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Conserved domains on  [gi|816166757|emb|CDZ53086|]
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L1 beta-lactamase [Neorhizobium galegae bv. orientalis]

Protein Classification

CAU/MBL1b family subclass B3 metallo-beta-lactamase( domain architecture ID 10888866)

CAU/MBL1b family subclass B3 metallo-beta-lactamase hydrolyzes the beta-lactam ring of beta-lactam antibiotics such as penicillin, cephalosporin and carbapenem, resulting in antibiotic resistance

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 30-281 2.81e-164

Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of Mbl1b-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


:

Pssm-ID: 293868  Cd Length: 252  Bit Score: 455.76  E-value: 2.81e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  30 WSEPASPFRITDNIYYVGTKGLASYLIISGREAILLDATLDENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRL 109
Cdd:cd16310    1 WTAPTEPFRIVDNIYYVGTKGIGSYLITSNHGAILLDGGLEENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 110 KKSTGAEVAAMAGDKSALENGRQEGDTDYGGAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSPDRGS 189
Cdd:cd16310   81 KADTGAKLWASRGDRPALEAGKHIGDNITQPAPFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTWSTTVKENGR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 190 VRRVVFPCSISVAGNILVDNKSYPTIVEDFRRSFGRLASMKADVVLPAHPEVVGLFKRKEKLDAGDNQAFVDSGLLIKIV 269
Cdd:cd16310  161 PLRVVFPCSLSVAGNVLVGNKTYPTIVEDYRASFARLRAMKADIVLTSHPEVADLLARKAKQDAGQANAFVDPGELARIV 240

                        250
                 ....*....|..
gi 816166757 270 DQSRVAFDRALA 281
Cdd:cd16310  241 DQSEAAFNKELA 252
 
Name Accession Description Interval E-value
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 30-281 2.81e-164

Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of Mbl1b-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293868  Cd Length: 252  Bit Score: 455.76  E-value: 2.81e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  30 WSEPASPFRITDNIYYVGTKGLASYLIISGREAILLDATLDENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRL 109
Cdd:cd16310    1 WTAPTEPFRIVDNIYYVGTKGIGSYLITSNHGAILLDGGLEENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 110 KKSTGAEVAAMAGDKSALENGRQEGDTDYGGAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSPDRGS 189
Cdd:cd16310   81 KADTGAKLWASRGDRPALEAGKHIGDNITQPAPFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTWSTTVKENGR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 190 VRRVVFPCSISVAGNILVDNKSYPTIVEDFRRSFGRLASMKADVVLPAHPEVVGLFKRKEKLDAGDNQAFVDSGLLIKIV 269
Cdd:cd16310  161 PLRVVFPCSLSVAGNVLVGNKTYPTIVEDYRASFARLRAMKADIVLTSHPEVADLLARKAKQDAGQANAFVDPGELARIV 240

                        250
                 ....*....|..
gi 816166757 270 DQSRVAFDRALA 281
Cdd:cd16310  241 DQSEAAFNKELA 252
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 53-238 2.89e-29

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: 110.55  E-value: 2.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  53 SYLIISGREAILLDATLDENVAS-IERNIQSLEfglRDIKIIINSHAHFDHAAGIGRLKKSTGAEVAAMAGDKSALENGR 131
Cdd:COG0491   17 SYLIVGGDGAVLIDTGLGPADAEaLLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEAPA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 132 QEGDTDyggavFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSpdrgsvRRVVFpcsisvAGNILVDNKS 211
Cdd:COG0491   94 AGALFG-----REPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPD------EKVLF------TGDALFSGGV 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 816166757 212 YPTI-----VEDFRRSFGRLASMKADVVLPAH 238
Cdd:COG0491  157 GRPDlpdgdLAQWLASLERLLALPPDLVIPGH 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 53-238 2.17e-28

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: 107.25  E-value: 2.17e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757    53 SYLIISGREAILLDATLDEnvasIERNIQSLE-FGLRDIKIIINSHAHFDHAAGIGRLKKSTGAEVAAMAGDKSALENGR 131
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGE----AEDLLAELKkLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757   132 QEGdtDYGGAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSpdrgsvRRVVFPCSISVAGNILVDNKS 211
Cdd:smart00849  78 ALL--GELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPE------GKILFTGDLLFAGGDGRTLVD 149

                          170       180
                   ....*....|....*....|....*...
gi 816166757   212 YPTI-VEDFRRSFGRLASMKADVVLPAH 238
Cdd:smart00849 150 GGDAaASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
53-238 8.98e-23

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 92.82  E-value: 8.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757   53 SYLIISGREAILLDATLDENvASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRLKKSTGAEVAAMAGDKSALENGRQ 132
Cdd:pfam00753   8 SYLIEGGGGAVLIDTGGSAE-AALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  133 EGDTDYGGAVFPAV---KVDRILNDGDKVTLGDVTLTASLTAGHTKGCttWSMTSPDrgsvRRVVFPCSISVAGNILVDN 209
Cdd:pfam00753  87 GLAASRLGLPGPPVvplPPDVVLEEGDGILGGGLGLLVTHGPGHGPGH--VVVYYGG----GKVLFTGDLLFAGEIGRLD 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 816166757  210 K-------SYPTIVEDFRRSFGRLASMKADVVLPAH 238
Cdd:pfam00753 161 LplggllvLHPSSAESSLESLLKLAKLKAAVIVPGH 196
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 60-180 1.16e-08

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 54.42  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  60 REAILLDA---TLDENVASIErniqslEFGLRdIKIIINSHAHFDHAAGIGRLKKStgaevaaMAGDKSALENGRQEgdt 136
Cdd:PLN02962  36 KPALLIDPvdkTVDRDLSLVK------ELGLK-LIYAMNTHVHADHVTGTGLLKTK-------LPGVKSIISKASGS--- 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 816166757 137 dyggavfpavKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTW 180
Cdd:PLN02962  99 ----------KADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTY 132
 
Name Accession Description Interval E-value
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 30-281 2.81e-164

Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of Mbl1b-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293868  Cd Length: 252  Bit Score: 455.76  E-value: 2.81e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  30 WSEPASPFRITDNIYYVGTKGLASYLIISGREAILLDATLDENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRL 109
Cdd:cd16310    1 WTAPTEPFRIVDNIYYVGTKGIGSYLITSNHGAILLDGGLEENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 110 KKSTGAEVAAMAGDKSALENGRQEGDTDYGGAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSPDRGS 189
Cdd:cd16310   81 KADTGAKLWASRGDRPALEAGKHIGDNITQPAPFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTWSTTVKENGR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 190 VRRVVFPCSISVAGNILVDNKSYPTIVEDFRRSFGRLASMKADVVLPAHPEVVGLFKRKEKLDAGDNQAFVDSGLLIKIV 269
Cdd:cd16310  161 PLRVVFPCSLSVAGNVLVGNKTYPTIVEDYRASFARLRAMKADIVLTSHPEVADLLARKAKQDAGQANAFVDPGELARIV 240

                        250
                 ....*....|..
gi 816166757 270 DQSRVAFDRALA 281
Cdd:cd16310  241 DQSEAAFNKELA 252
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 30-281 4.05e-107

BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Bradyrhizobium diazoefficiens BJP-1, Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Caulobacter crescentus Mbl1b. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 311.18  E-value: 4.05e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  30 WSEPASPFRITDNIYYVGTKGLASYLIISGREAILLDATLDENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRL 109
Cdd:cd16288    1 WNAPFEPFRIAGNVYYVGTSGLASYLITTPQGLILIDTGLESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 110 KKSTGAEVAAMAGDKSALENG-RQEGDTDYGGAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSPDRG 188
Cdd:cd16288   81 KKLTGAKLMASAEDAALLASGgKSDFHYGDDSLAFPPVKVDRVLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTMTVKDDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 189 SVRRVVFPCSISVA-GNILVDNKSYPTIVEDFRRSFGRLASMKADVVLPAHPEVVGLFKRKEKLDAGDNQAFVDSGLLIK 267
Cdd:cd16288  161 KVYQVVFADSLTVNpGYKLVGNPTYPGIAEDYRHSFATLRALQCDIFLASHAEYFDLKEKRARLAAGQPNAFIDPEGYRN 240

                        250
                 ....*....|....
gi 816166757 268 IVDQSRVAFDRALA 281
Cdd:cd16288  241 FIEKAKADFEKQLA 254
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 30-281 1.93e-98

Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of BJP-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 289.00  E-value: 1.93e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  30 WSEPASPFRITDNIYYVGTKGLASYLIISGREAILLDATLDENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRL 109
Cdd:cd16309    1 WNEPMEPFKLIGNIYYVGTAGLGVFLITTPEGHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 110 KKSTGAEVAAMAGDKSALENGRQ-EGDTDYggAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTS-PDR 187
Cdd:cd16309   81 KKATGAQLVASAADKPLLESGYVgSGDTKN--LQFPPVRVDRVIGDGDKVTLGGTTLTAHLTPGHSPGCTSWTTTVkDTA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 188 GSVRRVVFPCSISVAGNILVDNKSYPTIVEDFRRSFGRLASMKADVVLPAHPEVVGLFKRKEKLDAGDNQAFVDSGLLIK 267
Cdd:cd16309  159 GPPREVLFFCSATVAGNQLVGPPTYPGIVDDYRATFAKARAMKADVFLANHPEFFGLVAKRARQSAGEPDAFVDAGELQR 238

                        250
                 ....*....|....
gi 816166757 268 IVDQSRVAFDRALA 281
Cdd:cd16309  239 FNTKMEDDFEKALA 252
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 30-273 5.81e-94

metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B3 MBLs include Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Stenotrophomonas Maltophilia L1, and Bradyrhizobium diazoefficiens BJP-1, Serratia marcescens SMB-1, and Pseudomonas Aeruginosa AIM-1. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 277.50  E-value: 5.81e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  30 WSEPASPFRITDNIYYVGTKGLASYLIISGREAILLDATLDENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRL 109
Cdd:cd07708    1 WPNPFPPFQIAGNTYYVGTDDLAAYLIVTPQGNILIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 110 KKSTGAEVAAMAGDKSALENGRQEGDTDYGGAV--FPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSPDR 187
Cdd:cd07708   81 KKQTGAKVMAGAEDVSLLLSGGSSDFHYANDSStyFPQSTVDRAVHDGERVTLGGTVLTAHATPGHTPGCTTWTMTLKDH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 188 GSVRRVVFPCSISVA-GNILVDNKSYPTIVEDFRRSFGRLASMKADVVLPAHPEVVGLFKRKEKLDAGDNQAFVDSGLLI 266
Cdd:cd07708  161 GKQYQVVFADSLTVNpGYRLVDNPTYPKIVEDYRHSFAVVEAMRCDILLGPHPGVFDMKNKYVLLSKGQNNPFVDPGGCK 240


                 ....*..
gi 816166757 267 KIVDQSR 273
Cdd:cd07708  241 AYAEAKA 247
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 30-281 2.16e-81

Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of FEZ-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293865  Cd Length: 255  Bit Score: 245.82  E-value: 2.16e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  30 WSEPASPFRITDNIYYVGTKGLASYLIISGREAILLDATLDENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRL 109
Cdd:cd16307    1 WTTPFPPFRIAGNLYYVGSRDLASYLITTPRGNILINSNLESSVPQIKASIEKLGFKFSDTKILLISHAHFDHAAGSALI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 110 KKSTGAEVAAMAGDKSALENGRQEgDTDYG---GAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSPD 186
Cdd:cd16307   81 KRETHAKYMVMDGDVDVVESGGKS-DFFYGndpSTYFPPAHVDKVLHDGEQVELGGTVLTAHLTAGHTKGCTTWTMKVKD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 187 RGSVRRVVFPCSISV-AGNILVDNKSYPTIVEDFRRSFGRLASMKADVVLPAHPEVVGLFKRKEKLDAGDNQAFVDSGLL 265
Cdd:cd16307  160 HGKTYDVVIVGSPNVnPGAKLVNNITYPGIAEDYAHTFAVLRSLPCDIFLGAHGGYFDLKNKYVRLQKGGANPFIDPEGY 239

                        250
                 ....*....|....*.
gi 816166757 266 IKIVDQSRVAFDRALA 281
Cdd:cd16307  240 KAYVAEKEQAFRTELE 255
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 30-263 1.57e-70

AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Pseudomonas Aeruginosa AIM-1, Serratia marcescens SMB-1, Erythrobacter vulgaris EVM-1, and Janthinobacterium lividum THIN-B. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of AIM-1-,SMB-1-, EVM-1-, THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 218.37  E-value: 1.57e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  30 WSEPASPFRITDNIYYVGTKGLASYLIISGREAILLDATLDENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRL 109
Cdd:cd16290    1 WNQPQAPFRIHGNTYYVGTGGLSAVLITSPQGLILIDGALPQSAPQIEANIRALGFRLEDVKLILNSHAHFDHAGGIAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 110 KKSTGAEVAAMAGDKSALENGRQeGDTD--YGGAV-FPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSPD 186
Cdd:cd16290   81 QRDSGATVAASPAGAAALRSGGV-DPDDpqAGAADpFPPVAKVRVVADGEVVKLGPLAVTAHATPGHTPGGTSWTWRSCE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 187 RGSVRRVVFPCSISV--AGNILVDNKSYPTIVEDFRRSFGRLASMKADVVLPAHPEVVGLFKRKEKLDAG-DNQAFVDSG 263
Cdd:cd16290  160 GGRCLDIVYADSLTAvsADGFRFSDDAHPARVAAFRRSIATVAALPCDILISAHPDASGLWEKLARRAREpGPNPFIDPN 239
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 30-281 9.18e-59

SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of SMB-1- and THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 188.15  E-value: 9.18e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  30 WSEPASPFRITDNIYYVGTKGLASYLIISGREAILLDATLDENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRL 109
Cdd:cd16313    1 WNAPQEPFQIYGNTYYVGTGGISAVLITSPQGHILIDGGFPKSPEQIAASIRQLGFKLEDVKYILSSHDHWDHAGGIAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 110 KKSTGAEVAAMAGDKSALENGRQ-EGDTDYGG-AVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSPDR 187
Cdd:cd16313   81 QKLTGAQVLASPATVAVLRSGSMgKDDPQFGGlTPMPPVASVRAVRDGEVVKLGPLAVTAHATPGHTTGGTSWTWQSCEQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 188 GSVRRVVFPCSISVAGNILVDNKSYPTIVEDFRRSFGRLASMKADVVLPAHPEVVGLFKRKEKLDAGDNQAFVDSGLLIK 267
Cdd:cd16313  161 GRCANMVFADSLTAVSADGYRFSAHPAVLADVEQSIAAVEKLACDILVSAHPEFSDMWTRVKRGAAEGNAAFIDGGGCRA 240

                        250
                 ....*....|....
gi 816166757 268 IVDQSRVAFDRALA 281
Cdd:cd16313  241 YAAKAREKLNKRLA 254
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 30-247 6.61e-58

Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup EVM-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 185.63  E-value: 6.61e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  30 WSEPASPFRITDNIYYVGTKGLASYLIISGREAILLDATLDENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRL 109
Cdd:cd16315    1 WDKPAPPARIFGNTYYVGTCGISAILITGDDGHVLIDSGTEEAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 110 KKSTGAEVAAMAGDKSALENGRQEGDTDYGGAV--FPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSPDR 187
Cdd:cd16315   81 QRATGARVAASAAAAPVLESGKPAPDDPQAGLHepFPPVRVDRIVEDGDTVALGSLRLTAHATPGHTPGALSWTWRSCEG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 816166757 188 GSVRRVVFPCSISVagnilVDNKSY-----PTIVEDFRRSFGRLASMKADVVLPAHPEVVGLFKR 247
Cdd:cd16315  161 ADCRTIVYADSLSP-----VSADGYrfsdhPDYVAAYRAGLAKVAALPCDILLTPHPSASDMFER 220
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 30-281 1.10e-56

Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of THIN-B2-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293869  Cd Length: 257  Bit Score: 182.88  E-value: 1.10e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  30 WSEPASPFRITDNIYYVGTKGLASYLIISGREAILLDATLDENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRL 109
Cdd:cd16311    1 WNADQAPFRIFGNTYYVGVKGLSSVLVTSPQGHVLVDGGLPESAPKIIANIEALGFRIEDVKLILNSHGHIDHAGGLAEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 110 KKSTGAEVAAMAGDKSALENGRQEGDTDYGGAV--FPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSPDR 187
Cdd:cd16311   81 QRRSGALVAASPSAALDLASGEVGPDDPQYHALpkYPPVKDMRLARDGGQFNVGPVSLTAHATPGHTPGGLSWTWQSCDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 188 GSVRRVVFPCSI---SVAGNILVDNKSYPTIVEDFRRSFGRLASMKADVVLPAHPEVVGLFKRKEKLDAGDNQAFVDSGL 264
Cdd:cd16311  161 PRCLNMVYADSQnavSRPGFKFSASSEYPNAVADLRRSFETLEKLPCDVLISAHPEASQLWERLEASDRSARPALVDREA 240

                        250
                 ....*....|....*..
gi 816166757 265 LIKIVDQSRVAFDRALA 281
Cdd:cd16311  241 CRRYASRAREALEKRIA 257
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 30-281 3.14e-55

Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of GOB-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 179.20  E-value: 3.14e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  30 WSEPASPFRITDNIYYVGTKGLASYLIISGREAILLDATLDENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRL 109
Cdd:cd16308    1 WSQPYAPFRIAGNLYYVGTYDLACYLIVTPKGNILINTGLAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 110 KKSTGAEVAAMAGDKSALENGrqeGDTDY----GGAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSP 185
Cdd:cd16308   81 KQQTGAKMMVDEKDAKVLADG---GKSDYemggYGSTFAPVKADKLLHDGDTIKLGGTKLTLLHHPGHTKGSCSFLFDVK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 186 DRGSVRRVVfpcsISVAGNILVDNK-----SYPTIVEDFRRSFGRLASMKADVVLPAHPEVVGLFKRKEKLDAGDNQAFV 260
Cdd:cd16308  158 DEKRTYRVL----IANMPTILPDTKlsgmpGYPGIAKDYAYTFEAMKALSFDIWLASHASQFDLHQKHKPGAPYNPAAFA 233

                        250       260
                 ....*....|....*....|.
gi 816166757 261 DSGLLIKIVDQSRVAFDRALA 281
Cdd:cd16308  234 DRAGYDKALAGLEKSYDKKIK 254
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 30-243 8.15e-54

Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of L1- and Pom-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293847  Cd Length: 239  Bit Score: 175.00  E-value: 8.15e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  30 WSEPASPFRITDNIYYVGTKGLASYLIISGREAILLDATLDENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRL 109
Cdd:cd16289    1 WLQPMAPLQIADHTWYIGTESLTALLVKTPDGAVLLDGGMPQAADMLLDNMRALGVAPGDLKLILHSHAHADHAGPLAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 110 KKSTGAEVAAMAGDKSALENGRQEgDTDYG-GAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSPDRG 188
Cdd:cd16289   81 KRATGARVAANAESAVLLARGGSD-DIHFGdGITFPPVQADRIVMDGEVVTLGGVTFTAHFTPGHTPGSTSWTWTDTRDG 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 816166757 189 SVRRVVFPCSISVAGNILVDNKSYPTIVEDFRRSFGRLASMKADVVLPAHPEVVG 243
Cdd:cd16289  160 KPVRIAYADSLSAPGYQLLGNPRYPRIVEDYRRTFATVRALPCDVLLTPHPGASG 214
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 30-281 3.08e-53

Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 174.02  E-value: 3.08e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  30 WSEPASPFRITDNIYYVGTKGLASYLIISGREAILLDATLDENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRL 109
Cdd:cd16312    1 WNQPVKPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIEALGFRIEDVKLILNSHAHWDHAGGIAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 110 KKSTGAEVAAMAGDKSALENGRQ-EGDTDYGG---AVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSP 185
Cdd:cd16312   81 QKASGATVAASAHGAQVLQSGTNgKDDPQYQAkpvVHVAKVAKVKEVGEGDTLKVGPLRLTAHMTPGHTPGGTTWTWTSC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 186 DRGSVRRVVFPCSI---SVAGNILVDNKSYPTIVEDFRRSFGRLASMKADVVLPAHPEVVGLFKrKEKLDAGDNQAFVDS 262
Cdd:cd16312  161 EGQRCLDVVYADSLnpySSGDFYYTGKGGYPDISASFRASIAKVAALPCDIIIAVHPGFTDVLD-KAKRRSGDTNPFIDA 239

                        250
                 ....*....|....*....
gi 816166757 263 GLLIKIVDQSRVAFDRALA 281
Cdd:cd16312  240 EACRAYAAGAAKSLEKRLA 258
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 30-285 2.11e-49

Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup AIM-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 163.91  E-value: 2.11e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  30 WSEPASPFRITDNIYYVGTKGLASYLIISGREAILLDATLDENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRL 109
Cdd:cd16314    1 WDDPAPPRRIYGNTWYVGTCGISALLVTSDAGHILIDGGTDKAAPLIEANIRALGFRPEDVRYIVSSHEHFDHAGGIARL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 110 KKSTGAEVAAMAGDKSALENGRQE-GDTDYG-GAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSPDR 187
Cdd:cd16314   81 QRATGAPVVAREPAATTLERGRSDrSDPQFLvVEKFPPVASVQRIGDGEVLRVGPLALTAHATPGHTPGGTSWTWRSCEG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 188 GSVRRVVFPCSISVAGNILVDNKSYPTIVEDFRRSFGRLASMKADVVLPAHPEVVGLFKRkekLDAGDNQAFVDSGLLIK 267
Cdd:cd16314  161 AVCRDMVYADSVTAISDDIYRYSDHPGMVAAFRNTLDTVAALPCDILVTPHPSASGLWER---LGPAAGIPLADTGACRA 237

                        250
                 ....*....|....*...
gi 816166757 268 IVDQSRVAFDRALASARA 285
Cdd:cd16314  238 YAQTGRARLDARLADEAA 255
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 36-263 1.44e-38

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) 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: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 135.79  E-value: 1.44e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  36 PFRITDNIYYVGTKGLASYLIISGREAILLDaTLDENVAS--IERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRLKKST 113
Cdd:cd16280    7 PFQVFDNLYYVGNKWVSAWAIDTGDGLILID-ALNNNEAAdlIVDGLEKLGLDPADIKYILITHGHGDHYGGAAYLKDLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 114 GAEVAAMAGDKSALENGRQEGDtdyGGAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTtwSMTSP--DRGSVR 191
Cdd:cd16280   86 GAKVVMSEADWDMMEEPPEEGD---NPRWGPPPERDIVIKDGDTLTLGDTTITVYLTPGHTPGTL--SLIFPvkDGGKTH 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 816166757 192 RVVfpcsisVAGNILVDNKSYPTIVEDFRRSFGRLASMK----ADVVLPAHPEVVGLFKRKEKL---DAGDNQAFVDSG 263
Cdd:cd16280  161 RAG------LWGGTGLNTGPNLERREQYIASLERFKKIAeeagVDVFLSNHPFQDGSLEKREALrnrKPGEPNPFVDGQ 233
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 53-238 2.89e-29

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: 110.55  E-value: 2.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  53 SYLIISGREAILLDATLDENVAS-IERNIQSLEfglRDIKIIINSHAHFDHAAGIGRLKKSTGAEVAAMAGDKSALENGR 131
Cdd:COG0491   17 SYLIVGGDGAVLIDTGLGPADAEaLLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEAPA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 132 QEGDTDyggavFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSpdrgsvRRVVFpcsisvAGNILVDNKS 211
Cdd:COG0491   94 AGALFG-----REPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPD------EKVLF------TGDALFSGGV 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 816166757 212 YPTI-----VEDFRRSFGRLASMKADVVLPAH 238
Cdd:COG0491  157 GRPDlpdgdLAQWLASLERLLALPPDLVIPGH 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 53-238 2.17e-28

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: 107.25  E-value: 2.17e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757    53 SYLIISGREAILLDATLDEnvasIERNIQSLE-FGLRDIKIIINSHAHFDHAAGIGRLKKSTGAEVAAMAGDKSALENGR 131
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGE----AEDLLAELKkLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757   132 QEGdtDYGGAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSpdrgsvRRVVFPCSISVAGNILVDNKS 211
Cdd:smart00849  78 ALL--GELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPE------GKILFTGDLLFAGGDGRTLVD 149

                          170       180
                   ....*....|....*....|....*...
gi 816166757   212 YPTI-VEDFRRSFGRLASMKADVVLPAH 238
Cdd:smart00849 150 GGDAaASDALESLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 53-178 1.55e-24

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: 97.36  E-value: 1.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  53 SYLIISG-REAILLDATLDenvaSIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRLKKSTGAEVAAMAGDKSALENGr 131
Cdd:cd06262   12 CYLVSDEeGEAILIDPGAG----ALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAELLEDP- 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 816166757 132 QEGDTDYGGAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCT 178
Cdd:cd06262   87 ELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSV 133
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
53-238 8.98e-23

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 92.82  E-value: 8.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757   53 SYLIISGREAILLDATLDENvASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRLKKSTGAEVAAMAGDKSALENGRQ 132
Cdd:pfam00753   8 SYLIEGGGGAVLIDTGGSAE-AALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  133 EGDTDYGGAVFPAV---KVDRILNDGDKVTLGDVTLTASLTAGHTKGCttWSMTSPDrgsvRRVVFPCSISVAGNILVDN 209
Cdd:pfam00753  87 GLAASRLGLPGPPVvplPPDVVLEEGDGILGGGLGLLVTHGPGHGPGH--VVVYYGG----GKVLFTGDLLFAGEIGRLD 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 816166757  210 K-------SYPTIVEDFRRSFGRLASMKADVVLPAH 238
Cdd:pfam00753 161 LplggllvLHPSSAESSLESLLKLAKLKAAVIVPGH 196
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 54-238 3.81e-19

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 83.04  E-value: 3.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  54 YLIISGREAILLDATLDENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRLKKSTGAEVAAMAGDKSALENGRQE 133
Cdd:cd07721   14 YLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREAPYLEGEKPY 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 134 GDTDYGG------AVFP--AVKVDRILNDGDKVTLGDvTLTASLTAGHTKGCTtwSMTSPDRGSVrrvvfpcsIS---VA 202
Cdd:cd07721   94 PPPVRLGllgllsPLLPvkPVPVDRTLEDGDTLDLAG-GLRVIHTPGHTPGHI--SLYLEEDGVL--------IAgdaLV 162

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 816166757 203 GNILVDNKSYPTIVEDF---RRSFGRLASMKADVVLPAH 238
Cdd:cd07721  163 TVGGELVPPPPPFTWDMeeaLESLRKLAELDPEVLAPGH 201
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 44-187 1.27e-18

ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; MBL-fold metallo-hydrolase domain; Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO, EC 1.13.11.18) is a non-heme iron-dependent oxygenase which catalyzes the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria. Mutations in ethe1 (the human PDO gene) are responsible for a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy. Arabidopsis thaliana ETHE1 is essential for embryo and endosperm development. Bacterial ETHE1-type PDOs are also called Type 1 PDOs. Type II PDOs (also called PDOAs), are mainly proteobacterial. These enzymes 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: 293810 [Multi-domain]  Cd Length: 177  Bit Score: 80.91  E-value: 1.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  44 YYVGTKGLASYLIISG--REAILLDATLDenvaSIERNIQSL-EFGLRdIKIIINSHAHFDHAAGIGRLKKSTGAEVAAm 120
Cdd:cd07724    5 FFDPGLGTLSYLVGDPetGEAAVIDPVRD----SVDRYLDLAaELGLK-ITYVLETHVHADHVSGARELAERTGAPIVI- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 816166757 121 agdksalengrqegdtdygGAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSPDR 187
Cdd:cd07724   79 -------------------GEGAPASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDA 126
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 54-238 5.39e-18

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 79.88  E-value: 5.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  54 YLIISGREAILLDATLDENVA-SIERNIQSLEFGlrdIKIIINSHAHFDHAAGIGRLKKSTGAEVAAMAGDKSALENGRQ 132
Cdd:cd07743   12 VYVFGDKEALLIDSGLDEDAGrKIRKILEELGWK---LKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFIENPLL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 133 EGDTDYGGAVFPA----------VKVDRILNDGdKVTLGDVTLTASLTAGHtkgctTWSMT---SPDrgsvrRVVFpCSI 199
Cdd:cd07743   89 EPSYLGGAYPPKElrnkflmakpSKVDDIIEEG-ELELGGVGLEIIPLPGH-----SFGQIgilTPD-----GVLF-AGD 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 816166757 200 SVAGNILVDNKSYPTI--VEDFRRSFGRLASMKADVVLPAH 238
Cdd:cd07743  157 ALFGEEVLEKYGIPFLydVEEQLETLEKLEELDADYYVPGH 197
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 54-196 7.16e-15

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 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. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 71.61  E-value: 7.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  54 YLIIS--GREAILLDaTLDENVASIERniqsLEFGLRDIKIIINSHAHFDHAAGIGRLKKSTGAEVAAMAGDKSALENGR 131
Cdd:cd16322   14 YLVADegGGEAVLVD-PGDESEKLLAR----FGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDLPLYEAAD 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 816166757 132 QEGDTdYGGAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSMTSPD---------RGSVRRVVFP 196
Cdd:cd16322   89 LGAKA-FGLGIEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGllfsgdllfQGSIGRTDLP 161
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 44-175 2.36e-14

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 70.21  E-value: 2.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  44 YYVGTKGL-ASYLIISGREAILLDATLDENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRL-KKSTGAEVAA-- 119
Cdd:cd07726    8 GFLGFPGRiASYLLDGEGRPALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLaEALPNAKVYVhp 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 816166757 120 -----MAgDKSALENGRQE--GDT--DYGGAVFPaVKVDRI--LNDGDKVTLGDVTLTASLTAGHTK 175
Cdd:cd07726   88 rgarhLI-DPSKLWASARAvyGDEadRLGGEILP-VPEERVivLEDGETLDLGGRTLEVIDTPGHAP 152
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 53-238 3.85e-14

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 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: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 69.19  E-value: 3.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  53 SYLIISGREAILLDATLdeNVASIERNIQSLefGLRDIkIIINSHAHFDHAAGIGRLkkstgAEVAAMAGDKSAL--ENG 130
Cdd:cd07712   11 IYLLRGRDRALLIDTGL--GIGDLKEYVRTL--TDLPL-LVVATHGHFDHIGGLHEF-----EEVYVHPADAEILaaPDN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 131 RQEGDTDYGGAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKGcttwSMTSPDRGsvRRVVFPCSISVAGNILVDNK 210
Cdd:cd07712   81 FETLTWDAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPG----SIALLDRA--NRLLFSGDVVYDGPLIMDLP 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 816166757 211 SYPtiVEDFRRSFGRLASMK--ADVVLPAH 238
Cdd:cd07712  155 HSD--LDDYLASLEKLSKLPdeFDKVLPGH 182
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 53-176 1.54e-13

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 67.10  E-value: 1.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  53 SYLIISG--REAILLDATLDENV-ASIERNiqslefGLRdIKIIINSHAHFDHAAGIGRLKKSTG-AEVaamagdksale 128
Cdd:cd07723   11 IYLIVDEatGEAAVVDPGEAEPVlAALEKN------GLT-LTAILTTHHHWDHTGGNAELKALFPdAPV----------- 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 816166757 129 ngrqegdtdYGGAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKG 176
Cdd:cd07723   73 ---------YGPAEDRIPGLDHPVKDGDEIKLGGLEVKVLHTPGHTLG 111
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 45-242 2.39e-12

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) 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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 64.05  E-value: 2.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  45 YVGTKglaSYLIISGREAILLD--ATLDENVASIERNIQSlefglRDIKIIINSHAHFDHAAGIGRLKKSTGAEVAAMag 122
Cdd:cd16278   15 LDGTN---TYLLGAPDGVVVIDpgPDDPAHLDALLAALGG-----GRVSAILVTHTHRDHSPGAARLAERTGAPVRAF-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 123 dksalengrqegDTDYGGAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTK--------------------GCTTwSM 182
Cdd:cd16278   85 ------------GPHRAGGQDTDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSdhlcfaledegalftgdhvmGWST-TV 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 183 TSPDRGSVRrvvfpcsisvagnilvdnksyptiveDFRRSFGRLASMKADVVLPAHPEVV 242
Cdd:cd16278  152 IAPPDGDLG--------------------------DYLASLERLLALDDRLLLPGHGPPI 185
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 53-176 5.47e-11

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes 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: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 61.08  E-value: 5.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  53 SYLIISGREAILLDATLDENVA------------------SIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRLKKST- 113
Cdd:cd07729   34 AYLIEHPEGTILVDTGFHPDAAddpgglelafppgvteeqTLEEQLARLGLDPEDIDYVILSHLHFDHAGGLDLFPNATi 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 816166757 114 ---GAEVAAMAGDKSALENGRQEGDTDYggAVFPAVKVDRIlnDGDKVTLGDVTLTasLTAGHTKG 176
Cdd:cd07729  114 ivqRAELEYATGPDPLAAGYYEDVLALD--DDLPGGRVRLV--DGDYDLFPGVTLI--PTPGHTPG 173
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 53-242 7.14e-11

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: 60.00  E-value: 7.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  53 SYLIISGREAILLDATLD--ENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRLKKSTGAEVAAMAgdksaleng 130
Cdd:cd07725   17 VYLLRDGDETTLIDTGLAteEDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGATVYILD--------- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 131 rqegdtdyggavfpavkvDRILNDGDKVTLGDVTLTASLTAGHTKGCTTWSmtspDRGsvRRVVFpcsisVAGNILVD-- 208
Cdd:cd07725   88 ------------------VTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLY----DED--RRELF-----VGDAVLPKit 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 816166757 209 -NKS-YPTIVED----FRRSFGRLASMKADVVLPAHPEVV 242
Cdd:cd07725  139 pNVSlWAVRVEDplgaYLESLDKLEKLDVDLAYPGHGGPI 178
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 60-176 2.29e-10

Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Salmonella enterica serovar typhimurium YcbL which has type II hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as glyoxalase II) activity, and has a single metal ion binding site, and Thermus thermophilus TTHA1623 which does not have GLX2 activity and has two metal ion binding sites with a glyoxalase II-type metal coordination. 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: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 58.72  E-value: 2.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  60 REAILLDATLDenvasIERNIQSLE-FGLRDIKIIInSHAHFDHAAGIGRLKKSTGAEVAA-MAGDKSALENGRQEGDTd 137
Cdd:cd07737   22 KEAAVIDPGGD-----ADKILQAIEdLGLTLKKILL-THGHLDHVGGAAELAEHYGVPIIGpHKEDKFLLENLPEQSQM- 94

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 816166757 138 YGGAVFPAVKVDRILNDGDKVTLGDVTLTASLTAGHTKG 176
Cdd:cd07737   95 FGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPG 133
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 55-238 4.54e-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) 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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 55.26  E-value: 4.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  55 LIISGREAILLDATLDENVA-SIERNIQSLefGLRDIKIIINSHAHFDHAAGIGRLKKsTGAEVAAMAGDKSALENgRQE 133
Cdd:cd16282   19 FIVGDDGVVVIDTGASPRLArALLAAIRKV--TDKPVRYVVNTHYHGDHTLGNAAFAD-AGAPIIAHENTREELAA-RGE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 134 GDTD----YGGAVFPAVKV---DRILNDGDKVTLGDVTLTA-SLTAGHTKGcttwsmtspDrgSV-----RRVVFpcsis 200
Cdd:cd16282   95 AYLElmrrLGGDAMAGTELvlpDRTFDDGLTLDLGGRTVELiHLGPAHTPG---------D--LVvwlpeEGVLF----- 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 816166757 201 vAGNiLVDNKSYPTI----VEDFRRSFGRLASMKADVVLPAH 238
Cdd:cd16282  159 -AGD-LVFNGRIPFLpdgsLAGWIAALDRLLALDATVVVPGH 198
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 60-180 1.16e-08

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 54.42  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  60 REAILLDA---TLDENVASIErniqslEFGLRdIKIIINSHAHFDHAAGIGRLKKStgaevaaMAGDKSALENGRQEgdt 136
Cdd:PLN02962  36 KPALLIDPvdkTVDRDLSLVK------ELGLK-LIYAMNTHVHADHVTGTGLLKTK-------LPGVKSIISKASGS--- 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 816166757 137 dyggavfpavKVDRILNDGDKVTLGDVTLTASLTAGHTKGCTTW 180
Cdd:PLN02962  99 ----------KADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTY 132
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 53-242 4.42e-08

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: 52.15  E-value: 4.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  53 SYLIISGREAILLDATldENVASIERNIQSL--EFGLRDIKIIINSHAHFDHAAGIGRLKKS-TGAEVAAMagdKSALEN 129
Cdd:cd07722   20 TYLVGTGKRRILIDTG--EGRPSYIPLLKSVldSEGNATISDILLTHWHHDHVGGLPDVLDLlRGPSPRVY---KFPRPE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 130 GRQEGDTDYGGAVFpavkvdriLNDGDKVTLGDVTLTASLTAGHTKgcttwsmtspDRGSVR----RVVFpcsisVAGNI 205
Cdd:cd07722   95 EDEDPDEDGGDIHD--------LQDGQVFKVEGATLRVIHTPGHTT----------DHVCFLleeeNALF-----TGDCV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 816166757 206 LvdNKSYpTIVEDFR---RSFGRLASMKADVVLPAHPEVV 242
Cdd:cd07722  152 L--GHGT-AVFEDLAaymASLKKLLSLGPGRIYPGHGPVI 188
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 52-167 2.77e-07

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 50.66  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  52 ASYLIISGREAILLDATLDenvasIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRLKKSTGAE---VAAMAGDKSALE 128
Cdd:COG1235   36 SSILVEADGTRLLIDAGPD-----LREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYGPNpipVYATPGTLEALE 110

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 816166757 129 NGrqegdTDYGGAVFPAVKVDRILNDGDKVTLGDVTLTA 167
Cdd:COG1235  111 RR-----FPYLFAPYPGKLEFHEIEPGEPFEIGGLTVTP 144
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 43-167 7.65e-07

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 48.76  E-value: 7.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  43 IYYVGTkglASYLIISGREAILLDATLDENVASIERNIQSLEfGLRDIKIIINSHAHFDHA--AGIGRLKKsTGAEVAAM 120
Cdd:COG2220    6 ITWLGH---ATFLIETGGKRILIDPVFSGRASPVNPLPLDPE-DLPKIDAVLVTHDHYDHLddATLRALKR-TGATVVAP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 816166757 121 AGDKSALengRQEGdtdyggavFPAVkvdRILNDGDKVTLGDVTLTA 167
Cdd:COG2220   81 LGVAAWL---RAWG--------FPRV---TELDWGESVELGGLTVTA 113
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 39-166 4.47e-06

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 46.71  E-value: 4.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  39 ITDNIYYVGT---------------KGLA--SYLIISGrEAILLDaTLDENVASI-ERNIQSLeFGLRDIKIIINSHAHF 100
Cdd:cd07709    3 IADDIYWVGVndwdlrlfegeyptpRGTSynSYLIKDE-KTALID-TVKEPFFDEfLENLEEV-IDPRKIDYIVVNHQEP 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 816166757 101 DHAAGIGRLKKST-GAEVAAMAGDKSALENgrqegdtDYGGAVFPAVKVDrilnDGDKVTLGDVTLT 166
Cdd:cd07709   80 DHSGSLPELLELApNAKIVCSKKAARFLKH-------FYPGIDERFVVVK----DGDTLDLGKHTLK 135
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
50-195 6.35e-06

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 46.34  E-value: 6.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  50 GLASYLIISGREAILLDA---TLdenvasieRNIQSLEFGLRDIKIIINSHAHFDHAAGIGRLKKSTGA-------EVAA 119
Cdd:COG1234   18 ATSSYLLEAGGERLLIDCgegTQ--------RQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLagrekplTIYG 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 816166757 120 MAGDKSALENGRQEGDTDYGgavFPaVKVdRILNDGDKVTLGDVTLTASLTAgHTKGCTTWSMTSPDrgsvRRVVF 195
Cdd:COG1234   90 PPGTKEFLEALLKASGTDLD---FP-LEF-HEIEPGEVFEIGGFTVTAFPLD-HPVPAYGYRFEEPG----RSLVY 155
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 80-176 9.88e-06

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 46.37  E-value: 9.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  80 IQSLEFGLRDIKIIINSHAHFDHAAGIGRLKKSTGAEVAAMAGDKSalengRQEGdtdyggavfpavkVDRILNDGDKVT 159
Cdd:PLN02398 112 IDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDKD-----RIPG-------------IDIVLKDGDKWM 173

                         90
                 ....*....|....*..
gi 816166757 160 LGDVTLTASLTAGHTKG 176
Cdd:PLN02398 174 FAGHEVLVMETPGHTRG 190
NorV COG0426
Flavorubredoxin [Energy production and conversion];
36-166 1.92e-05

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 45.59  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  36 PFRITDNIYYVGT---------------KGLA--SYLIIsGREAILLDaTLDENVASI-ERNIQSLeFGLRDIKIIINSH 97
Cdd:COG0426    2 AVEIAHGVYWVGVldwdrrlfegeyptpRGTTynSYLIV-DEKTALID-TVGESFFEEfLENLSKV-IDPKKIDYIIVNH 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 816166757  98 AHFDHAAGIGR-LKKSTGAEV--AAMAgdKSALEN--GRQEGDTdyggavfpavkvdRILNDGDKVTLGDVTLT 166
Cdd:COG0426   79 QEPDHSGSLPElLELAPNAKIvcSKKA--ARFLPHfyGIPDFRF-------------IVVKEGDTLDLGGHTLQ 137
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
38-117 4.00e-05

Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440850  Cd Length: 273  Bit Score: 44.10  E-value: 4.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  38 RIT---DNiyYVGTKGLA-----SYLIISGREAILLDaTLDENVasIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGR- 108
Cdd:COG1237    3 KITvlvDN--TAGDEGLLaehglSALIETEGKRILFD-TGQSDV--LLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPAl 77


                 ....*....
gi 816166757 109 LKKSTGAEV 117
Cdd:COG1237   78 LELNPKAPV 86
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 38-109 5.59e-05

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. 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: 293799  Cd Length: 269  Bit Score: 43.76  E-value: 5.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  38 RIT---DNiyYVGTKGLA-----SYLIISGREAILLDATLDEnvaSIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRL 109
Cdd:cd07713    1 KITvlvDN--TAGDEGLLaehglSLLIETEGKKILFDTGQSG---VLLHNAKKLGIDLSDIDAVVLSHGHYDHTGGLKAL 75
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 56-238 9.24e-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: 42.49  E-value: 9.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  56 IISG-REAILLDA--TLD--ENVAS-IERNIQSLefglrdiKIIINSHAHFDHAAGIGRLKK--------STGAEVAAMa 121
Cdd:cd07739   20 LIYGeTEAVLVDAqfTRAdaERLADwIKASGKTL-------TTIYITHGHPDHYFGLEVLLEafpdakvvATPAVVAHI- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 122 gdKSALENGRQEGDTDYGGAVFPAVKVDRILnDGDKVTLGDVTLTAsLTAGHTkgcTTWSMTS---PdrgSVRRVVfpCS 198
Cdd:cd07739   92 --KAQLEPKLAFWGPLLGGNAPARLVVPEPL-DGDTLTLEGHPLEI-VGVGGG---DTDDTTYlwiP---SLKTVV--AG 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 816166757 199 ISVAGNI---LVDNKSyPTIVEDFRRSFGRLASMKADVVLPAH 238
Cdd:cd07739  160 DVVYNGVhvwLADATT-PELRAAWLAALDKIEALNPETVVPGH 201
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 53-184 9.70e-05

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 42.83  E-value: 9.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  53 SYLII--SGREAILLDATLDENVASierniQSLEFGLRdIKIIINSHAHFDHAAGIGRLKKS-TGAEVAAMAGDKSalen 129
Cdd:PLN02469  14 AYLIIdeSTKDAAVVDPVDPEKVLQ-----AAHEHGAK-IKLVLTTHHHWDHAGGNEKIKKLvPGIKVYGGSLDNV---- 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 816166757 130 grqEGDTDYggavfpavkvdriLNDGDKVTLG-DVTLTASLTAGHTKGCTTWSMTS 184
Cdd:PLN02469  84 ---KGCTHP-------------VENGDKLSLGkDVNILALHTPCHTKGHISYYVTG 123
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
47-106 1.55e-04

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 42.64  E-value: 1.55e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 816166757  47 GTKG------LASYLIIS--GREAILLDA-TLdenVASIERNIQSLEFG------LRDIKIIINSHAHFDHAAGI 106
Cdd:COG5212   18 GCSGgisdgnLTTYLLRPlgSDDYVLLDAgTV---VSGLELAEQKGAFKgrqgyvLEHIKGYLISHAHLDHIAGL 89
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 52-109 7.02e-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: 39.75  E-value: 7.02e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 816166757  52 ASYLIISGREAILLDATLD-ENVASIERNIQSLEFGLRDIKIIINSHAHFDHaagIGRL 109
Cdd:cd16295   13 SCYLLETGGKRILLDCGLFqGGKELEELNNEPFPFDPKEIDAVILTHAHLDH---SGRL 68
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 47-167 1.31e-03

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 38.40  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  47 GTKGlASYLIISGREAILLDA-----TLDENVASIERNIQslefglrDIKIIINSHAHFDHAAGIGRLKKSTGAEVAAMA 121
Cdd:cd07733    6 GSKG-NCTYLETEDGKLLIDAglsgrKITGRLAEIGRDPE-------DIDAILVTHEHADHIKGLGVLARKYNVPIYATA 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 816166757 122 GDKSALENGRQEGDTDyggavfpavkVDRILNDGDKVTLGDVTLTA 167
Cdd:cd07733   78 GTLRAMERKVGLIDVD----------QKQIFEPGETFSIGDFDVES 113
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 47-111 2.24e-03

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 39.01  E-value: 2.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 816166757  47 GTKGLASYLIISGREAILLDATLDENvaSIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRLKK 111
Cdd:COG1236   10 GEVTGSCYLLETGGTRILIDCGLFQG--GKERNWPPFPFRPSDVDAVVLTHAHLDHSGALPLLVK 72
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 63-173 2.32e-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: 38.44  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757   63 ILLDATLDEnVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRLKKSTGAEVAAMAGDKSALEngRQEGDTDYGGAV 142
Cdd:pfam12706   3 ILIDPGPDL-RQQALPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLR--RNFPYLFLLEHY 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 816166757  143 FPAVkvdRILNDGDKVTLGDVTLTASLTAGH 173
Cdd:pfam12706  80 GVRV---HEIDWGESFTVGDGGLTVTATPAR 107
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 42-238 3.61e-03

uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YmaE and Nostoc all1228 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. 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: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 37.56  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  42 NIYYVGTK-----GLASYLIISGREAILLDAT--LDENVASIERniqslefgLRDIKIIINSHAhfDHAAGIGRLKKSTG 114
Cdd:cd07727    1 GVYYCGFHseksfGAASYLILRPEGNILVDSPrySPPLAKRIEA--------LGGIRYIFLTHR--DDVADHAKWAERFG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757 115 AEVAAMAGDKSAlengrqegdtdYGGAVFPAVkvdriLNDGDKVTLGDvTLTASLTAGHTKGCTT--WS----------- 181
Cdd:cd07727   71 AKRIIHEDDVNA-----------VTRPDEVIV-----LWGGDPWELDP-DLTLIPVPGHTRGSVVllYKekgvlftgdhl 133

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 816166757 182 MTSPDRGSVrrVVFPcsisvagnilvdnKSYPTIVEDFRRSFGRLASMKADVVLPAH 238
Cdd:cd07727  134 AWSRRRGWL--SAFR-------------YVCWYSWPEQAESVERLADLDFEWVLPGH 175
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 38-111 4.31e-03

Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293860  Cd Length: 212  Bit Score: 37.61  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  38 RITDNIY------------YVGTKGLasyLIISGREAILLDATLDEnvASIERNIQSLEFGLR-DIKIIINSHAHFDHAA 104
Cdd:cd16302    5 KLSDHVYvhvsyletetfgKVPCNGM---IVINGGEAVVFDTPTND--SQSEELIDWIENSLKaKVKAVVPTHFHDDCLG 79


                 ....*..
gi 816166757 105 GIGRLKK 111
Cdd:cd16302   80 GLKAFHR 86
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 50-166 6.91e-03

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 37.14  E-value: 6.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816166757  50 GLASYLIISGREAILLDATLDENVASIERNIQSL--EFGLRDIKIIINSHAHFDHAAGIgrlkkstgAEVAAMAGDKSAL 127
Cdd:COG2333   11 GDAILIRTPDGKTILIDTGPRPSFDAGERVVLPYlrALGIRRLDLLVLTHPDADHIGGL--------AAVLEAFPVGRVL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 816166757 128 ENGRQEGDTDYGGAVFPAVKVD---RILNDGDKVTLGDVTLT 166
Cdd:COG2333   83 VSGPPDTSETYERLLEALKEKGipvRPCRAGDTWQLGGVRFE 124
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 74-110 7.24e-03

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. 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: 293814  Cd Length: 249  Bit Score: 37.24  E-value: 7.24e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 816166757  74 ASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGRLK 110
Cdd:cd07728   80 SSIEESLAELGLTPEDIDYVLMTHLHFDHASGLTKVK 116
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 55-108 7.76e-03

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) 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: 293839  Cd Length: 252  Bit Score: 37.09  E-value: 7.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 816166757  55 LIISGREAILLDATL-------------DENVASIERNIQSLEFGLRDIKIIINSHAHFDHAAGIGR 108
Cdd:cd16281   47 LIETGGRNILIDTGIgdkqdpkfrsiyvQHSEHSLLKSLARLGLSPEDITDVILTHLHFDHCGGATR 113
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 87-113 9.74e-03

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) 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 annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 36.86  E-value: 9.74e-03
                         10        20
                 ....*....|....*....|....*..
gi 816166757  87 LRDIKIIINSHAHFDHAAGIGRLKKST 113
Cdd:cd07730   81 PEDIDAVILSHLHWDHIGGLSDFPNAR 107
 
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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