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Conserved domains on  [gi|927313394|ref|WP_053807788|]
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MULTISPECIES: MBL fold metallo-hydrolase [Vibrio]

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 ...
 1-226 1.76e-39

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


:

Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 136.59  E-value: 1.76e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394   1 MKITQIRNATQVIDYAGKTFLIDPMLAPKGTYPgfegtanshlrNPtveLPLPLESIINVDAVLLTHTHPDHWDETAVNA 80
Cdd:COG2220    4 MKITWLGHATFLIETGGKRILIDPVFSGRASPV-----------NP---LPLDPEDLPKIDAVLVTHDHYDHLDDATLRA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394  81 IPKDKLIFVQHEGDETILLSQGFTNVKIFS--EETEYHGISFTRTVCQHGSDAAFQHdqmaeiLGEVTGVIFSHaDEEKL 158
Cdd:COG2220   70 LKRTGATVVAPLGVAAWLRAWGFPRVTELDwgESVELGGLTVTAVPARHSSGRPDRN------GGLWVGFVIET-DGKTI 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927313394 159 YVVGDTIWIPGVEETMKKEQPGVVILNTGWAHvlgfgpIIMGKEDVLKTHQVLPKAKIVATHMGAVNH 226
Cdd:COG2220  143 YHAGDTGYFPEMKEIGERFPIDVALLPIGAYP------FTMGPEEAAEAARDLKPKVVIPIHYGTFPL 204
 
Name Accession Description Interval E-value
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 1-226 1.76e-39

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 136.59  E-value: 1.76e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394   1 MKITQIRNATQVIDYAGKTFLIDPMLAPKGTYPgfegtanshlrNPtveLPLPLESIINVDAVLLTHTHPDHWDETAVNA 80
Cdd:COG2220    4 MKITWLGHATFLIETGGKRILIDPVFSGRASPV-----------NP---LPLDPEDLPKIDAVLVTHDHYDHLDDATLRA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394  81 IPKDKLIFVQHEGDETILLSQGFTNVKIFS--EETEYHGISFTRTVCQHGSDAAFQHdqmaeiLGEVTGVIFSHaDEEKL 158
Cdd:COG2220   70 LKRTGATVVAPLGVAAWLRAWGFPRVTELDwgESVELGGLTVTAVPARHSSGRPDRN------GGLWVGFVIET-DGKTI 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927313394 159 YVVGDTIWIPGVEETMKKEQPGVVILNTGWAHvlgfgpIIMGKEDVLKTHQVLPKAKIVATHMGAVNH 226
Cdd:COG2220  143 YHAGDTGYFPEMKEIGERFPIDVALLPIGAYP------FTMGPEEAAEAARDLKPKVVIPIHYGTFPL 204
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 6-172 2.28e-12

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: 63.84  E-value: 2.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394   6 IRNATQVIDYAGKTFLIDPMLAPKGTYPGFEGtanshlRNPTVELPLPLESIINVDAVLLTHTHPDHWDETAVNAIPKDK 85
Cdd:cd16283    2 IGHATFLIQIEGLNILTDPVFSERASPVSFGG------PKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394  86 LIFVQHeGDETILLSQGFTNVKIFS--EETEYHGISFTRTVCQHGS-----DaafqhdqMAEILGevTGVIFSHADeEKL 158
Cdd:cd16283   76 PYLVPL-GLKKWFLKKGITNVVELDwwQSTEIGGVRITFVPAQHWSrrtlfD-------TNESLW--GGWVIEGEG-FRI 144

                        170
                 ....*....|....
gi 927313394 159 YVVGDTIWIPGVEE 172
Cdd:cd16283  145 YFAGDTGYFPGFRE 158
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 1-164 1.63e-05

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 44.80  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394   1 MKITQIRNATQVIDYAGKTFLIDPMLApkgtypgfegtanshlRNPTVelPLPLESIiNVDAVLLTHTHPDHWDETAVNA 80
Cdd:PRK00685   1 MKITWLGHSAFLIETGGKKILIDPFIT----------------GNPLA--DLKPEDV-KVDYILLTHGHGDHLGDTVEIA 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394  81 IPKDKLIFVQHEgDETILLSQGFTNV-------KIfseetEYHGISFTRTVCQHGSdaAFQHDQMAEILGEVTGVIFsHA 153
Cdd:PRK00685  62 KRTGATVIANAE-LANYLSEKGVEKThpmniggTV-----EFDGGKVKLTPALHSS--SFIDEDGITYLGNPTGFVI-TF 132

                        170
                 ....*....|.
gi 927313394 154 DEEKLYVVGDT 164
Cdd:PRK00685 133 EGKTIYHAGDT 143
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
12-192 8.73e-04

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 39.27  E-value: 8.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394   12 VIDYAGKTFLIDPmlapkgtypGFEGTANSHLRNPTVELPlplesIINVDAVLLTHTHPDH------WDETAVNAIPKDK 85
Cdd:pfam00753  10 LIEGGGGAVLIDT---------GGSAEAALLLLLAALGLG-----PKDIDAVILTHGHFDHigglgeLAEATDVPVIVVA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394   86 LIFVQHEGDETILLSQGFTNVKIFSEETEyHGISFTRTVCQHGSDAAFQHdqmAEILGEVTGVIFSHADEEKLYVVGDTI 165
Cdd:pfam00753  76 EEARELLDEELGLAASRLGLPGPPVVPLP-PDVVLEEGDGILGGGLGLLV---THGPGHGPGHVVVYYGGGKVLFTGDLL 151

                         170       180
                  ....*....|....*....|....*..
gi 927313394  166 WIPGVEETMKKEQPGVVILNTGWAHVL 192
Cdd:pfam00753 152 FAGEIGRLDLPLGGLLVLHPSSAESSL 178
 
Name Accession Description Interval E-value
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 1-226 1.76e-39

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 136.59  E-value: 1.76e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394   1 MKITQIRNATQVIDYAGKTFLIDPMLAPKGTYPgfegtanshlrNPtveLPLPLESIINVDAVLLTHTHPDHWDETAVNA 80
Cdd:COG2220    4 MKITWLGHATFLIETGGKRILIDPVFSGRASPV-----------NP---LPLDPEDLPKIDAVLVTHDHYDHLDDATLRA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394  81 IPKDKLIFVQHEGDETILLSQGFTNVKIFS--EETEYHGISFTRTVCQHGSDAAFQHdqmaeiLGEVTGVIFSHaDEEKL 158
Cdd:COG2220   70 LKRTGATVVAPLGVAAWLRAWGFPRVTELDwgESVELGGLTVTAVPARHSSGRPDRN------GGLWVGFVIET-DGKTI 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927313394 159 YVVGDTIWIPGVEETMKKEQPGVVILNTGWAHvlgfgpIIMGKEDVLKTHQVLPKAKIVATHMGAVNH 226
Cdd:COG2220  143 YHAGDTGYFPEMKEIGERFPIDVALLPIGAYP------FTMGPEEAAEAARDLKPKVVIPIHYGTFPL 204
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 6-172 2.28e-12

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: 63.84  E-value: 2.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394   6 IRNATQVIDYAGKTFLIDPMLAPKGTYPGFEGtanshlRNPTVELPLPLESIINVDAVLLTHTHPDHWDETAVNAIPKDK 85
Cdd:cd16283    2 IGHATFLIQIEGLNILTDPVFSERASPVSFGG------PKRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394  86 LIFVQHeGDETILLSQGFTNVKIFS--EETEYHGISFTRTVCQHGS-----DaafqhdqMAEILGevTGVIFSHADeEKL 158
Cdd:cd16283   76 PYLVPL-GLKKWFLKKGITNVVELDwwQSTEIGGVRITFVPAQHWSrrtlfD-------TNESLW--GGWVIEGEG-FRI 144

                        170
                 ....*....|....
gi 927313394 159 YVVGDTIWIPGVEE 172
Cdd:cd16283  145 YFAGDTGYFPGFRE 158
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 3-186 1.33e-06

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: 47.95  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394   3 ITQIRnATQ--VIDYAGKTFLIDPmlapkGtyPGfegtANSHLRNPTVElplplesIINVDAVLLTHTHPDHWdeTAVNA 80
Cdd:cd07741   14 ITQLR-ASGgiWIELNGKNIHIDP-----G--PG----ALVRMCRPKLD-------PTKLDAIILSHRHLDHS--NDANV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394  81 I-----------------PKDKLifvqhEGDETILLS---QGFTNVKIFSEETEYH-GISFTRTVC-QHGsdaafqhdqm 138
Cdd:cd07741   73 LieamteggfkkrgtllaPEDAL-----NGEPVVLLYyhrRKLEEIEILEEGDEYElGGIKIEATRhKHS---------- 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 927313394 139 aeilGEVT-GVIFsHADEEKLYVVGDTIWIPGVEEtmKKEQPGVVILNT 186
Cdd:cd07741  138 ----DPTTyGFIF-RTSDKKIGYISDTRYFEELIE--YYSNCDVLIINV 179
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 1-164 1.63e-05

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 44.80  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394   1 MKITQIRNATQVIDYAGKTFLIDPMLApkgtypgfegtanshlRNPTVelPLPLESIiNVDAVLLTHTHPDHWDETAVNA 80
Cdd:PRK00685   1 MKITWLGHSAFLIETGGKKILIDPFIT----------------GNPLA--DLKPEDV-KVDYILLTHGHGDHLGDTVEIA 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394  81 IPKDKLIFVQHEgDETILLSQGFTNV-------KIfseetEYHGISFTRTVCQHGSdaAFQHDQMAEILGEVTGVIFsHA 153
Cdd:PRK00685  62 KRTGATVIANAE-LANYLSEKGVEKThpmniggTV-----EFDGGKVKLTPALHSS--SFIDEDGITYLGNPTGFVI-TF 132

                        170
                 ....*....|.
gi 927313394 154 DEEKLYVVGDT 164
Cdd:PRK00685 133 EGKTIYHAGDT 143
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
12-192 8.73e-04

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 39.27  E-value: 8.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394   12 VIDYAGKTFLIDPmlapkgtypGFEGTANSHLRNPTVELPlplesIINVDAVLLTHTHPDH------WDETAVNAIPKDK 85
Cdd:pfam00753  10 LIEGGGGAVLIDT---------GGSAEAALLLLLAALGLG-----PKDIDAVILTHGHFDHigglgeLAEATDVPVIVVA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394   86 LIFVQHEGDETILLSQGFTNVKIFSEETEyHGISFTRTVCQHGSDAAFQHdqmAEILGEVTGVIFSHADEEKLYVVGDTI 165
Cdd:pfam00753  76 EEARELLDEELGLAASRLGLPGPPVVPLP-PDVVLEEGDGILGGGLGLLV---THGPGHGPGHVVVYYGGGKVLFTGDLL 151

                         170       180
                  ....*....|....*....|....*..
gi 927313394  166 WIPGVEETMKKEQPGVVILNTGWAHVL 192
Cdd:pfam00753 152 FAGEIGRLDLPLGGLLVLHPSSAESSL 178
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 2-97 1.74e-03

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: 37.95  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394    2 KITQIRNATQVIDYAGKTFLIDPMLAPKGTYPGFEgtanshlrnptvelplplesiiNVDAVLLTHTHPDHWDETAVNAI 81
Cdd:pfam13483   1 EITWLGHSSFLIEGGGARILTDPFRATVGYRPPPV----------------------TADLVLISHGHDDHGHPETLPGN 58

                          90
                  ....*....|....*.
gi 927313394   82 PKdkliFVQHEGDETI 97
Cdd:pfam13483  59 PH----VLDGGGSYTV 70
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 13-72 2.70e-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: 2.70e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394  13 IDYAGKTFLIDpmlapKGTYPGFEGTAnshlRNPTVELPLPLESIinvDAVLLTHTHPDH 72
Cdd:cd16295   17 LETGGKRILLD-----CGLFQGGKELE----ELNNEPFPFDPKEI---DAVILTHAHLDH 64
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 19-221 4.29e-03

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: 37.29  E-value: 4.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394   19 TFLIDPmlapkgtYPGFEGTANshlrnPTVELPLPLESiiNVDAVLLTHTHPDHWD------ETAVNAI--PKDKLIFVQ 90
Cdd:pfam12706   2 RILIDP-------GPDLRQQAL-----PALQPGRLRDD--PIDAVLLTHDHYDHLAglldlrEGRPRPLyaPLGVLAHLR 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394   91 HEGDETILLSQGFTNVKIFSEETEY----HGISFTRTVCQHGSDAAFQHDQmaeilGEVTGVIFShADEEKLYVVGDTIW 166
Cdd:pfam12706  68 RNFPYLFLLEHYGVRVHEIDWGESFtvgdGGLTVTATPARHGSPRGLDPNP-----GDTLGFRIE-GPGKRVYYAGDTGY 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 927313394  167 IPG-VEETMKkeQPGVVILNTG-WAHVLGFGPIIMGKEDVLKTHQVLPKAKIVATHM 221
Cdd:pfam12706 142 FPDeIGERLG--GADLLLLDGGaWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
4-72 5.30e-03

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 37.48  E-value: 5.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927313394   4 TQIRNAT-QVIDYAGKTFLIDPmlapkgtypGfEGTANSHLRnptveLPLPLESIinvDAVLLTHTHPDH 72
Cdd:COG1234   14 TPGRATSsYLLEAGGERLLIDC---------G-EGTQRQLLR-----AGLDPRDI---DAIFITHLHGDH 65
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 44-84 6.00e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 36.82  E-value: 6.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 927313394  44 RNPTVELPLPLESIINVDAVLLTHTHPDHWDetAVNAIPKD 84
Cdd:cd07732   60 RDPLLLGGLRSEEDPSVDAVLLSHAHLDHYG--LLNYLRPD 98
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 12-72 9.62e-03

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: 36.11  E-value: 9.62e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927313394  12 VIDYAGKTFLIDPmlapkgtypGFEGTANshLRNPTVELPLplesiiNVDAVLLTHTHPDH 72
Cdd:cd06262   15 VSDEEGEAILIDP---------GAGALEK--ILEAIEELGL------KIKAILLTHGHFDH 58
 
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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