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Conserved domains on  [gi|19112306|ref|NP_595514|]
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3'-tRNA-processing endonuclease Trz2 [Schizosaccharomyces pombe]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 413-599 4.94e-65

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: 213.18  E-value: 4.94e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 413 LGTSATCPTWRRSLSSYSVAIDG-TVIMLDCGEGAISQFFRQYGTN-TEPMLRKLKAIFITHLHSDHYLGLLNVLQAWNK 490
Cdd:cd07718   4 LGTGSAIPSKYRNVSGILLRIPGdGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAERKK 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 491 ANTNNSMHINIIGPKFLWQWLQRLKSPANLqaLLNRIIFIIA--------------KETVTTPLQLTSDLSISSVPSIHI 556
Cdd:cd07718  84 LFKPPSPPLYVVAPRQLRRWLREYSSLEDL--GLHDISFISNrvsqslpesddplsRDLLSNLLEELGLKSIETVPVIHC 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 19112306 557 NDSYSCIISHTKYGKLVYSGDTRPNEKLVKAGIGASLLLHEST 599
Cdd:cd07718 162 PDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 50-119 5.94e-13

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: 64.15  E-value: 5.94e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306    50 SVVSSLNPDSLIaPLLCVSLDNRKYLIGSMGELTQMKFRSQASNYgGKSVSVFLMPPSlqslnAWGITAG 119
Cdd:pfam13691   1 QVVTTPTADTPG-PLLLLHFDSKRYLFGNVGEGTQRALNEQKVRL-SKLEDIFLTGKV-----SWSNIGG 63
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 198-259 3.00e-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.


The actual alignment was detected with superfamily member PRK00055:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 270  Bit Score: 52.49  E-value: 3.00e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112306  198 SFNSKEAAGVFNADKALALGVPFGPSNGKLCAGEAVLSKDGTTwIYPHQVVGPPRK-RQYFYV 259
Cdd:PRK00055 111 RIAEKDKPGKLDAEKLKALGVPPGPLFGKLKRGEDVTLEDGRI-INPADVLGPPRKgRKVAYC 172
 
Name Accession Description Interval E-value
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 413-599 4.94e-65

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: 213.18  E-value: 4.94e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 413 LGTSATCPTWRRSLSSYSVAIDG-TVIMLDCGEGAISQFFRQYGTN-TEPMLRKLKAIFITHLHSDHYLGLLNVLQAWNK 490
Cdd:cd07718   4 LGTGSAIPSKYRNVSGILLRIPGdGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAERKK 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 491 ANTNNSMHINIIGPKFLWQWLQRLKSPANLqaLLNRIIFIIA--------------KETVTTPLQLTSDLSISSVPSIHI 556
Cdd:cd07718  84 LFKPPSPPLYVVAPRQLRRWLREYSSLEDL--GLHDISFISNrvsqslpesddplsRDLLSNLLEELGLKSIETVPVIHC 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 19112306 557 NDSYSCIISHTKYGKLVYSGDTRPNEKLVKAGIGASLLLHEST 599
Cdd:cd07718 162 PDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
412-668 8.56e-54

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 185.01  E-value: 8.56e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 412 VLGTSATCPTWRRSLSSYSVAIDGTVIMLDCGEGAISQFfRQYGTNtepmLRKLKAIFITHLHSDHYLGLLNVLQAWnkA 491
Cdd:COG1234   5 FLGTGGAVPTPGRATSSYLLEAGGERLLIDCGEGTQRQL-LRAGLD----PRDIDAIFITHLHGDHIAGLPGLLSTR--S 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 492 NTNNSMHINIIGPKFLWQWLQRLKSPANLQALLnRIIFIIAKETVTTPLQltsDLSISSVPSIHINDSYSCIISHTKyGK 571
Cdd:COG1234  78 LAGREKPLTIYGPPGTKEFLEALLKASGTDLDF-PLEFHEIEPGEVFEIG---GFTVTAFPLDHPVPAYGYRFEEPG-RS 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 572 LVYSGDTRPNEKLVKAGIGASLLLHESTFEDDLKHEAIQRQHSTASEALSVAQSMKAKALILTHFSQRSYDadflPPDW- 650
Cdd:COG1234 153 LVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDD----PEELl 228

                       250       260
                ....*....|....*....|..
gi 19112306 651 ----TIYPKsKTIYANDGLQWQ 668
Cdd:COG1234 229 aearAVFPG-PVELAEDGMVIE 249
PRK00055 PRK00055
ribonuclease Z; Reviewed
 412-665 7.21e-45

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 161.50  E-value: 7.21e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306  412 VLGTSATCPTWRRSLSSYSVAIDGTVIMLDCGEGAISQFFRqygTNTEPMlrKLKAIFITHLHSDHYLGLLNVLQAWNka 491
Cdd:PRK00055   6 FLGTGSGVPTPTRNVSSILLRLGGELFLFDCGEGTQRQLLK---TGIKPR--KIDKIFITHLHGDHIFGLPGLLSTRS-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306  492 NTNNSMHINIIGPKFLWQWLQRLkspanlqallnRIIF------IIAKETVTT-PLQLTSDLSISSVP---------SIH 555
Cdd:PRK00055  79 LSGRTEPLTIYGPKGIKEFVETL-----------LRASgslgyrIAEKDKPGKlDAEKLKALGVPPGPlfgklkrgeDVT 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306  556 INDSYscIISHTKY------G-KLVYSGDTRPNEKLVKAGIGASLLLHESTFEDDLKHEAIQRQHSTASEALSVAQSMKA 628
Cdd:PRK00055 148 LEDGR--IINPADVlgpprkGrKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEELAKEYGHSTARQAAEIAKEAGV 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 19112306  629 KALILTHFSQRsYDADflPPDW-----TIYPksKTIYANDGL 665
Cdd:PRK00055 226 KRLILTHFSPR-YTGD--PEELlkearEIFP--NTELAEDLM 262
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 413-646 2.46e-43

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: 158.15  E-value: 2.46e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306   413 LGTSATCPTWRRSLSSYSVAIDGTVIMLDCGEGAISQFFRqygTNTEPMlrKLKAIFITHLHSDHYLGLLNVLQAWNkaN 492
Cdd:TIGR02651   5 LGTGGGVPTKERNLPSIALKLNGELWLFDCGEGTQRQMLR---SGISPM--KIDRIFITHLHGDHILGLPGLLSTMS--F 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306   493 TNNSMHINIIGPKFLWQWLQRLkspanLQALLNRIIFIIAKETVTTPLQL--TSDLSISSVPSIHINDSYS-CIISHTKY 569
Cdd:TIGR02651  78 QGRKEPLTIYGPPGIKEFIETS-----LRVSYTYLNYPIKIHEIEEGGLVfeDDGFKVEAFPLDHSIPSLGyRFEEKDRP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306   570 G------------------------------------------------KLVYSGDTRPNEKLVKAGIGASLLLHESTFE 601
Cdd:TIGR02651 153 GkfdrekakelgippgplygklkrgetvtlidgriidpedvlgpprkgrKIAYTGDTRPCEEVIEFAKNADLLIHEATFL 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 19112306   602 DDLKHEAIQRQHSTASEALSVAQSMKAKALILTHFSQRSYDADFL 646
Cdd:TIGR02651 233 DEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDEEEL 277
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
427-635 4.05e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 74.33  E-value: 4.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306   427 SSYSVAIDGTVIMLDCGEGAISQFFRQYgTNTEPMLRKLKAIFITHLHSDHYLGLLNVLQAWNKANTNNSMHINIIGPKF 506
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLL-AALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306   507 LWQWLQRLKSPAnlqallnRIIFIIAKETVTTPLQLTSDLSISSVPSIHINDSYSCIISHTKYGKLVYSGDT---RPNEK 583
Cdd:pfam00753  86 LGLAASRLGLPG-------PPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLlfaGEIGR 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 19112306   584 LVKAGIGASLLLHEStfeddlkheaiqrqHSTASEALSVAQSMKAKALILTH 635
Cdd:pfam00753 159 LDLPLGGLLVLHPSS--------------AESSLESLLKLAKLKAAVIVPGH 196
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 50-119 5.94e-13

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: 64.15  E-value: 5.94e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306    50 SVVSSLNPDSLIaPLLCVSLDNRKYLIGSMGELTQMKFRSQASNYgGKSVSVFLMPPSlqslnAWGITAG 119
Cdd:pfam13691   1 QVVTTPTADTPG-PLLLLHFDSKRYLFGNVGEGTQRALNEQKVRL-SKLEDIFLTGKV-----SWSNIGG 63
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 427-611 9.89e-13

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: 66.81  E-value: 9.89e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306    427 SSYSVAIDGTVIMLDCGEGAISQFF---RQYGtntepmLRKLKAIFITHLHSDHYLGLLNVLQAWNkantnnsmhINIIG 503
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLaelKKLG------PKKIDAIILTHGHPDHIGGLPELLEAPG---------APVYA 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306    504 PKFLWQWLQRLKSPANLQALLNRIIFIIAKETVTTPLQLTS-DLSISSVPSiHINDSySCIisHTKYGKLVYSGDTrpne 582
Cdd:smart00849  66 PEGTAELLKDLLALLGELGAEAEPAPPDRTLKDGDELDLGGgELEVIHTPG-HTPGS-IVL--YLPEGKILFTGDL---- 137

                          170       180
                   ....*....|....*....|....*....
gi 19112306    583 klVKAGIGASLLLHESTFEDDLKHEAIQR 611
Cdd:smart00849 138 --LFAGGDGRTLVDGGDAAASDALESLLK 164
GntH_guanitoxin NF041257
guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;
435-648 2.98e-09

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;


Pssm-ID: 469157 [Multi-domain]  Cd Length: 372  Bit Score: 59.25  E-value: 2.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306  435 GTVIMLDCGEGAISQFFRQYGTNT-------EPMLRKLKAIFITHLHSDHYLGLLNVLQAWNKANTNNSMHINiiGP--- 504
Cdd:NF041257  31 NTSILVELGNGERDKFFFDIGSGSvaniialQIPYNLLNKVFITHLHVDHYGDLPYLYPFGAWSGRWTPLRVW--GPsgr 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306  505 -------------KFLWQWlqrlkspaNLQALLNRIIFIIAKETVT-----TPLQLTSD---LSISSVPSIHIND---SY 560
Cdd:NF041257 109 tpelgtkhmvegmKEMLAW--------DTDAFSGFPIGDGYEIEVNefdfrDENGVVYEengVTVRSWPRSHAKDgavSY 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306  561 SCIISHTKYgklVYSGDTRPNEKLVKAGIGASLLLHEST-----------FEDDLKHEAIQRQHSTASEALSVAQSMKAK 629
Cdd:NF041257 181 RLDWNGLSF---VFTGDGRPNELTVEYAKGADVFIHECFdtpellsgkygVPPELARYTIDTHHTPPYAAGKVFSLVQPR 257

                        250
                 ....*....|....*....
gi 19112306  630 ALILTHFsqrSYDADFLPP 648
Cdd:NF041257 258 LAMATHF---FNDPDTVAE 273
PRK00055 PRK00055
ribonuclease Z; Reviewed
 198-259 3.00e-07

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 52.49  E-value: 3.00e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112306  198 SFNSKEAAGVFNADKALALGVPFGPSNGKLCAGEAVLSKDGTTwIYPHQVVGPPRK-RQYFYV 259
Cdd:PRK00055 111 RIAEKDKPGKLDAEKLKALGVPPGPLFGKLKRGEDVTLEDGRI-INPADVLGPPRKgRKVAYC 172
 
Name Accession Description Interval E-value
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 413-599 4.94e-65

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: 213.18  E-value: 4.94e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 413 LGTSATCPTWRRSLSSYSVAIDG-TVIMLDCGEGAISQFFRQYGTN-TEPMLRKLKAIFITHLHSDHYLGLLNVLQAWNK 490
Cdd:cd07718   4 LGTGSAIPSKYRNVSGILLRIPGdGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAERKK 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 491 ANTNNSMHINIIGPKFLWQWLQRLKSPANLqaLLNRIIFIIA--------------KETVTTPLQLTSDLSISSVPSIHI 556
Cdd:cd07718  84 LFKPPSPPLYVVAPRQLRRWLREYSSLEDL--GLHDISFISNrvsqslpesddplsRDLLSNLLEELGLKSIETVPVIHC 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 19112306 557 NDSYSCIISHTKYGKLVYSGDTRPNEKLVKAGIGASLLLHEST 599
Cdd:cd07718 162 PDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 413-665 2.52e-56

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: 191.51  E-value: 2.52e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 413 LGTSATCPTWRRSLSSYSVAIDGTVIMLDCGEGAISQFfRQYGTNtepmLRKLKAIFITHLHSDHYLGLLNVLQawnkan 492
Cdd:cd07717   4 LGTGSAVPTPERNLSSIALRLEGELWLFDCGEGTQRQL-LRAGLS----PSKIDRIFITHLHGDHILGLPGLLS------ 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 493 tnnSMH-------INIIGPKFLWQWLQRLkspanLQALLNRIIF-IIAKETVTTP--LQLTSDLSISSVPSIHINDSYSC 562
Cdd:cd07717  73 ---TMSllgrtepLTIYGPKGLKEFLETL-----LRLSASRLPYpIEVHELEPDPglVFEDDGFTVTAFPLDHRVPCFGY 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 563 IISHTKygKLVYSGDTRPNEKLVKAGIGASLLLHESTFEDDLKHEAIQRQHSTASEALSVAQSMKAKALILTHFSQRsYD 642
Cdd:cd07717 145 RFEEGR--KIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKAKETGHSTAKQAAEIAKKAGVKKLVLTHFSAR-YK 221

                       250       260
                ....*....|....*....|....*
gi 19112306 643 --ADFLPPDWTIYPksKTIYANDGL 665
Cdd:cd07717 222 dpEELLKEARAVFP--NTILAEDFM 244
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
412-668 8.56e-54

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 185.01  E-value: 8.56e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 412 VLGTSATCPTWRRSLSSYSVAIDGTVIMLDCGEGAISQFfRQYGTNtepmLRKLKAIFITHLHSDHYLGLLNVLQAWnkA 491
Cdd:COG1234   5 FLGTGGAVPTPGRATSSYLLEAGGERLLIDCGEGTQRQL-LRAGLD----PRDIDAIFITHLHGDHIAGLPGLLSTR--S 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 492 NTNNSMHINIIGPKFLWQWLQRLKSPANLQALLnRIIFIIAKETVTTPLQltsDLSISSVPSIHINDSYSCIISHTKyGK 571
Cdd:COG1234  78 LAGREKPLTIYGPPGTKEFLEALLKASGTDLDF-PLEFHEIEPGEVFEIG---GFTVTAFPLDHPVPAYGYRFEEPG-RS 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 572 LVYSGDTRPNEKLVKAGIGASLLLHESTFEDDLKHEAIQRQHSTASEALSVAQSMKAKALILTHFSQRSYDadflPPDW- 650
Cdd:COG1234 153 LVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDD----PEELl 228

                       250       260
                ....*....|....*....|..
gi 19112306 651 ----TIYPKsKTIYANDGLQWQ 668
Cdd:COG1234 229 aearAVFPG-PVELAEDGMVIE 249
PRK00055 PRK00055
ribonuclease Z; Reviewed
 412-665 7.21e-45

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 161.50  E-value: 7.21e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306  412 VLGTSATCPTWRRSLSSYSVAIDGTVIMLDCGEGAISQFFRqygTNTEPMlrKLKAIFITHLHSDHYLGLLNVLQAWNka 491
Cdd:PRK00055   6 FLGTGSGVPTPTRNVSSILLRLGGELFLFDCGEGTQRQLLK---TGIKPR--KIDKIFITHLHGDHIFGLPGLLSTRS-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306  492 NTNNSMHINIIGPKFLWQWLQRLkspanlqallnRIIF------IIAKETVTT-PLQLTSDLSISSVP---------SIH 555
Cdd:PRK00055  79 LSGRTEPLTIYGPKGIKEFVETL-----------LRASgslgyrIAEKDKPGKlDAEKLKALGVPPGPlfgklkrgeDVT 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306  556 INDSYscIISHTKY------G-KLVYSGDTRPNEKLVKAGIGASLLLHESTFEDDLKHEAIQRQHSTASEALSVAQSMKA 628
Cdd:PRK00055 148 LEDGR--IINPADVlgpprkGrKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDEELAKEYGHSTARQAAEIAKEAGV 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 19112306  629 KALILTHFSQRsYDADflPPDW-----TIYPksKTIYANDGL 665
Cdd:PRK00055 226 KRLILTHFSPR-YTGD--PEELlkearEIFP--NTELAEDLM 262
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 413-646 2.46e-43

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: 158.15  E-value: 2.46e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306   413 LGTSATCPTWRRSLSSYSVAIDGTVIMLDCGEGAISQFFRqygTNTEPMlrKLKAIFITHLHSDHYLGLLNVLQAWNkaN 492
Cdd:TIGR02651   5 LGTGGGVPTKERNLPSIALKLNGELWLFDCGEGTQRQMLR---SGISPM--KIDRIFITHLHGDHILGLPGLLSTMS--F 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306   493 TNNSMHINIIGPKFLWQWLQRLkspanLQALLNRIIFIIAKETVTTPLQL--TSDLSISSVPSIHINDSYS-CIISHTKY 569
Cdd:TIGR02651  78 QGRKEPLTIYGPPGIKEFIETS-----LRVSYTYLNYPIKIHEIEEGGLVfeDDGFKVEAFPLDHSIPSLGyRFEEKDRP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306   570 G------------------------------------------------KLVYSGDTRPNEKLVKAGIGASLLLHESTFE 601
Cdd:TIGR02651 153 GkfdrekakelgippgplygklkrgetvtlidgriidpedvlgpprkgrKIAYTGDTRPCEEVIEFAKNADLLIHEATFL 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 19112306   602 DDLKHEAIQRQHSTASEALSVAQSMKAKALILTHFSQRSYDADFL 646
Cdd:TIGR02651 233 DEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDEEEL 277
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 412-598 5.63e-30

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: 116.59  E-value: 5.63e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 412 VLGTSATCPTWRRSLSSYSVAIDGTVIMLDCGEGAISQFfRQYGTNtepmLRKLKAIFITHLHSDHYLGLLNVLQAWNKA 491
Cdd:cd16272   3 FLGTGGAVPSLTRNTSSYLLETGGTRILLDCGEGTVYRL-LKAGVD----PDKLDAIFLSHFHLDHIGGLPTLLFARRYG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 492 NTNNSMHIniIGPKFLWQWLQRLKSPAN--LQALLNRIIFIIAKETVTTPLqltSDLSISSVPSIHINDSYSCIISHTky 569
Cdd:cd16272  78 GRKKPLTI--YGPKGIKEFLEKLLNFPVeiLPLGFPLEIEELEEGGEVLEL---GDLKVEAFPVKHSVESLGYRIEAE-- 150

                       170       180       190
                ....*....|....*....|....*....|
gi 19112306 570 GK-LVYSGDTRPNEKLVKAGIGASLLLHES 598
Cdd:cd16272 151 GKsIVYSGDTGPCENLVELAKGADLLIHEC 180
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 412-596 3.09e-24

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


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 100.67  E-value: 3.09e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 412 VLGTSatCPTWR--RSLSSYSVAIDGTVIMLDCGEGAISQFFRQyGTNtepmLRKLKAIFITHLHSDHYLGLLNVL-QAW 488
Cdd:cd07719   4 LLGTG--GPIPDpdRAGPSTLVVVGGRVYLVDAGSGVVRRLAQA-GLP----LGDLDAVFLTHLHSDHVADLPALLlTAW 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 489 nkaNTNNSMHINIIGPK----------FLWQWLQRLKSPANLQALLNRIIFIIAKETVTTPLQLTSD-LSISSVPSIH-- 555
Cdd:cd07719  77 ---LAGRKTPLPVYGPPgtralvdgllAAYALDIDYRARIGDEGRPDPGALVEVHEIAAGGVVYEDDgVKVTAFLVDHgp 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 19112306 556 INDSYSCIIsHTKYGKLVYSGDTRPNEKLVKAGIGASLLLH 596
Cdd:cd07719 154 VPPALAYRF-DTPGRSVVFSGDTGPSENLIELAKGADLLVH 193
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 420-644 2.77e-23

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 99.58  E-value: 2.77e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 420 PTWRRSLSSYSVAIDGTVIMLDCGEGaisqfFRQYGTNTEPMLRKLKAIFITHLHSDHYLGLLNVLQAWNKAntnnsmHI 499
Cdd:COG1235  29 PRYGRTRSSILVEADGTRLLIDAGPD-----LREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYGPN------PI 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 500 NIIGPKFLWQWLQRLKS--PANLQALLNRIIFiiakeTVTTPLQLtSDLSISSVPSIH-INDSYSCIISHTKyGKLVYSG 576
Cdd:COG1235  98 PVYATPGTLEALERRFPylFAPYPGKLEFHEI-----EPGEPFEI-GGLTVTPFPVPHdAGDPVGYRIEDGG-KKLAYAT 170

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112306 577 DT-RPNEKLVKAGIGASLLLHESTFEDDlkHEAiqrqHSTASEALSVAQSMKAKALILTHFSQRSYDAD 644
Cdd:COG1235 171 DTgYIPEEVLELLRGADLLILDATYDDP--EPG----HLSNEEALELLARLGPKRLVLTHLSPDNNDHE 233
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 412-606 3.06e-17

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: 80.38  E-value: 3.06e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 412 VLGTSATCPTWRRSLSSYSVAIDGTVIMLDCGeGAISQFFRQYGTNTepmlRKLKAIFITHLHSDHYLGL-LNVLQAWNK 490
Cdd:cd07740   2 FLGSGDAFGSGGRLNTCFHVASEAGRFLIDCG-ASSLIALKRAGIDP----NAIDAIFITHLHGDHFGGLpFFLLDAQFV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 491 ANtnNSMHINIIGPKFLWQWLQRL------KSPANLQALLNRIIFIIAKETVTTPlqltsDLSISSVPSIHINDSYSCII 564
Cdd:cd07740  77 AK--RTRPLTIAGPPGLRERLRRAmealfpGSSKVPRRFDLEVIELEPGEPTTLG-----GVTVTAFPVVHPSGALPLAL 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 19112306 565 SHTKYGK-LVYSGDTRPNEKLVKAGIGASLLLHES-TFEDDLKH 606
Cdd:cd07740 150 RLEAAGRvLAYSGDTEWTDALVPLARGADLFICECyFFEKKVPG 193
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 412-598 5.29e-17

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: 79.02  E-value: 5.29e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 412 VLGTSATCPTWRRSLSSYSVAIDGTVIMLDCGEGAISQFFRQYGtntepmLRKLKAIFITHLHSDHYLGLLnVLQ-AWNK 490
Cdd:cd07716   4 VLGCSGSYPGPGGACSGYLLEADGFRILLDCGSGVLSRLQRYID------PEDLDAVVLSHLHPDHCADLG-VLQyARRY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 491 ANTNNSMH-INIIGPKFLWQWLQRLKSPANlqallnriIFIIAKETVTTPLQLTsDLSISSVPSIHINDSYSCIISHTky 569
Cdd:cd07716  77 HPRGARKPpLPLYGPAGPAERLAALYGLED--------VFDFHPIEPGEPLEIG-PFTITFFRTVHPVPCYAMRIEDG-- 145

                       170       180       190
                ....*....|....*....|....*....|
gi 19112306 570 GK-LVYSGDTRPNEKLVKAGIGASLLLHES 598
Cdd:cd07716 146 GKvLVYTGDTGYCDELVEFARGADLLLCEA 175
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
427-635 4.05e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 74.33  E-value: 4.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306   427 SSYSVAIDGTVIMLDCGEGAISQFFRQYgTNTEPMLRKLKAIFITHLHSDHYLGLLNVLQAWNKANTNNSMHINIIGPKF 506
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLL-AALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306   507 LWQWLQRLKSPAnlqallnRIIFIIAKETVTTPLQLTSDLSISSVPSIHINDSYSCIISHTKYGKLVYSGDT---RPNEK 583
Cdd:pfam00753  86 LGLAASRLGLPG-------PPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLlfaGEIGR 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 19112306   584 LVKAGIGASLLLHEStfeddlkheaiqrqHSTASEALSVAQSMKAKALILTH 635
Cdd:pfam00753 159 LDLPLGGLLVLHPSS--------------AESSLESLLKLAKLKAAVIVPGH 196
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 438-636 2.87e-14

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: 71.96  E-value: 2.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306   438 IMLDCGEGAISQFFRQYgTNTEPMLRKLKAIFITHLHSDHYLGLLNVLQAWNKantnnsmhiNIIGPKFLWQWLQRLKSP 517
Cdd:pfam12706   3 ILIDPGPDLRQQALPAL-QPGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPR---------PLYAPLGVLAHLRRNFPY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306   518 ANLQALLNRIIFIIAKE----------TVT-TPLQLTSDLSISSVPSihinDSYSCIISHTKyGKLVYSGDTRPNEKLVK 586
Cdd:pfam12706  73 LFLLEHYGVRVHEIDWGesftvgdgglTVTaTPARHGSPRGLDPNPG----DTLGFRIEGPG-KRVYYAGDTGYFPDEIG 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 19112306   587 AGI-GASLLLHESTFEDDlkHEAIQRQHSTASEALSVAQSMKAKALILTHF 636
Cdd:pfam12706 148 ERLgGADLLLLDGGAWRD--DEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 50-119 5.94e-13

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: 64.15  E-value: 5.94e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306    50 SVVSSLNPDSLIaPLLCVSLDNRKYLIGSMGELTQMKFRSQASNYgGKSVSVFLMPPSlqslnAWGITAG 119
Cdd:pfam13691   1 QVVTTPTADTPG-PLLLLHFDSKRYLFGNVGEGTQRALNEQKVRL-SKLEDIFLTGKV-----SWSNIGG 63
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 427-611 9.89e-13

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: 66.81  E-value: 9.89e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306    427 SSYSVAIDGTVIMLDCGEGAISQFF---RQYGtntepmLRKLKAIFITHLHSDHYLGLLNVLQAWNkantnnsmhINIIG 503
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLaelKKLG------PKKIDAIILTHGHPDHIGGLPELLEAPG---------APVYA 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306    504 PKFLWQWLQRLKSPANLQALLNRIIFIIAKETVTTPLQLTS-DLSISSVPSiHINDSySCIisHTKYGKLVYSGDTrpne 582
Cdd:smart00849  66 PEGTAELLKDLLALLGELGAEAEPAPPDRTLKDGDELDLGGgELEVIHTPG-HTPGS-IVL--YLPEGKILFTGDL---- 137

                          170       180
                   ....*....|....*....|....*....
gi 19112306    583 klVKAGIGASLLLHESTFEDDLKHEAIQR 611
Cdd:smart00849 138 --LFAGGDGRTLVDGGDAAASDALESLLK 164
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 427-613 1.43e-09

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: 58.28  E-value: 1.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 427 SSYSVAIDGTVIMLDCGEGaisqfFRQYGtntEPMLRKLKA----IFITHLHSDHYLGLLNVLQAWNKANtnnsmHINII 502
Cdd:cd07715  24 SCVEVRAGGELLILDAGTG-----IRELG---NELMKEGPPgeahLLLSHTHWDHIQGFPFFAPAYDPGN-----RIHIY 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 503 GPKF----LWQWLQRLKS----PANLQALLNRIIFIIAKEtvTTPLQLTsDLSISSVPSIHINDSYS-CIISHTKygKLV 573
Cdd:cd07715  91 GPHKdggsLEEVLRRQMSppyfPVPLEELLAAIEFHDLEP--GEPFSIG-GVTVTTIPLNHPGGALGyRIEEDGK--SVV 165

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 19112306 574 YSGDT-------RPNEKLVKAGIGASLLLHESTFEDDlkhEAIQRQH 613
Cdd:cd07715 166 YATDTehypddgESDEALLEFARGADLLIHDAQYTDE---EYPSKRG 209
GntH_guanitoxin NF041257
guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;
435-648 2.98e-09

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;


Pssm-ID: 469157 [Multi-domain]  Cd Length: 372  Bit Score: 59.25  E-value: 2.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306  435 GTVIMLDCGEGAISQFFRQYGTNT-------EPMLRKLKAIFITHLHSDHYLGLLNVLQAWNKANTNNSMHINiiGP--- 504
Cdd:NF041257  31 NTSILVELGNGERDKFFFDIGSGSvaniialQIPYNLLNKVFITHLHVDHYGDLPYLYPFGAWSGRWTPLRVW--GPsgr 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306  505 -------------KFLWQWlqrlkspaNLQALLNRIIFIIAKETVT-----TPLQLTSD---LSISSVPSIHIND---SY 560
Cdd:NF041257 109 tpelgtkhmvegmKEMLAW--------DTDAFSGFPIGDGYEIEVNefdfrDENGVVYEengVTVRSWPRSHAKDgavSY 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306  561 SCIISHTKYgklVYSGDTRPNEKLVKAGIGASLLLHEST-----------FEDDLKHEAIQRQHSTASEALSVAQSMKAK 629
Cdd:NF041257 181 RLDWNGLSF---VFTGDGRPNELTVEYAKGADVFIHECFdtpellsgkygVPPELARYTIDTHHTPPYAAGKVFSLVQPR 257

                        250
                 ....*....|....*....
gi 19112306  630 ALILTHFsqrSYDADFLPP 648
Cdd:NF041257 258 LAMATHF---FNDPDTVAE 273
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 434-635 2.98e-09

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: 57.58  E-value: 2.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 434 DGTVIMLDCGEGAISQFFRqYGTNtePmlRKLKAIFITHLHSDHYlGLLNVL------QAWNKANTnnsmhinIIGPK-- 505
Cdd:cd07741  28 NGKNIHIDPGPGALVRMCR-PKLD--P--TKLDAIILSHRHLDHS-NDANVLieamteGGFKKRGT-------LLAPEda 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 506 ------FLWQWLQRLkspanlqalLNRIIFIIAKETVTTPlqltsDLSISSVPSIH-INDSYSCIIsHTKYGKLVYSGDT 578
Cdd:cd07741  95 lngepvVLLYYHRRK---------LEEIEILEEGDEYELG-----GIKIEATRHKHsDPTTYGFIF-RTSDKKIGYISDT 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19112306 579 RPNEKLVKAGIGASLLLHESTFEDDLKHeaiqRQHSTASEALSVAQSMKAKALILTH 635
Cdd:cd07741 160 RYFEELIEYYSNCDVLIINVTRPRPRKG----VDHLSVEDVEKILKEIKPKLAILTH 212
PRK00055 PRK00055
ribonuclease Z; Reviewed
 198-259 3.00e-07

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 52.49  E-value: 3.00e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112306  198 SFNSKEAAGVFNADKALALGVPFGPSNGKLCAGEAVLSKDGTTwIYPHQVVGPPRK-RQYFYV 259
Cdd:PRK00055 111 RIAEKDKPGKLDAEKLKALGVPPGPLFGKLKRGEDVTLEDGRI-INPADVLGPPRKgRKVAYC 172
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 427-636 1.60e-06

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 49.53  E-value: 1.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 427 SSYSVAIDGTVIMLDcgegaisQFFRQYGTNTEPM------LRKLKAIFITHLHSDHYlgLLNVLQAWNKANtnnsmhIN 500
Cdd:COG2220  12 ATFLIETGGKRILID-------PVFSGRASPVNPLpldpedLPKIDAVLVTHDHYDHL--DDATLRALKRTG------AT 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 501 IIGPKFLWQWLQRLKspanlqalLNRIIFIIAKETVTTPlqltsDLSISSVPSIHIND----------SYscIISHTkyG 570
Cdd:COG2220  77 VVAPLGVAAWLRAWG--------FPRVTELDWGESVELG-----GLTVTAVPARHSSGrpdrngglwvGF--VIETD--G 139

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112306 571 KLVY-SGDTrpneklvkaGIGASLLLHESTFEDDLkheAI-----QRQHSTASEALSVAQSMKAKALILTHF 636
Cdd:COG2220 140 KTIYhAGDT---------GYFPEMKEIGERFPIDV---ALlpigaYPFTMGPEEAAEAARDLKPKVVIPIHY 199
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 429-577 1.30e-05

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. 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: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 47.02  E-value: 1.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 429 YSVAIDGTVIMLDCGegaiSQFFR--QYGTNT--------EPMLRKLKAIFITHLHSDHYLGLLNVLQAWNkantnnsmh 498
Cdd:cd07714  14 YVVEYDDDIIIIDCG----LKFPDedMPGVDYiipdfsylEENKDKIKGIFITHGHEDHIGALPYLLPELN--------- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 499 INIIGPKFLWQWLQRLKSPANLQaLLNRIIFIIAKETVTtplqlTSDLSISSVPSIH-INDSYSCIIsHTKYGKLVYSGD 577
Cdd:cd07714  81 VPIYATPLTLALIKKKLEEFKLI-KKVKLNEIKPGERIK-----LGDFEVEFFRVTHsIPDSVGLAI-KTPEGTIVHTGD 153
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 434-488 2.32e-05

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 46.39  E-value: 2.32e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112306 434 DGTVIMLDCG--------EGAISQFFRQYGtntepmLRKLKAIFITHLHSDHYLGLLNVLQAW 488
Cdd:COG2333  20 DGKTILIDTGprpsfdagERVVLPYLRALG------IRRLDLLVLTHPDADHIGGLAAVLEAF 76
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 463-491 2.89e-05

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: 45.57  E-value: 2.89e-05
                        10        20
                ....*....|....*....|....*....
gi 19112306 463 RKLKAIFITHLHSDHYLGLLNVLQAWNKA 491
Cdd:cd07739  51 KTLTTIYITHGHPDHYFGLEVLLEAFPDA 79
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 434-489 3.03e-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: 45.35  E-value: 3.03e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19112306 434 DGTVIMLDCGEGAISQFFRQygtnTEPMLRKLKAIFITHLHSDHYLGLLNVLQAWN 489
Cdd:cd06262  19 EGEAILIDPGAGALEKILEA----IEELGLKIKAILLTHGHFDHIGGLAELKEAPG 70
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 420-505 3.36e-05

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 44.92  E-value: 3.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 420 PTWRRSLSSYSVAIDGTVIMLDCGEGAISQFFRQygtntepmlRKLKAIFITHLHSDHYLGLLNVlqAWNKantnnSMHI 499
Cdd:cd07736  31 PSYRRRPCSALIEVDGERILLDAGLTDLAERFPP---------GSIDAILLTHFHMDHVQGLFHL--RWGV-----GDPI 94


                ....*.
gi 19112306 500 NIIGPK 505
Cdd:cd07736  95 PVYGPP 100
PRK02126 PRK02126
ribonuclease Z; Provisional
 497-639 7.06e-05

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 45.29  E-value: 7.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306  497 MHINI-----------IGPkflwqWLQRLKspanlQALLNRIIfiiAKETVTTPLQLTSDLSISSVPsihINDSYSCIIS 565
Cdd:PRK02126 175 AHINIdknrlaelglpPGP-----WLRELK-----HAVLRGEP---DDTPIRVLWRDGGGEHERVRP---LGELKERVLR 238

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112306  566 HTKYGKLVYSGDTRPNE----KLVKAGIGASLLLHESTFEDDLKHEAIQRQHSTASEALSVAQSMKAKALILTHFSQR 639
Cdd:PRK02126 239 IEPGQKIGYVTDIGYTEenlaRIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPR 316
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 427-587 2.30e-04

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: 42.83  E-value: 2.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 427 SSYSVAIDGTVIMLDCGegaISQFFRQ-YGTNTEPML---RKLKAIFITHLHSDH-----YL----------------GL 481
Cdd:cd16295  13 SCYLLETGGKRILLDCG---LFQGGKElEELNNEPFPfdpKEIDAVILTHAHLDHsgrlpLLvkegfrgpiyatpatkDL 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 482 LNVLQawnkantNNSMHINiiGPKFLWQWLQRLKSPANLQALLNRIIFIiakeTVTTPLQLTSDLSISSVPSIHINDSYS 561
Cdd:cd16295  90 AELLL-------LDSAKIQ--EEEAEHPPAEPLYTEEDVEKALKHFRPV----EYGEPFEIGPGVKVTFYDAGHILGSAS 156

                       170       180
                ....*....|....*....|....*..
gi 19112306 562 CIISHTKYGKLVYSGD-TRPNEKLVKA 587
Cdd:cd16295 157 VELEIGGGKRILFSGDlGRKNTPLLRD 183
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 426-577 4.48e-04

Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 41.93  E-value: 4.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 426 LSSYSVAIDGTVIMLDCGEGAISQFFRQYGTNTEPMLRKLKAIFITHLHSDHYLGLLNVLQ------------------A 487
Cdd:cd07734  11 RSCFLVEFKGRTVLLDCGMNPGKEDPEACLPQFELLPPEIDAILISHFHLDHCGALPYLFRgfifrgpiyathptvalgR 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 488 WNKANTNNSMhiNIIGPKflwqwlQRLKSPANLQALLNRIIFIIAKETVttplQLTSDLSISSVPSIHINDSySCIISHT 567
Cdd:cd07734  91 LLLEDYVKSA--ERIGQD------QSLYTPEDIEEALKHIVPLGYGQSI----DLFPALSLTAYNAGHVLGA-AMWEIQI 157

                       170
                ....*....|
gi 19112306 568 KYGKLVYSGD 577
Cdd:cd07734 158 YGEKLVYTGD 167
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 427-485 5.42e-04

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 42.87  E-value: 5.42e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112306 427 SSYSVAIDGTVIMLDCGegaisQFFRQYGTNTEPM---LRKLKAIFITHLHSDHyLGLLNVL 485
Cdd:COG1236  15 SCYLLETGGTRILIDCG-----LFQGGKERNWPPFpfrPSDVDAVVLTHAHLDH-SGALPLL 70
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 418-489 6.54e-04

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 41.60  E-value: 6.54e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112306 418 TCPTWRRSLSSYSVAIDGT--VIMLDCG-----EGAISQFFRQYGtntepmlRKLKAIFITHLHSDHYLGLLNVLQAWN 489
Cdd:COG0491   5 PGGTPGAGLGVNSYLIVGGdgAVLIDTGlgpadAEALLAALAALG-------LDIKAVLLTHLHPDHVGGLAALAEAFG 76
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 414-513 6.68e-04

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: 41.31  E-value: 6.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112306 414 GTSA-------TCPT-------WRRSLSSYSVAIDGTVIMLDCGegaisQFFRQygtntePMLR----KLKAIFITHLHS 475
Cdd:cd16279   9 GTSSgvpvigcDCGVcdssdpkNRRLRSSILIETGGKNILIDTG-----PDFRQ------QALRagirKLDAVLLTHAHA 77

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 19112306 476 DHYLGLLNvLQAWNKantNNSMHINIIGPKFLWQWLQR 513
Cdd:cd16279  78 DHIHGLDD-LRPFNR---LQQRPIPVYASEETLDDLKR 111
PRK14866 PRK14866
hypothetical protein; Provisional
 207-254 3.85e-03

hypothetical protein; Provisional


Pssm-ID: 237840  Cd Length: 451  Bit Score: 40.37  E-value: 3.85e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 19112306  207 VFNADKALALGVPFGPSNGKLCAGEAVlSKDGTTwIYPHQVVGPPRKR 254
Cdd:PRK14866 397 RFDPELARKLGVPEGPAFGKLAAGQPV-EVDGET-ITPEMVHRETTKR 442
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 424-487 6.98e-03

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: 38.05  E-value: 6.98e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112306 424 RSLSSYSVAIDGTVIMLDCG---EGAISQFFRQygtntepmLRKLKA-------IFITHLHSDHYlGLLNVLQA 487
Cdd:cd07725  13 GHVNVYLLRDGDETTLIDTGlatEEDAEALWEG--------LKELGLkpsdidrVLLTHHHPDHI-GLAGKLQE 77
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 438-487 8.76e-03

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


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 37.90  E-value: 8.76e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19112306 438 IMLDCGEGAISqffrqYGTNTEPMLRK-----LKAIFITHLHSDHYLGLLNVLQA 487
Cdd:cd07722  30 ILIDTGEGRPS-----YIPLLKSVLDSegnatISDILLTHWHHDHVGGLPDVLDL 79
 
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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