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Conserved domains on  [gi|748726810|ref|WP_039984928|]
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MBL fold metallo-hydrolase [Fusobacterium periodonticum]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11454817)

MBL fold metallo-hydrolase similar to as Sus scrofa cytidine monophosphate-N-acetylneuraminic acid hydroxylase and Bacillus subtilis UPF0173 protein YddR; may be inactive as a hydrolase such as human inactive cytidine monophosphate-N-acetylneuraminic CMAHP

CATH:  3.60.15.30
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  11471246|17597585
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 109-353 5.77e-72

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


:

Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 224.03  E-value: 5.77e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 109 IIWFGHSSLFIQIAGKKILIDPVFSKYASPVPfsnkafegTNIYTVDDLPEIDVLLITHDHYDHLDYPTVKKLKDKVARV 188
Cdd:COG2220    6 ITWLGHATFLIETGGKRILIDPVFSGRASPVN--------PLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALKRTGATV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 189 IVPLGVDAHLLRWGFDeeKITTVDWDDEVTIDeNLKIYALETRHFSGRefSNRNQSLWVSYLIEekynDGLYRLFLSGDG 268
Cdd:COG2220   78 VAPLGVAAWLRAWGFP--RVTELDWGESVELG-GLTVTAVPARHSSGR--PDRNGGLWVGFVIE----TDGKTIYHAGDT 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 269 GYSPRFKSFKEKFKnIDLAVMEAGQYNeewslIHSLPEDIIKEVQDMEVTKLFPIHNSKFKLSKHtwdEPLKKLDSFTRN 348
Cdd:COG2220  149 GYFPEMKEIGERFP-IDVALLPIGAYP-----FTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDE---DPLERFAAALAA 219


                 ....*
gi 748726810 349 TNIEL 353
Cdd:COG2220  220 AGVRV 224
 
Name Accession Description Interval E-value
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 109-353 5.77e-72

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 224.03  E-value: 5.77e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 109 IIWFGHSSLFIQIAGKKILIDPVFSKYASPVPfsnkafegTNIYTVDDLPEIDVLLITHDHYDHLDYPTVKKLKDKVARV 188
Cdd:COG2220    6 ITWLGHATFLIETGGKRILIDPVFSGRASPVN--------PLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALKRTGATV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 189 IVPLGVDAHLLRWGFDeeKITTVDWDDEVTIDeNLKIYALETRHFSGRefSNRNQSLWVSYLIEekynDGLYRLFLSGDG 268
Cdd:COG2220   78 VAPLGVAAWLRAWGFP--RVTELDWGESVELG-GLTVTAVPARHSSGR--PDRNGGLWVGFVIE----TDGKTIYHAGDT 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 269 GYSPRFKSFKEKFKnIDLAVMEAGQYNeewslIHSLPEDIIKEVQDMEVTKLFPIHNSKFKLSKHtwdEPLKKLDSFTRN 348
Cdd:COG2220  149 GYFPEMKEIGERFP-IDVALLPIGAYP-----FTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDE---DPLERFAAALAA 219


                 ....*
gi 748726810 349 TNIEL 353
Cdd:COG2220  220 AGVRV 224
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 111-298 7.86e-57

Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. 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: 293841  Cd Length: 181  Bit Score: 183.63  E-value: 7.86e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 111 WFGHSSLFIQIAGKKILIDPVFSKYASPVPFSNKAFEGTNIYTVDDLPEIDVLLITHDHYDHLDYPTVKKLKDKVArVIV 190
Cdd:cd16283    1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPP-YLV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 191 PLGVDAHLLRWGFdeEKITTVDWDDEVTIDeNLKIYALETRHFSGREFSNRNQSLWVSYLIEEKYndglYRLFLSGDGGY 270
Cdd:cd16283   80 PLGLKKWFLKKGI--TNVVELDWWQSTEIG-GVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEG----FRIYFAGDTGY 152

                        170       180
                 ....*....|....*....|....*...
gi 748726810 271 SPRFKSFKEKFKNIDLAVMEAGQYNEEW 298
Cdd:cd16283  153 FPGFREIGRRFGPIDLALLPIGAYEPRW 180
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 126-324 4.45e-32

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: 119.72  E-value: 4.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810  126 ILIDPVFSKYAspvPFSNKAFEGTNIYTvddlpEIDVLLITHDHYDHL-DYPTVKKLKDKvaRVIVPLGVDAHLLRWG-- 202
Cdd:pfam12706   3 ILIDPGPDLRQ---QALPALQPGRLRDD-----PIDAVLLTHDHYDHLaGLLDLREGRPR--PLYAPLGVLAHLRRNFpy 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810  203 -FDEEK----ITTVDWDDEVTI-DENLKIYALETRHFSGREFsNRNQSLWVSYLIEekynDGLYRLFLSGDGGYSPrfKS 276
Cdd:pfam12706  73 lFLLEHygvrVHEIDWGESFTVgDGGLTVTATPARHGSPRGL-DPNPGDTLGFRIE----GPGKRVYYAGDTGYFP--DE 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 748726810  277 FKEKFKNIDLAVMEAGQYNEEWSL--IHSLPEDIIKEVQDMEVTKLFPIH 324
Cdd:pfam12706 146 IGERLGGADLLLLDGGAWRDDEMIhmGHMTPEEAVEAAADLGARRKVLIH 195
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 109-189 1.10e-09

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 57.90  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 109 IIWFGHSSLFIQIAGKKILIDPVFSkyaspvpfSNKAFEGtniyTVDDLpEIDVLLITHDHYDHL-DypTVKKLKDKVAR 187
Cdd:PRK00685   3 ITWLGHSAFLIETGGKKILIDPFIT--------GNPLADL----KPEDV-KVDYILLTHGHGDHLgD--TVEIAKRTGAT 67


                 ..
gi 748726810 188 VI 189
Cdd:PRK00685  68 VI 69
 
Name Accession Description Interval E-value
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 109-353 5.77e-72

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 224.03  E-value: 5.77e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 109 IIWFGHSSLFIQIAGKKILIDPVFSKYASPVPfsnkafegTNIYTVDDLPEIDVLLITHDHYDHLDYPTVKKLKDKVARV 188
Cdd:COG2220    6 ITWLGHATFLIETGGKRILIDPVFSGRASPVN--------PLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALKRTGATV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 189 IVPLGVDAHLLRWGFDeeKITTVDWDDEVTIDeNLKIYALETRHFSGRefSNRNQSLWVSYLIEekynDGLYRLFLSGDG 268
Cdd:COG2220   78 VAPLGVAAWLRAWGFP--RVTELDWGESVELG-GLTVTAVPARHSSGR--PDRNGGLWVGFVIE----TDGKTIYHAGDT 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 269 GYSPRFKSFKEKFKnIDLAVMEAGQYNeewslIHSLPEDIIKEVQDMEVTKLFPIHNSKFKLSKHtwdEPLKKLDSFTRN 348
Cdd:COG2220  149 GYFPEMKEIGERFP-IDVALLPIGAYP-----FTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDE---DPLERFAAALAA 219


                 ....*
gi 748726810 349 TNIEL 353
Cdd:COG2220  220 AGVRV 224
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 111-298 7.86e-57

Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. 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: 293841  Cd Length: 181  Bit Score: 183.63  E-value: 7.86e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 111 WFGHSSLFIQIAGKKILIDPVFSKYASPVPFSNKAFEGTNIYTVDDLPEIDVLLITHDHYDHLDYPTVKKLKDKVArVIV 190
Cdd:cd16283    1 WIGHATFLIQIEGLNILTDPVFSERASPVSFGGPKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPP-YLV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 191 PLGVDAHLLRWGFdeEKITTVDWDDEVTIDeNLKIYALETRHFSGREFSNRNQSLWVSYLIEEKYndglYRLFLSGDGGY 270
Cdd:cd16283   80 PLGLKKWFLKKGI--TNVVELDWWQSTEIG-GVRITFVPAQHWSRRTLFDTNESLWGGWVIEGEG----FRIYFAGDTGY 152

                        170       180
                 ....*....|....*....|....*...
gi 748726810 271 SPRFKSFKEKFKNIDLAVMEAGQYNEEW 298
Cdd:cd16283  153 FPGFREIGRRFGPIDLALLPIGAYEPRW 180
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 126-324 4.45e-32

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: 119.72  E-value: 4.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810  126 ILIDPVFSKYAspvPFSNKAFEGTNIYTvddlpEIDVLLITHDHYDHL-DYPTVKKLKDKvaRVIVPLGVDAHLLRWG-- 202
Cdd:pfam12706   3 ILIDPGPDLRQ---QALPALQPGRLRDD-----PIDAVLLTHDHYDHLaGLLDLREGRPR--PLYAPLGVLAHLRRNFpy 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810  203 -FDEEK----ITTVDWDDEVTI-DENLKIYALETRHFSGREFsNRNQSLWVSYLIEekynDGLYRLFLSGDGGYSPrfKS 276
Cdd:pfam12706  73 lFLLEHygvrVHEIDWGESFTVgDGGLTVTATPARHGSPRGL-DPNPGDTLGFRIE----GPGKRVYYAGDTGYFP--DE 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 748726810  277 FKEKFKNIDLAVMEAGQYNEEWSL--IHSLPEDIIKEVQDMEVTKLFPIH 324
Cdd:pfam12706 146 IGERLGGADLLLLDGGAWRDDEMIhmGHMTPEEAVEAAADLGARRKVLIH 195
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 109-179 1.05e-09

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


Pssm-ID: 433247 [Multi-domain]  Cd Length: 160  Bit Score: 56.83  E-value: 1.05e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 748726810  109 IIWFGHSSLFIQIAGKKILIDPVFSKYASPVPfsnkafegtniytvddLPEIDVLLITHDHYDHLDYPTVK 179
Cdd:pfam13483   2 ITWLGHSSFLIEGGGARILTDPFRATVGYRPP----------------PVTADLVLISHGHDDHGHPETLP 56
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 109-189 1.10e-09

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 57.90  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 109 IIWFGHSSLFIQIAGKKILIDPVFSkyaspvpfSNKAFEGtniyTVDDLpEIDVLLITHDHYDHL-DypTVKKLKDKVAR 187
Cdd:PRK00685   3 ITWLGHSAFLIETGGKKILIDPFIT--------GNPLADL----KPEDV-KVDYILLTHGHGDHLgD--TVEIAKRTGAT 67


                 ..
gi 748726810 188 VI 189
Cdd:PRK00685  68 VI 69
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
113-324 4.63e-09

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 56.36  E-value: 4.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 113 GHSSLFIQIAGKKILIDP---VFSkyaspvpfsnkAFEGTNIytvdDLPEIDVLLITHDHYDH-LDYPTVKKL-----KD 183
Cdd:COG1234   18 ATSSYLLEAGGERLLIDCgegTQR-----------QLLRAGL----DPRDIDAIFITHLHGDHiAGLPGLLSTrslagRE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 184 KVARVIVPLGVDA---HLLRWGFDEE--KITTVDWDDEVTI-DENLKIYALETRHfsgREFSnrnqslwVSYLIEEKynd 257
Cdd:COG1234   83 KPLTIYGPPGTKEfleALLKASGTDLdfPLEFHEIEPGEVFeIGGFTVTAFPLDH---PVPA-------YGYRFEEP--- 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 748726810 258 GLyRLFLSGDGGYSPRFKSFkekFKNIDLAVMEAGQYNEEWSL----IHSLPEDIIKEVQDMEVTKLFPIH 324
Cdd:COG1234  150 GR-SLVYSGDTRPCEALVEL---AKGADLLIHEATFLDEEAELaketGHSTAKEAAELAAEAGVKRLVLTH 216
PRK11709 PRK11709
putative L-ascorbate 6-phosphate lactonase; Provisional
 159-229 9.38e-05

putative L-ascorbate 6-phosphate lactonase; Provisional


Pssm-ID: 236958  Cd Length: 355  Bit Score: 43.83  E-value: 9.38e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 748726810 159 EIDVLLITHDHYDHLDYPT----VKKLKDKVaRVIVPLGVDAHLLRWGFDEEKITTVDWDDEVTIdENLKIYALE 229
Cdd:PRK11709 109 EIDAVLATHDHSDHIDVNVaaavLQNCADHV-KFIGPQACVDLWIGWGVPKERCIVVKPGDVVKV-KDIKIHALD 181
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
109-172 1.38e-04

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 42.36  E-value: 1.38e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 748726810  109 IIWFGHSSLFIQIAGKKILIDPVFSkyaspvpfSNKAFEGTNIYTVDDLPEIDVLLITHDHYDH 172
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGS--------AEAALLLLLAALGLGPKDIDAVILTHGHFDH 56
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 113-172 2.86e-04

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: 41.42  E-value: 2.86e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 748726810 113 GHSSLFIQIAGKKILID----PVFSKYASpVPFsnkafegtniYTVDDLPEIDVLLITHDHYDH 172
Cdd:cd16292   13 GRSCVILEFKGKTIMLDcgihPGYSGLAS-LPF----------FDEIDLSEIDLLLITHFHLDH 65
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 115-291 3.35e-04

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: 40.89  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 115 SSLFIQIAGKKILIDP---VFSkyaspvpfsnkafegtNIYTVDDLPEIDVLLITHDHYDH----------LDYPTVKKL 181
Cdd:cd07716   19 SGYLLEADGFRILLDCgsgVLS----------------RLQRYIDPEDLDAVVLSHLHPDHcadlgvlqyaRRYHPRGAR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 182 KDKVaRVIVPLGVDAHLLRWGFDEE--KITTVDWDDEVTIDeNLKIYALETRH----FSGReFSNRNQSLwvSYlieeky 255
Cdd:cd07716   83 KPPL-PLYGPAGPAERLAALYGLEDvfDFHPIEPGEPLEIG-PFTITFFRTVHpvpcYAMR-IEDGGKVL--VY------ 151

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 748726810 256 ndglyrlflSGDGGYSPRFKSFkekFKNIDLAVMEA 291
Cdd:cd07716  152 ---------TGDTGYCDELVEF---ARGADLLLCEA 175
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 113-173 1.00e-03

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


Pssm-ID: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 40.01  E-value: 1.00e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 748726810 113 GHSSLFIQIAGKKILID----PVFSKYASPVPfsnkafegtniYTVDDLPEIDVLLITHDHYDHL 173
Cdd:cd07734   10 GRSCFLVEFKGRTVLLDcgmnPGKEDPEACLP-----------QFELLPPEIDAILISHFHLDHC 63
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 115-172 4.25e-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: 37.82  E-value: 4.25e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 748726810 115 SSLFIQIAGKKILID--------PVFSKYASPVPFsnkafegtniytvdDLPEIDVLLITHDHYDH 172
Cdd:cd16295   13 SCYLLETGGKRILLDcglfqggkELEELNNEPFPF--------------DPKEIDAVILTHAHLDH 64
PRK02113 PRK02113
MBL fold metallo-hydrolase;
115-173 7.82e-03

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 37.45  E-value: 7.82e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 748726810 115 SSLFIQIAGKKILID--PVFSKYASPVPFSnkafegtniytvddlpEIDVLLITHDHYDHL 173
Cdd:PRK02113  36 TSALVETEGARILIDcgPDFREQMLRLPFG----------------KIDAVLITHEHYDHV 80
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 113-291 8.28e-03

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: 36.86  E-value: 8.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 113 GHSSLFIQIAGKKILIDpvfskyaspvpfsnkAFEGTnIYTVD----DLPEIDVLLITHDHYDH-LDYPTV-----KKLK 182
Cdd:cd16272   16 NTSSYLLETGGTRILLD---------------CGEGT-VYRLLkagvDPDKLDAIFLSHFHLDHiGGLPTLlfarrYGGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748726810 183 DKVARVIVPLGVDAHLLR---------WGFDEEKITTVDWDDEVTIDENLKIYALETRHfsgrefsnRNQSLWVSYLIEE 253
Cdd:cd16272   80 KKPLTIYGPKGIKEFLEKllnfpveilPLGFPLEIEELEEGGEVLELGDLKVEAFPVKH--------SVESLGYRIEAEG 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 748726810 254 KyndglyRLFLSGDGGYSPrfkSFKEKFKNIDLAVMEA 291
Cdd:cd16272  152 K------SIVYSGDTGPCE---NLVELAKGADLLIHEC 180
 
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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