLGGGELE----------VIHTPGhtpgsIVLYLPEGK--ILFTGD 136

                          170
                   ....*....|....*
gi 1080386478  171 TAWTDELVELARDAD 185
Cdd:smart00849 137 LLFAGGDGRTLVDGG 151
 
Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-258 3.02e-73

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 223.92  E-value: 3.02e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   1 MRLKVLGCTGSMGGPSAPASGYLIELDnGRTFVIDLGPGVLAELQKIS-DPAACD-LLLTHVHPDHTADIPGLLVWRRFH 78
Cdd:COG1234     1 MKLTFLGTGGAVPTPGRATSSYLLEAG-GERLLIDCGEGTQRQLLRAGlDPRDIDaIFITHLHGDHIAGLPGLLSTRSLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  79 PtapaSSRNL-LVGPGDIHDRIGTMCKALGSEEDANLEdtFDQVvsNPGEPLlvgggeADGGAVVTPYNMVHPVPAVGYR 157
Cdd:COG1234    80 G----REKPLtIYGPPGTKEFLEALLKASGTDLDFPLE--FHEI--EPGEVF------EIGGFTVTAFPLDHPVPAYGYR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478 158 IEADGLTIAYTGDTAWTDELVELARDADIFICEATWCSNEEG-TPPDMHLTGYEAGKAATLAGVKKLVLTHIPP-YADGE 235
Cdd:COG1234   146 FEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAElAKETGHSTAKEAAELAAEAGVKRLVLTHFSPrYDDPE 225

                         250       260
                  ....*....|....*....|...
gi 1080386478 236 EALRAAKSTFAGDVELAYLGMEL 258
Cdd:COG1234   226 ELLAEARAVFPGPVELAEDGMVI 248
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 2-191 7.43e-68

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: 207.68  E-value: 7.43e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   2 RLKVLGCTGSMGGPSAPASGYLIELDNGRtFVIDLGPGVLAELQKISDPAACD-LLLTHVHPDHTADIPGLLVWRRFHPT 80
Cdd:cd07716     1 KLTVLGCSGSYPGPGGACSGYLLEADGFR-ILLDCGSGVLSRLQRYIDPEDLDaVVLSHLHPDHCADLGVLQYARRYHPR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  81 APASSRNLLVGPGDIHDRIGTMckalgseedANLEDTFDQVVSNPGEPLLVGGgeadggAVVTPYNMVHPVPAVGYRIEA 160
Cdd:cd07716    80 GARKPPLPLYGPAGPAERLAAL---------YGLEDVFDFHPIEPGEPLEIGP------FTITFFRTVHPVPCYAMRIED 144

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1080386478 161 DGLTIAYTGDTAWTDELVELARDADIFICEA 191
Cdd:cd07716   145 GGKVLVYTGDTGYCDELVEFARGADLLLCEA 175
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 3-258 3.08e-40

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: 139.12  E-value: 3.08e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   3 LKVLGCTGSMGGPSAPASGYLIELdNGRTFVIDLGPGVLAELQK--ISDPAACDLLLTHVHPDHTADIPGLLvwrrfhpt 80
Cdd:cd07717     1 LTFLGTGSAVPTPERNLSSIALRL-EGELWLFDCGEGTQRQLLRagLSPSKIDRIFITHLHGDHILGLPGLL-------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  81 apaSSRNL--------LVGPGDIHDRIGTMCKALGSEEDANLEdtFDQVVSNPGEPLLvgggeaDGGAVVTPYNMVHPVP 152
Cdd:cd07717    72 ---STMSLlgrtepltIYGPKGLKEFLETLLRLSASRLPYPIE--VHELEPDPGLVFE------DDGFTVTAFPLDHRVP 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478 153 AVGYRIEAdGLTIAYTGDTAWTDELVELARDADIFICEATWCSNEEGTPPD-MHLTGYEAGKAATLAGVKKLVLTHIPP- 230
Cdd:cd07717   141 CFGYRFEE-GRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKAKEtGHSTAKQAAEIAKKAGVKKLVLTHFSAr 219

                         250       260
                  ....*....|....*....|....*...
gi 1080386478 231 YADGEEALRAAKSTFaGDVELAYLGMEL 258
Cdd:cd07717   220 YKDPEELLKEARAVF-PNTILAEDFMTI 246
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-258 4.88e-35

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 126.45  E-value: 4.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   1 MRLKVLGCTGSMGGPSAPASGYLIELDnGRTFVIDLGPGVLAEL--QKISdPAACD-LLLTHVHPDHTADIPGLL----V 73
Cdd:PRK00055    2 MELTFLGTGSGVPTPTRNVSSILLRLG-GELFLFDCGEGTQRQLlkTGIK-PRKIDkIFITHLHGDHIFGLPGLLstrsL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  74 WRRFHPT---APASSR----NLLVGPGDI------HDRIGTmckaLGSEEDANLEDTFDQVVSNpgepLLVGGG-EADGG 139
Cdd:PRK00055   80 SGRTEPLtiyGPKGIKefveTLLRASGSLgyriaeKDKPGK----LDAEKLKALGVPPGPLFGK----LKRGEDvTLEDG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478 140 AVVTPynmvhpvpAVGYRIEADGLTIAYTGDTAWTDELVELARDADIFICEATWCSNEEGTP-PDMHLTGYEAGKAATLA 218
Cdd:PRK00055  152 RIINP--------ADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEELAkEYGHSTARQAAEIAKEA 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1080386478 219 GVKKLVLTHI-PPYADGEEALRA-AKSTFaGDVELAYLGMEL 258
Cdd:PRK00055  224 GVKRLILTHFsPRYTGDPEELLKeAREIF-PNTELAEDLMRV 264
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-258 1.45e-34

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 124.62  E-value: 1.45e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   1 MRLKVLGCTGSMGGP--------SAPA--------SGYLIElDNGRTFVIDLGPGV----LAELQKISDPAAcdLLLTHV 60
Cdd:COG1235     1 MKVTFLGSGSSGGVPqigcdcpvCASTdprygrtrSSILVE-ADGTRLLIDAGPDLreqlLRLGLDPSKIDA--ILLTHE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  61 HPDHTAdipGLLVWRRFHPTAPASsrnlLVGPGDIHDRIGTMCKALGSEEDANLedtfDQVVSNPGEPLLVGGGEadgga 140
Cdd:COG1235    78 HADHIA---GLDDLRPRYGPNPIP----VYATPGTLEALERRFPYLFAPYPGKL----EFHEIEPGEPFEIGGLT----- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478 141 vVTPYNMVHP-VPAVGYRIEADGLTIAYTGDTA-WTDELVELARDADIFICEATWCSNEEGtppdmHLTGYEAGKAATLA 218
Cdd:COG1235   142 -VTPFPVPHDaGDPVGYRIEDGGKKLAYATDTGyIPEEVLELLRGADLLILDATYDDPEPG-----HLSNEEALELLARL 215

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1080386478 219 GVKKLVLTHI---PPYADGEEALRAAKSTFAGdVELAYLGMEL 258
Cdd:COG1235   216 GPKRLVLTHLspdNNDHELDYDELEAALLPAG-VEVAYDGMEI 257
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 3-191 4.13e-34

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: 121.22  E-value: 4.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   3 LKVLGcTGSmGGPSA--PASGYLIELDNGRtFVIDLGPGVLAEL-QKISDPAACD-LLLTHVHPDHTADIPGLLV-WRRF 77
Cdd:cd16272     1 LTFLG-TGG-AVPSLtrNTSSYLLETGGTR-ILLDCGEGTVYRLlKAGVDPDKLDaIFLSHFHLDHIGGLPTLLFaRRYG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  78 HPTAPASsrnlLVGPGDIHDRIGTMCKALGSEEDANLEDTFdqvvsnpgEPLLVGGGEA-DGGAVVTPYNMVHPVPAVGY 156
Cdd:cd16272    78 GRKKPLT----IYGPKGIKEFLEKLLNFPVEILPLGFPLEI--------EELEEGGEVLeLGDLKVEAFPVKHSVESLGY 145

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1080386478 157 RIEADGLTIAYTGDTAWTDELVELARDADIFICEA 191
Cdd:cd16272   146 RIEAEGKSIVYSGDTGPCENLVELAKGADLLIHEC 180
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 4-193 6.71e-29

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: 108.12  E-value: 6.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   4 KVLGCTGSMGGPSAPASGYLIELDNGRtFVIDLGPGVLAELQKIS-DPAACD-LLLTHVHPDHTADIPGLL-----VWRR 76
Cdd:cd07740     1 TFLGSGDAFGSGGRLNTCFHVASEAGR-FLIDCGASSLIALKRAGiDPNAIDaIFITHLHGDHFGGLPFFLldaqfVAKR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  77 fhpTAPASsrnlLVGPGDIHDRIGTMCKAL---GSEEDANLEDTFDQVVsnPGEPLLVGGgeadggAVVTPYNMVHPVPA 153
Cdd:cd07740    80 ---TRPLT----IAGPPGLRERLRRAMEALfpgSSKVPRRFDLEVIELE--PGEPTTLGG------VTVTAFPVVHPSGA 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1080386478 154 VGY--RIEADGLTIAYTGDTAWTDELVELARDADIFICEATW 193
Cdd:cd07740   145 LPLalRLEAAGRVLAYSGDTEWTDALVPLARGADLFICECYF 186
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 2-188 1.77e-23

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


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 93.73  E-value: 1.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   2 RLKVLGcTGS-MGGPSAPASGYLIELDnGRTFVIDLGPGVLAELQKISDPAAcDL---LLTHVHPDHTADIPGLLVWRrf 77
Cdd:cd07719     1 RVTLLG-TGGpIPDPDRAGPSTLVVVG-GRVYLVDAGSGVVRRLAQAGLPLG-DLdavFLTHLHSDHVADLPALLLTA-- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  78 hPTAPASSRNLLVGPGDIHDRIGTMCKALGSEEDANLEDtFDQVVSNPGEPLLV------GGGEADGGAVVTPYNMVHPV 151
Cdd:cd07719    76 -WLAGRKTPLPVYGPPGTRALVDGLLAAYALDIDYRARI-GDEGRPDPGALVEVheiaagGVVYEDDGVKVTAFLVDHGP 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1080386478 152 --PAVGYRIEADGLTIAYTGDTAWTDELVELARDADIFI 188
Cdd:cd07719   154 vpPALAYRFDTPGRSVVFSGDTGPSENLIELAKGADLLV 192
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 21-227 1.10e-19

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: 84.16  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  21 GYLIELdNGRTFVIDLGPGVLAELQKIS-DPAACD-LLLTHVHPDHTADIPGLL------VWRRfhptapassRNLLVGP 92
Cdd:cd07741    22 GIWIEL-NGKNIHIDPGPGALVRMCRPKlDPTKLDaIILSHRHLDHSNDANVLIeamtegGFKK---------RGTLLAP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  93 GDihdrigtmckALGSEED---ANLEDTFDQVVsnpgepLLVGGGEAD-GGAVVTPYNMVHPVPA-VGYRIEADGLTIAY 167
Cdd:cd07741    92 ED----------ALNGEPVvllYYHRRKLEEIE------ILEEGDEYElGGIKIEATRHKHSDPTtYGFIFRTSDKKIGY 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478 168 TGDTAWTDELVELARDADIFICEATWCSNEEGTppdMHLTGYEAGKAATLAGVKKLVLTH 227
Cdd:cd07741   156 ISDTRYFEELIEYYSNCDVLIINVTRPRPRKGV---DHLSVEDVEKILKEIKPKLAILTH 212
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 28-192 2.13e-18

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: 81.00  E-value: 2.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  28 NGRTFVIDLGPG--VLA-ELQKISDPAACDLLLTHVHPDHT--------ADIPGllvwRRFH----PTAPASSRNLL--- 89
Cdd:cd07715    31 GGELLILDAGTGirELGnELMKEGPPGEAHLLLSHTHWDHIqgfpffapAYDPG----NRIHiygpHKDGGSLEEVLrrq 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  90 -------VGPGDIHDRIgtmckalgseedanledTFDQVVsnPGEPLLVGGgeadggAVVTPYNMVHPVPAVGYRIEADG 162
Cdd:cd07715   107 msppyfpVPLEELLAAI-----------------EFHDLE--PGEPFSIGG------VTVTTIPLNHPGGALGYRIEEDG 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1080386478 163 LTIAYTGDT-------AWTDELVELARDADIFICEAT 192
Cdd:cd07715   162 KSVVYATDTehypddgESDEALLEFARGADLLIHDAQ 198
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 30-228 1.40e-17

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: 78.12  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  30 RTFVIDLGPGVLAELQKISDPAACD------LLLTHVHPDHTADIPGLlvwRRFHPTApassrnlLVGPGDIHDRIgtmc 103
Cdd:pfam12706   1 RRILIDPGPDLRQQALPALQPGRLRddpidaVLLTHDHYDHLAGLLDL---REGRPRP-------LYAPLGVLAHL---- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478 104 KALGSEEDANLEDTFDQVVSNPGEPLLVGggeaDGGAVVTP---------YNMVHPVPAVGYRIEADGLTIAYTGDTA-W 173
Cdd:pfam12706  67 RRNFPYLFLLEHYGVRVHEIDWGESFTVG----DGGLTVTAtparhgsprGLDPNPGDTLGFRIEGPGKRVYYAGDTGyF 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1080386478 174 TDELVELARDADIFICEATWCSNEEgtPPDM-HLTGYEAGKAATLAGVKKLVLTHI 228
Cdd:pfam12706 143 PDEIGERLGGADLLLLDGGAWRDDE--MIHMgHMTPEEAVEAAADLGARRKVLIHI 196
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 6-192 5.92e-15

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: 71.43  E-value: 5.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   6 LGcTGSmggpSAPA-----SGYLIELDNGRTFVIDLGPGVLAELQKISDPAACDLLL--------THVHPDHTADIPGLL 72
Cdd:cd07718     4 LG-TGS----AIPSkyrnvSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEEADEVLrnlkcifiSHLHADHHLGLIRLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  73 VwRRFHPTAPASSRNLLVGP----------GDIHDRIGTMCKALGSEEDANLEDTFDQVVSNPGEPLLvgggEADGGAVV 142
Cdd:cd07718    79 A-ERKKLFKPPSPPLYVVAPrqlrrwlreySSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLL----EELGLKSI 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1080386478 143 TPYNMVHPVPAVGYRIE-ADGLTIAYTGDTAWTDELVELARDADIFICEAT 192
Cdd:cd07718   154 ETVPVIHCPDAYGIVLThEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 20-241 1.45e-13

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 68.02  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  20 SGYLIELDnGRTFVID-----LGPGVLAELQKISDPAACDL-LLTHVHPDHtADIPGLLVWRRFHPTapassrnlLVGPG 93
Cdd:COG2220    12 ATFLIETG-GKRILIDpvfsgRASPVNPLPLDPEDLPKIDAvLVTHDHYDH-LDDATLRALKRTGAT--------VVAPL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  94 DIHDRIgtmcKALGseedanledtFDQVVS-NPGEPLLVGGGEadggavVTPYNMVHPV--------PAVGYRIEADGLT 164
Cdd:COG2220    82 GVAAWL----RAWG----------FPRVTElDWGESVELGGLT------VTAVPARHSSgrpdrnggLWVGFVIETDGKT 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478 165 IAYTGDTAWTDELVELAR--DADIFICEAtwcsneegTPPDMHLTGYEAGKAATLAGVKKLVLTH----IPPYADGEEAL 238
Cdd:COG2220   142 IYHAGDTGYFPEMKEIGErfPIDVALLPI--------GAYPFTMGPEEAAEAARDLKPKVVIPIHygtfPLLDEDPLERF 213


                  ...
gi 1080386478 239 RAA 241
Cdd:COG2220   214 AAA 216
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-192 1.08e-09

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 57.89  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   1 MRLKVLGCTGSMGGpsapaSGYLIELDNGRtFVIDLG--PGVLAEL-----QKISDPAAcdLLLTHVHPDHTADIPgLLV 73
Cdd:COG1236     1 MKLTFLGAAGEVTG-----SCYLLETGGTR-ILIDCGlfQGGKERNwppfpFRPSDVDA--VVLTHAHLDHSGALP-LLV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  74 WRRFHP---TAPAS---SRNLLVGPGDIHDRIGTMcKALGSEEDAnlEDTFDQVVS-NPGEPLLVGGGEadggavVTPYN 146
Cdd:COG1236    72 KEGFRGpiyATPATadlARILLGDSAKIQEEEAEA-EPLYTEEDA--ERALELFQTvDYGEPFEIGGVR------VTFHP 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1080386478 147 MVHpVP-AVGYRIEADGLTIAYTGDTAWTDELV----ELARDADIFICEAT 192
Cdd:COG1236   143 AGH-ILgSAQVELEVGGKRIVFSGDYGREDDPLlappEPVPPADVLITEST 192
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 1-172 1.09e-08

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: 53.40  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   1 MRLKVLGcTGSMGG-----------------PSA---PASGYlIELDNGRTfVIDLGpgvLAELQKISDPAACD-LLLTH 59
Cdd:cd07736     1 MKLTFLG-TGDAGGvpvygcdcsacqrarqdPSYrrrPCSAL-IEVDGERI-LLDAG---LTDLAERFPPGSIDaILLTH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  60 VHPDHTAdipGLLVWRR--------FHPTAPASSRNLLVGPGDIHdrigtmckalgseedanledtFdQVVSNPGEPLLV 131
Cdd:cd07736    75 FHMDHVQ---GLFHLRWgvgdpipvYGPPDPQGCADLFKHPGILD---------------------F-QPLVAPFQSFEL 129

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1080386478 132 GGGEadggavVTPYNMVHPVPAVGYRIEADGLTIAYTGDTA 172
Cdd:cd07736   130 GGLK------ITPLPLNHSKPTFGYLLESGGKRLAYLTDTL 164
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 1-191 1.29e-07

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: 50.55  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   1 MRLKVLGCTGSMGGPS--------APASGY--------LIELDnGRTFVIDLGPG----VLAElqKISDPAAcdLLLTHV 60
Cdd:cd16279     1 MKLTFLGTGTSSGVPVigcdcgvcDSSDPKnrrlrssiLIETG-GKNILIDTGPDfrqqALRA--GIRKLDA--VLLTHA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  61 HPDHTADIPGLLVWRRFHPtapassrnllvGPGDIH------DRIGTMCKALGSEEDANLEDTFDQVVSNPGEPLLVGGG 134
Cdd:cd16279    76 HADHIHGLDDLRPFNRLQQ-----------RPIPVYaseetlDDLKRRFPYFFAATGGGGVPKLDLHIIEPDEPFTIGGL 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1080386478 135 EadggavVTPYNMVH-PVPAVGYRIEadglTIAYTGDT-AWTDELVELARDADIFICEA 191
Cdd:cd16279   145 E------ITPLPVLHgKLPSLGFRFG----DFAYLTDVsEIPEESLEKLRGLDVLILDA 193
PRK02126 PRK02126
ribonuclease Z; Provisional
 162-247 1.53e-07

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 51.45  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478 162 GLTIAYTGDTAWTDE----LVELARDADIFICEATWCSNEEgtppDM-----HLTGYEAGKAATLAGVKKLVLTHIPP-Y 231
Cdd:PRK02126  242 GQKIGYVTDIGYTEEnlarIVELAAGVDLLFIEAVFLDEDA----EKarrknHLTARQAGRLAREAGVKRLLPFHFSPrY 317

                          90
                  ....*....|....*..
gi 1080386478 232 ADGEEAL-RAAKSTFAG 247
Cdd:PRK02126  318 QGRGAELyREARAAFAG 334
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 20-185 2.33e-07

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: 49.47  E-value: 2.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   20 SGYLIElDNGRTFVIDLGPG----VLAELQKISDPAACDLLLTHVHPDHTADIPGLLvwRRFHPTapassrnlLVGPGDI 95
Cdd:smart00849   1 NSYLVR-DDGGAILIDTGPGeaedLLAELKKLGPKKIDAIILTHGHPDHIGGLPELL--EAPGAP--------VYAPEGT 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   96 HDRIGTMCKALGSEEDANLEDTFDQVVsNPGEPLLVGGGEADggavvtpynmVHPVPA-----VGYRIEADGltIAYTGD 170
Cdd:smart00849  70 AELLKDLLALLGELGAEAEPAPPDRTL-KDGDELDLGGGELE----------VIHTPGhtpgsIVLYLPEGK--ILFTGD 136

                          170
                   ....*....|....*
gi 1080386478  171 TAWTDELVELARDAD 185
Cdd:smart00849 137 LLFAGGDGRTLVDGG 151
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 55-190 2.66e-07

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. 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.


Pssm-ID: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 49.92  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  55 LLLTHVHPDHTA-------DIPgllvwrrFHPTAPasSRNLLvgpgdihdrigtmcKALGSEEDANLEDTFDQVVSNPGE 127
Cdd:cd07732    79 VLLSHAHLDHYGllnylrpDIP-------VYMGEA--TKRIL--------------KALLPFFGEGDPVPRNIRVFESGK 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080386478 128 PLLVGggeaDggAVVTPYNMVHPVP-AVGYRIEADGLTIAYTGD-------TAWTDELVE-LARDADIFICE 190
Cdd:cd07732   136 SFTIG----D--FTVTPYLVDHSAPgAYAFLIEAPGKRIFYTGDfrfhgrkPELTEAFVEkAPKNIDVLLME 201
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
22-193 1.28e-06

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 47.75  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  22 YLIElDNGRTFVIDLGPGVLAELQKISDPAACD------LLLTHVHPDHTAdipGLLVWRRFHPTAPASSRNLLVGPGDI 95
Cdd:pfam00753   9 YLIE-GGGGAVLIDTGGSAEAALLLLLAALGLGpkdidaVILTHGHFDHIG---GLGELAEATDVPVIVVAEEARELLDE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  96 HDRIGTMCKALGSEEdanledtfdqVVSNPGEPLLVGGGEADGGAVVTPYNMVHPVPAVGYRIEADGLTIAYTGDTAWTD 175
Cdd:pfam00753  85 ELGLAASRLGLPGPP----------VVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAG 154

                         170
                  ....*....|....*...
gi 1080386478 176 ELVELARDADIFICEATW 193
Cdd:pfam00753 155 EIGRLDLPLGGLLVLHPS 172
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 15-171 1.45e-05

Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase domain; Includes Dictyostelium discoideum cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A (also known as cyclic GMP-binding protein A, phosphodiesterase 5, phosphodiesterase D, and PDE5) and cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B (also known as cyclic GMP-binding protein B, phosphodiesterase 6, phosphodiesterase E, and PDE6. 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: 293824  Cd Length: 189  Bit Score: 44.59  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  15 PSAPASGYLIELdNGRTFVIDLGPGVLAELQK--ISDPAACDLLLTHVHPDHTADIPGLLVwrrfhptapASSRNLLVGP 92
Cdd:cd07738    11 PKGHTSGFIIWI-NGRGIMVDPPVNSTSYLRQngISPRLVDHVILTHCHADHDAGTFQKIL---------EEEKITLYTT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080386478  93 GDIHDRIGTMCKALGSEEDANLEDTFDQVVSNPGEPLLVGGGEADggavvTPYNmVHPVPAVGYRIEADGLTIAYTGDT 171
Cdd:cd07738    81 RTINESFLRKYAALTGLPPDFLEELFDFRPVIIGEKTKINGAEFE-----FDYS-FHSIPTIRFKVSYGGKSIAYSGDT 153
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 22-171 3.00e-05

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: 43.43  E-value: 3.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  22 YLIELDNGRTFVIDLGPGVLAELQKISDPAACDL---LLTHVHPDHTADIPGLlvwrRFHPTAPassrnLLVGPGDIhDR 98
Cdd:cd06262    13 YLVSDEEGEAILIDPGAGALEKILEAIEELGLKIkaiLLTHGHFDHIGGLAEL----KEAPGAP-----VYIHEADA-EL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080386478  99 IGTMCKALGSEEDANLEDTFDQVVSNPGEPLLVGGGEadggavVTpynmVHPVP-----AVGYRIEADGltIAYTGDT 171
Cdd:cd06262    83 LEDPELNLAFFGGGPLPPPEPDILLEDGDTIELGGLE------LE----VIHTPghtpgSVCFYIEEEG--VLFTGDT 148
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 49-170 7.87e-05

cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; MBL-fold metallo-hydrolase domain; CPSF3 (also known as cleavage and polyadenylation specificity factor 73 kDa subunit/CPSF-73) functions as a 3' endonuclease in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and in 3' end processing of metazoan histone pre-mRNAs. This subgroup also contains the yeast homolog of CPSF-73, Ysh1/Brr5 which has roles in mRNA and snoRNA synthesis. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain, and a RMMBL domain (RNA-metabolizing metallo-beta-lactamase). 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: 293850  Cd Length: 194  Bit Score: 42.57  E-value: 7.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  49 DPAACDLLL-THVHPDHTADIPGLLVWRRF-------HPTApASSRNLL-----VGPGDIHDRigtmckaLGSEEDanLE 115
Cdd:cd16292    49 DLSEIDLLLiTHFHLDHCGALPYFLQKTNFkgrvfmtHPTK-AIYKWLLsdyvrVSNISSDEM-------LYTETD--LE 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1080386478 116 DTFDQV-VSNPGEPLLVGGGEadggavVTPYNMVHPVPAVGYRIEADGLTIAYTGD 170
Cdd:cd16292   119 ASMDKIeTIDFHQEVEVNGIK------FTAYNAGHVLGAAMFMVEIAGVRVLYTGD 168
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 3-191 1.30e-03

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


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 38.98  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478   3 LKVLGCTGSMGGpsapaSGYLIELDnGRTFVID----LGPGVLAELQKIS---DPAACD-LLLTHVHPDHTADIPgLLVW 74
Cdd:cd16295     1 LTFLGAAREVTG-----SCYLLETG-GKRILLDcglfQGGKELEELNNEPfpfDPKEIDaVILTHAHLDHSGRLP-LLVK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  75 RRFHP----TAPasSRNLLvgpgDI----------HDRIGTMCKALGSEEDAnlEDTFDQVVSNP-GEPLLVGggeadGG 139
Cdd:cd16295    74 EGFRGpiyaTPA--TKDLA----ELllldsakiqeEEAEHPPAEPLYTEEDV--EKALKHFRPVEyGEPFEIG-----PG 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080386478 140 AVVTPYN--------MVHpvpavgyrIEAD-GLTIAYTGD----TAWTDELVELARDADIFICEA 191
Cdd:cd16295   141 VKVTFYDaghilgsaSVE--------LEIGgGKRILFSGDlgrkNTPLLRDPAPPPEADYLIMES 197
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 23-170 9.84e-03

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 36.37  E-value: 9.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  23 LIELDNGRTFVIDLGPG---------VLAELQK--ISDPAAcdLLLTHVHPDHTADIPGLLvwRRFHPtapassRNLLVG 91
Cdd:COG2333    15 LIRTPDGKTILIDTGPRpsfdagervVLPYLRAlgIRRLDL--LVLTHPDADHIGGLAAVL--EAFPV------GRVLVS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386478  92 PGDIHDRIGTMCKALGSEEDANLED-------TFDQV---VSNPGEPLLVGGGEADGGAVVtpynmvhpvpavgyRIEAD 161
Cdd:COG2333    85 GPPDTSETYERLLEALKEKGIPVRPcragdtwQLGGVrfeVLWPPEDLLEGSDENNNSLVL--------------RLTYG 150


                  ....*....
gi 1080386478 162 GLTIAYTGD 170
Cdd:COG2333   151 GFSFLLTGD 159
 
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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