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Conserved domains on  [gi|612903821|gb|EZV15525|]
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hypothetical protein U926_02636 [Staphylococcus aureus 12S00881]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869982)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme that may have substrate towards phosphotriesters, esters, and/or lactones

CATH:  3.60.15.30|3.60.15.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585|11471246|12177301|11513844
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 2-197 6.08e-78

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: 239.61  E-value: 6.08e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821   2 FFKQFYDNHLSQASYLVGCQRTGEAIIIDPVRD-LSKYIEVADSEGLTITQATETHIHADFASGIRDVAKRLNANIYVSG 80
Cdd:cd07724    1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDsVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  81 EGEDALGYKnmpsktqFVKHGDIIQVGNVKLEVLHTPGHTPESISFLLTDlgggssvPMGLFSGDFIFVGDIGRPDLLek 160
Cdd:cd07724   81 GAPASFFDR-------LLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGD-------PDAVFTGDTLFVGDVGRPDLP-- 144

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 612903821 161 svqikGSTEISAKQMYESVQN-IKNLPDYVQIWPGHGA 197
Cdd:cd07724  145 -----GEAEGLARQLYDSLQRkLLLLPDETLVYPGHDY 177
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 349-438 1.09e-22

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


:

Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 92.34  E-value: 1.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 349 ISTQSVHsADMTGKEEHVLDVRNDEEWNNGHLYQAVNIPYGKLLNENIPFNKEDKIYVHCQSGVRSSIAVGILESKGFEN 428
Cdd:COG0607    6 ISPAELA-ELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAGYTN 84

                         90
                 ....*....|
gi 612903821 429 VVNIREGYQD 438
Cdd:COG0607   85 VYNLAGGIEA 94
 
Name Accession Description Interval E-value
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 2-197 6.08e-78

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: 239.61  E-value: 6.08e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821   2 FFKQFYDNHLSQASYLVGCQRTGEAIIIDPVRD-LSKYIEVADSEGLTITQATETHIHADFASGIRDVAKRLNANIYVSG 80
Cdd:cd07724    1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDsVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  81 EGEDALGYKnmpsktqFVKHGDIIQVGNVKLEVLHTPGHTPESISFLLTDlgggssvPMGLFSGDFIFVGDIGRPDLLek 160
Cdd:cd07724   81 GAPASFFDR-------LLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGD-------PDAVFTGDTLFVGDVGRPDLP-- 144

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 612903821 161 svqikGSTEISAKQMYESVQN-IKNLPDYVQIWPGHGA 197
Cdd:cd07724  145 -----GEAEGLARQLYDSLQRkLLLLPDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 11-197 6.19e-41

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: 145.22  E-value: 6.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  11 LSQASYLVGCqrTGEAIIIDPVRDLS---KYIEVADSEGLTITQATETHIHADFASGIRDVAKRLNANIYVSGEGEDALG 87
Cdd:COG0491   13 LGVNSYLIVG--GDGAVLIDTGLGPAdaeALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  88 YKNMPSK--------TQFVKHGDIIQVGNVKLEVLHTPGHTPESISFLLTDLGggssvpmGLFSGDFIFVGDIGRPDLLE 159
Cdd:COG0491   91 APAAGALfgrepvppDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEK-------VLFTGDALFSGGVGRPDLPD 163

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 612903821 160 KsvqikgsteiSAKQMYESVQNIKNLPDYVqIWPGHGA 197
Cdd:COG0491  164 G----------DLAQWLASLERLLALPPDL-VIPGHGP 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 15-195 8.73e-25

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: 100.32  E-value: 8.73e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821    15 SYLVGCqrTGEAIIIDPV-RDLSKYIEVADSEGL-TITQATETHIHADFASGIRDVAKRLNANIYVSGEGEDAL------ 86
Cdd:smart00849   2 SYLVRD--DGGAILIDTGpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLkdllal 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821    87 -----GYKNMPSKTQFVKHGDIIQVGNVKLEVLHTPGHTPESISFLLTDLGggssvpmGLFSGDFIFVGDIGRPDLleks 161
Cdd:smart00849  80 lgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGK-------ILFTGDLLFAGGDGRTLV---- 148

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 612903821   162 vqikgstEISAKQMYESVQNIKNL--PDYVQIWPGH 195
Cdd:smart00849 149 -------DGGDAAASDALESLLKLlkLLPKLVVPGH 177
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 349-438 1.09e-22

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 92.34  E-value: 1.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 349 ISTQSVHsADMTGKEEHVLDVRNDEEWNNGHLYQAVNIPYGKLLNENIPFNKEDKIYVHCQSGVRSSIAVGILESKGFEN 428
Cdd:COG0607    6 ISPAELA-ELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAGYTN 84

                         90
                 ....*....|
gi 612903821 429 VVNIREGYQD 438
Cdd:COG0607   85 VYNLAGGIEA 94
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 359-437 3.45e-22

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 90.05  E-value: 3.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 359 MTGKEEHVLDVRNDEEWNNGHLYQAVNIPYGKLLNENI--PFNKEDKIYVHCQSGVRSSIAVGILESKGFENVVNIREGY 436
Cdd:cd00158    6 LDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAAllELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLEGGM 85


                 .
gi 612903821 437 Q 437
Cdd:cd00158   86 L 86
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 8-195 4.95e-18

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 83.27  E-value: 4.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821   8 DNHlsqaSYLVGCQRTGEAIIIDPVrDLSKYIEVADSEGLTITQATETHIHADFASGIRDVaKRLNANIYVSGEGEDalg 87
Cdd:PLN02469  11 DNY----AYLIIDESTKDAAVVDPV-DPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKI-KKLVPGIKVYGGSLD--- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  88 ykNMPSKTQFVKHGDIIQVGN-VKLEVLHTPGHTPESISFLLTDLGGGSSvpmGLFSGDFIFVGDIGRpdlleksvqikg 166
Cdd:PLN02469  82 --NVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDP---AVFTGDTLFIAGCGK------------ 144

                        170       180       190
                 ....*....|....*....|....*....|
gi 612903821 167 STEISAKQMYESV-QNIKNLPDYVQIWPGH 195
Cdd:PLN02469 145 FFEGTAEQMYQSLcVTLGSLPKPTQVYCGH 174
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 359-439 3.03e-17

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 76.37  E-value: 3.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  359 MTGKEEHVLDVRNDEEWNNGHLYQAVNIPYGKLLNENIPF----------NKEDKIYVHCQSGVRSSIAVGILESKGFEN 428
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLlellekllelLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|.
gi 612903821  429 VVNIREGYQDF 439
Cdd:pfam00581  81 VYVLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 366-439 1.84e-13

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 65.94  E-value: 1.84e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821   366 VLDVRNDEEWNNGHLYQAVNIPYGKLLNENIPF--------------NKEDKIYVHCQSGVRSSIAVGILESKGFENVVN 431
Cdd:smart00450   7 LLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELdilefeellkrlglDKDKPVVVYCRSGNRSAKAAWLLRELGFKNVYL 86


                   ....*...
gi 612903821   432 IREGYQDF 439
Cdd:smart00450  87 LDGGYKEW 94
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
11-195 1.80e-12

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 65.85  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821   11 LSQASYLVgcQRTGEAIIIDPVRDLSKYIEV----ADSEGLTITQATETHIHADFASGIRDVAKRLNANIYVSGEGEDAL 86
Cdd:pfam00753   4 GQVNSYLI--EGGGGAVLIDTGGSAEAALLLllaaLGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAREL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821   87 GYKNMPSKTQFVKH----------------GDIIQVGNVKLEVLHTPGHTPESISFLLtdlgGGSSVpmgLFSGDFIFVG 150
Cdd:pfam00753  82 LDEELGLAASRLGLpgppvvplppdvvleeGDGILGGGLGLLVTHGPGHGPGHVVVYY----GGGKV---LFTGDLLFAG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 612903821  151 DIGRPDL-LEKSVQIKGSteiSAKQMYESVQNIKNLpDYVQIWPGH 195
Cdd:pfam00753 155 EIGRLDLpLGGLLVLHPS---SAESSLESLLKLAKL-KAAVIVPGH 196
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 347-442 7.52e-09

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 57.19  E-value: 7.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 347 SGISTQSVHSADMTGKEEHV--LDVRNDEEWNNGHLYQAVNIPYGKLLNENIPFNKE--DKIYVHCQSGVRSSIAVGILE 422
Cdd:PRK05597 256 SGGFGEVLDVPRVSALPDGVtlIDVREPSEFAAYSIPGAHNVPLSAIREGANPPSVSagDEVVVYCAAGVRSAQAVAILE 335

                         90       100
                 ....*....|....*....|
gi 612903821 423 SKGFENVVNIREGYQDFPES 442
Cdd:PRK05597 336 RAGYTGMSSLDGGIEGWLDS 355
 
Name Accession Description Interval E-value
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 2-197 6.08e-78

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: 239.61  E-value: 6.08e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821   2 FFKQFYDNHLSQASYLVGCQRTGEAIIIDPVRD-LSKYIEVADSEGLTITQATETHIHADFASGIRDVAKRLNANIYVSG 80
Cdd:cd07724    1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDsVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  81 EGEDALGYKnmpsktqFVKHGDIIQVGNVKLEVLHTPGHTPESISFLLTDlgggssvPMGLFSGDFIFVGDIGRPDLLek 160
Cdd:cd07724   81 GAPASFFDR-------LLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGD-------PDAVFTGDTLFVGDVGRPDLP-- 144

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 612903821 161 svqikGSTEISAKQMYESVQN-IKNLPDYVQIWPGHGA 197
Cdd:cd07724  145 -----GEAEGLARQLYDSLQRkLLLLPDETLVYPGHDY 177
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 15-195 1.77e-41

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: 144.91  E-value: 1.77e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  15 SYLVGCQRTGEAIIIDPVrDLSKYIEVADSEGLTITQATETHIHADFASGIRDVAKRL-NANIYVSGEGedalgykNMPS 93
Cdd:cd07723   11 IYLIVDEATGEAAVVDPG-EAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFpDAPVYGPAED-------RIPG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  94 KTQFVKHGDIIQVGNVKLEVLHTPGHTPESISFLLTDLGggssvpmGLFSGDFIFVGDIGRPDlleksvqikgstEISAK 173
Cdd:cd07723   83 LDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEP-------ALFTGDTLFSGGCGRFF------------EGTAE 143

                        170       180
                 ....*....|....*....|..
gi 612903821 174 QMYESVQNIKNLPDYVQIWPGH 195
Cdd:cd07723  144 QMYASLQKLLALPDDTLVYCGH 165
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 11-197 6.19e-41

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: 145.22  E-value: 6.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  11 LSQASYLVGCqrTGEAIIIDPVRDLS---KYIEVADSEGLTITQATETHIHADFASGIRDVAKRLNANIYVSGEGEDALG 87
Cdd:COG0491   13 LGVNSYLIVG--GDGAVLIDTGLGPAdaeALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  88 YKNMPSK--------TQFVKHGDIIQVGNVKLEVLHTPGHTPESISFLLTDLGggssvpmGLFSGDFIFVGDIGRPDLLE 159
Cdd:COG0491   91 APAAGALfgrepvppDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEK-------VLFTGDALFSGGVGRPDLPD 163

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 612903821 160 KsvqikgsteiSAKQMYESVQNIKNLPDYVqIWPGHGA 197
Cdd:COG0491  164 G----------DLAQWLASLERLLALPPDL-VIPGHGP 190
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 3-195 5.92e-38

Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. 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: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 135.74  E-value: 5.92e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821   3 FKQFYDNHlsqaSYLVGCQRTGEAIIIDPVRDLSKYIEVADSEGLTITQATETHIHADFASGIRDVAKRLNANIYVSgeG 82
Cdd:cd16275    6 KAGPMINY----SYIIIDKATREAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMS--K 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  83 EDALGYKNMPSKTQFVKHGDIIQVGNVKLEVLHTPGHTPESISFLLtdlgGGSsvpmgLFSGDFIFVGDIGRPDLleksv 162
Cdd:cd16275   80 EEIDYYGFRCPNLIPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLL----GDS-----LFTGDTLFIEGCGRCDL----- 145

                        170       180       190
                 ....*....|....*....|....*....|....
gi 612903821 163 qiKGSteiSAKQMYESVQNIKNL-PDYVQIWPGH 195
Cdd:cd16275  146 --PGG---DPEEMYESLQRLKKLpPPNTRVYPGH 174
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 16-220 2.01e-32

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: 122.07  E-value: 2.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  16 YLVGCQRTGEAIIIDPVRDLSKYIEVADSEGLTITQATETHIHADFASGIRDVAKRLNANIYV---------SGEGEDAL 86
Cdd:cd16322   14 YLVADEGGGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLhpddlplyeAADLGAKA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  87 GYKNM---PSKTQFVKHGDIIQVGNVKLEVLHTPGHTPESISFLLTDLGggssvpmGLFSGDFIFVGDIGRPDLleksvq 163
Cdd:cd16322   94 FGLGIeplPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEG-------LLFSGDLLFQGSIGRTDL------ 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 612903821 164 iKGSTEisaKQMYESVQNIKNLPDYVQIWPGHGagspcgkalgaiPISTIGYEKINN 220
Cdd:cd16322  161 -PGGDP---KAMAASLRRLLTLPDETRVFPGHG------------PPTTLGEERRTN 201
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 4-195 6.45e-30

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: 114.69  E-value: 6.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821   4 KQFYDNHLSQASYLVGCqRTGEAIIIDP-VRDLSKYIEVADSEGLTITQATETHIHADFASGIRDVAKRLNANIYVSGEG 82
Cdd:cd06262    1 KRLPVGPLQTNCYLVSD-EEGEAILIDPgAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  83 EDAL------------GYKNMPSKTQFVKHGDIIQVGNVKLEVLHTPGHTPESISFLLTDLGggssvpmGLFSGDFIFVG 150
Cdd:cd06262   80 AELLedpelnlaffggGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEG-------VLFTGDTLFAG 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 612903821 151 DIGRPDLleksvqiKGSteiSAKQMYESVQN-IKNLPDYVQIWPGH 195
Cdd:cd06262  153 SIGRTDL-------PGG---DPEQLIESIKKlLLLLPDDTVVYPGH 188
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 13-195 2.82e-28

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: 110.34  E-value: 2.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  13 QASYLVGCQRTGEAIIIDPVRDLSKYIEVADSEGLTITQATETHIHADFASGIRDVAKRLNANIYVSGEgEDALGYKNMP 92
Cdd:cd07737   11 QNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHK-EDKFLLENLP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  93 SK--------------TQFVKHGDIIQVGNVKLEVLHTPGHTPESISFLltdlgggsSVPMGL-FSGDFIFVGDIGRPDL 157
Cdd:cd07737   90 EQsqmfgfppaeaftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFF--------NRESKLaIVGDVLFKGSIGRTDF 161

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 612903821 158 LeksvqiKGSTEisakQMYESVQN-IKNLPDYVQIWPGH 195
Cdd:cd07737  162 P------GGNHA----QLIASIKEkLLPLGDDVTFIPGH 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 15-195 8.73e-25

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: 100.32  E-value: 8.73e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821    15 SYLVGCqrTGEAIIIDPV-RDLSKYIEVADSEGL-TITQATETHIHADFASGIRDVAKRLNANIYVSGEGEDAL------ 86
Cdd:smart00849   2 SYLVRD--DGGAILIDTGpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLkdllal 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821    87 -----GYKNMPSKTQFVKHGDIIQVGNVKLEVLHTPGHTPESISFLLTDLGggssvpmGLFSGDFIFVGDIGRPDLleks 161
Cdd:smart00849  80 lgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGK-------ILFTGDLLFAGGDGRTLV---- 148

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 612903821   162 vqikgstEISAKQMYESVQNIKNL--PDYVQIWPGH 195
Cdd:smart00849 149 -------DGGDAAASDALESLLKLlkLLPKLVVPGH 177
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 349-438 1.09e-22

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 92.34  E-value: 1.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 349 ISTQSVHsADMTGKEEHVLDVRNDEEWNNGHLYQAVNIPYGKLLNENIPFNKEDKIYVHCQSGVRSSIAVGILESKGFEN 428
Cdd:COG0607    6 ISPAELA-ELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAGYTN 84

                         90
                 ....*....|
gi 612903821 429 VVNIREGYQD 438
Cdd:COG0607   85 VYNLAGGIEA 94
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 359-437 3.45e-22

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 90.05  E-value: 3.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 359 MTGKEEHVLDVRNDEEWNNGHLYQAVNIPYGKLLNENI--PFNKEDKIYVHCQSGVRSSIAVGILESKGFENVVNIREGY 436
Cdd:cd00158    6 LDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAAllELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLEGGM 85


                 .
gi 612903821 437 Q 437
Cdd:cd00158   86 L 86
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 15-197 7.03e-19

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 84.08  E-value: 7.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  15 SYLVGcqRTGEAIIIDPVRDLSKYIE--VADSEGLTITQATETHIHADFASGIRDVAKRLNANIYVSGEGEDALGYKNMP 92
Cdd:cd16278   20 TYLLG--APDGVVVIDPGPDDPAHLDalLAALGGGRVSAILVTHTHRDHSPGAARLAERTGAPVRAFGPHRAGGQDTDFA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  93 SkTQFVKHGDIIQVGNVKLEVLHTPGHTPESISFLLTDLGggssvpmGLFSGDFIFvgdiGRpdlleksvqikGSTEISA 172
Cdd:cd16278   98 P-DRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEG-------ALFTGDHVM----GW-----------STTVIAP 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 612903821 173 -----KQMYESVQNIKNLPDyVQIWPGHGA 197
Cdd:cd16278  155 pdgdlGDYLASLERLLALDD-RLLLPGHGP 183
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 8-195 4.95e-18

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 83.27  E-value: 4.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821   8 DNHlsqaSYLVGCQRTGEAIIIDPVrDLSKYIEVADSEGLTITQATETHIHADFASGIRDVaKRLNANIYVSGEGEDalg 87
Cdd:PLN02469  11 DNY----AYLIIDESTKDAAVVDPV-DPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKI-KKLVPGIKVYGGSLD--- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  88 ykNMPSKTQFVKHGDIIQVGN-VKLEVLHTPGHTPESISFLLTDLGGGSSvpmGLFSGDFIFVGDIGRpdlleksvqikg 166
Cdd:PLN02469  82 --NVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDP---AVFTGDTLFIAGCGK------------ 144

                        170       180       190
                 ....*....|....*....|....*....|
gi 612903821 167 STEISAKQMYESV-QNIKNLPDYVQIWPGH 195
Cdd:PLN02469 145 FFEGTAEQMYQSLcVTLGSLPKPTQVYCGH 174
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 359-439 3.03e-17

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 76.37  E-value: 3.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  359 MTGKEEHVLDVRNDEEWNNGHLYQAVNIPYGKLLNENIPF----------NKEDKIYVHCQSGVRSSIAVGILESKGFEN 428
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLlellekllelLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|.
gi 612903821  429 VVNIREGYQDF 439
Cdd:pfam00581  81 VYVLDGGFEAW 91
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 25-195 2.14e-16

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: 76.90  E-value: 2.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  25 EAIIID---PVRDLSKYIEvadseglTITQ----ATETHIHADFASGIRDVAKR---------LNANIYVSGEGEDALGY 88
Cdd:cd07712   19 RALLIDtglGIGDLKEYVR-------TLTDlpllVVATHGHFDHIGGLHEFEEVyvhpadaeiLAAPDNFETLTWDAATY 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  89 KNMPS-KTQFVKHGDIIQVGNVKLEVLHTPGHTPESISFLLTDLGggssvpmGLFSGDFIFVGDIgrpdlleksVQIKGS 167
Cdd:cd07712   92 SVPPAgPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANR-------LLFSGDVVYDGPL---------IMDLPH 155

                        170       180
                 ....*....|....*....|....*....
gi 612903821 168 TEISakQMYESVQNIKNLPDYV-QIWPGH 195
Cdd:cd07712  156 SDLD--DYLASLEKLSKLPDEFdKVLPGH 182
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 1-195 4.26e-16

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 77.53  E-value: 4.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821   1 MFFKQFYDNHLSQASYLVGCQRTGE--AIIIDPV-----RDLSKYIEVadseGLTITQATETHIHADFASGIRDVAKRLN 73
Cdd:PLN02962  11 LLFRQLFEKESSTYTYLLADVSHPDkpALLIDPVdktvdRDLSLVKEL----GLKLIYAMNTHVHADHVTGTGLLKTKLP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  74 aniyvsgegedalGYKNMPSKTQ------FVKHGDIIQVGNVKLEVLHTPGHTPESISFLLTDlGGGSSVPMGLFSGDFI 147
Cdd:PLN02962  87 -------------GVKSIISKASgskadlFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGE-GPDQPQPRMAFTGDAL 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 612903821 148 FVGDIGRPDLLEKsvqikgsteiSAKQMYESVQN-IKNLPDYVQIWPGH 195
Cdd:PLN02962 153 LIRGCGRTDFQGG----------SSDQLYKSVHSqIFTLPKDTLIYPAH 191
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 15-197 1.54e-14

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: 71.80  E-value: 1.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  15 SYLVGCQR------TGEAIiiDPVRDLSKyiEVADSEGL-TITQATETHIHADFASGIRDVAKRLNAN---IYVSGEGED 84
Cdd:cd07722   20 TYLVGTGKrrilidTGEGR--PSYIPLLK--SVLDSEGNaTISDILLTHWHHDHVGGLPDVLDLLRGPsprVYKFPRPEE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  85 ALGYKNMPSKTQFVKHGDIIQVGNVKLEVLHTPGHTPESISFLLTDLGggssvpmGLFSGDFIfvgdIGrpdlleksvqi 164
Cdd:cd07722   96 DEDPDEDGGDIHDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEEN-------ALFTGDCV----LG----------- 153

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 612903821 165 KGSTEIS--AKQMyESVQNIKNLPdYVQIWPGHGA 197
Cdd:cd07722  154 HGTAVFEdlAAYM-ASLKKLLSLG-PGRIYPGHGP 186
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 366-439 1.84e-13

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 65.94  E-value: 1.84e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821   366 VLDVRNDEEWNNGHLYQAVNIPYGKLLNENIPF--------------NKEDKIYVHCQSGVRSSIAVGILESKGFENVVN 431
Cdd:smart00450   7 LLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELdilefeellkrlglDKDKPVVVYCRSGNRSAKAAWLLRELGFKNVYL 86


                   ....*...
gi 612903821   432 IREGYQDF 439
Cdd:smart00450  87 LDGGYKEW 94
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 14-195 5.12e-13

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: 67.90  E-value: 5.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  14 ASYLVgcQRTGEAIIIDP-VRDLSKYIEVA-DSEGLTITQATE---THIHADFASGIRDVAKRL-NANIYV--------- 78
Cdd:cd07726   17 ASYLL--DGEGRPALIDTgPSSSVPRLLAAlEALGIAPEDVDYiilTHIHLDHAGGAGLLAEALpNAKVYVhprgarhli 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  79 ------------SGEGEDALGYKNMP---SKTQFVKHGDIIQVGNVKLEVLHTPGHTPESISFLLTDLGggssvpmGLFS 143
Cdd:cd07726   95 dpsklwasaravYGDEADRLGGEILPvpeERVIVLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESD-------GLFT 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 612903821 144 GDfifVGDIGRPDLlekSVQIKGST---EISAKQMYESVQNIKNL-PDYvqIWPGH 195
Cdd:cd07726  168 GD---AAGVRYPEL---DVVGPPSTpppDFDPEAWLESLDRLLSLkPER--IYLTH 215
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 352-436 7.87e-13

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.


Pssm-ID: 238782 [Multi-domain]  Cd Length: 90  Bit Score: 63.82  E-value: 7.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 352 QSVHSADMTGKEEHVLDVRNDEEWNNGHLYQAVNIPYGKL---LNEnIPFNKEdkIYVHCQSGVRSSIAVGILESKGFeN 428
Cdd:cd01524    2 QWHELDNYRADGVTLIDVRTPQEFEKGHIKGAINIPLDELrdrLNE-LPKDKE--IIVYCAVGLRGYIAARILTQNGF-K 77


                 ....*...
gi 612903821 429 VVNIREGY 436
Cdd:cd01524   78 VKNLDGGY 85
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
11-195 1.80e-12

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 65.85  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821   11 LSQASYLVgcQRTGEAIIIDPVRDLSKYIEV----ADSEGLTITQATETHIHADFASGIRDVAKRLNANIYVSGEGEDAL 86
Cdd:pfam00753   4 GQVNSYLI--EGGGGAVLIDTGGSAEAALLLllaaLGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAREL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821   87 GYKNMPSKTQFVKH----------------GDIIQVGNVKLEVLHTPGHTPESISFLLtdlgGGSSVpmgLFSGDFIFVG 150
Cdd:pfam00753  82 LDEELGLAASRLGLpgppvvplppdvvleeGDGILGGGLGLLVTHGPGHGPGHVVVYY----GGGKV---LFTGDLLFAG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 612903821  151 DIGRPDL-LEKSVQIKGSteiSAKQMYESVQNIKNLpDYVQIWPGH 195
Cdd:pfam00753 155 EIGRLDLpLGGLLVLHPS---SAESSLESLLKLAKL-KAAVIVPGH 196
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 55-196 4.86e-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: 61.55  E-value: 4.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  55 THIHADFASGIRDVAKRLNANIYVSGegedalgyknmpskTQFVKHGDIIQVGNVKLEVLHTPGHTPESISFLLTDLGgg 134
Cdd:cd07725   62 THHHPDHIGLAGKLQEKSGATVYILD--------------VTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRR-- 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612903821 135 ssvpmGLFSGDFIfVGDI-----GRPDLLEKSVqikgsteisaKQMYESVQNIKNLpDYVQIWPGHG 196
Cdd:cd07725  126 -----ELFVGDAV-LPKItpnvsLWAVRVEDPL----------GAYLESLDKLEKL-DVDLAYPGHG 175
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 55-196 2.21e-09

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: 56.85  E-value: 2.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  55 THIHADFASGIRDVAKRLNANIYVSG------EGEDALGY---------------KNMPSKTQFVKHGDIIQVGnVKLEV 113
Cdd:cd07721   56 THGHIDHIGSLAALKEAPGAPVYAHEreapylEGEKPYPPpvrlgllgllspllpVKPVPVDRTLEDGDTLDLA-GGLRV 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 114 LHTPGHTPESISFLLTDLGggssVpmgLFSGDFIFVGDigrpdlleksvqikGSTEISAK-------QMYESVQNIKNLp 186
Cdd:cd07721  135 IHTPGHTPGHISLYLEEDG----V---LIAGDALVTVG--------------GELVPPPPpftwdmeEALESLRKLAEL- 192

                        170
                 ....*....|
gi 612903821 187 DYVQIWPGHG 196
Cdd:cd07721  193 DPEVLAPGHG 202
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 8-195 2.85e-09

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 58.32  E-value: 2.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821   8 DNHlsqaSYLVGCQRTGEAIIIDPvRDLSKYIEVADSEGLTITQATETHIHADFASGIRDVAKRLNANIYVSGEGEDalg 87
Cdd:PLN02398  86 DNY----AYLLHDEDTGTVGVVDP-SEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDKD--- 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  88 ykNMPSKTQFVKHGDIIQVGNVKLEVLHTPGHTPESISFLLTdlGGGSsvpmgLFSGDFIFVGDIGRpdLLEksvqikGS 167
Cdd:PLN02398 158 --RIPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFP--GSGA-----IFTGDTLFSLSCGK--LFE------GT 220

                        170       180
                 ....*....|....*....|....*...
gi 612903821 168 TEisakQMYESVQNIKNLPDYVQIWPGH 195
Cdd:PLN02398 221 PE----QMLSSLQKIISLPDDTNIYCGH 244
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 345-436 2.89e-09

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 54.62  E-value: 2.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 345 PKSGISTQSVHSADMTGKEEHVLDVRNDEEWNNGHLYQAVNIPYGKLLN----------ENIPFNKEDKIYVHCQSGVRS 414
Cdd:cd01526    6 PEERVSVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSkaaelkslqeLPLDNDKDSPIYVVCRRGNDS 85

                         90       100
                 ....*....|....*....|...
gi 612903821 415 SIAVGILESKGFE-NVVNIREGY 436
Cdd:cd01526   86 QTAVRKLKELGLErFVRDIIGGL 108
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 347-442 7.52e-09

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 57.19  E-value: 7.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 347 SGISTQSVHSADMTGKEEHV--LDVRNDEEWNNGHLYQAVNIPYGKLLNENIPFNKE--DKIYVHCQSGVRSSIAVGILE 422
Cdd:PRK05597 256 SGGFGEVLDVPRVSALPDGVtlIDVREPSEFAAYSIPGAHNVPLSAIREGANPPSVSagDEVVVYCAAGVRSAQAVAILE 335

                         90       100
                 ....*....|....*....|
gi 612903821 423 SKGFENVVNIREGYQDFPES 442
Cdd:PRK05597 336 RAGYTGMSSLDGGIEGWLDS 355
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 367-435 2.06e-08

Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes uncharacterized putative rhodanese-related domains.


Pssm-ID: 238786 [Multi-domain]  Cd Length: 101  Bit Score: 51.63  E-value: 2.06e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612903821 367 LDVRNDEEWNNGHLYQAVNIP---YGKLLNENIPFNKEDKIYVHCQSGVRSSIAVGILESKGFENVVNIREG 435
Cdd:cd01528   21 IDVREPEELEIAFLPGFLHLPmseIPERSKELDSDNPDKDIVVLCHHGGRSMQVAQWLLRQGFENVYNLQGG 92
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 368-431 2.17e-08

Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein 67B2 of Drosophila melanogaster and other similar proteins, many of which are uncharacterized.


Pssm-ID: 238777 [Multi-domain]  Cd Length: 106  Bit Score: 51.89  E-value: 2.17e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612903821 368 DVRNDEEWNNGHLYQAVNIPYGKLLNE-NIP-------FN-----KEDKIYVHCQSGVRSSIAVGILESKGFENVVN 431
Cdd:cd01519   20 DVREPEELKTGKIPGAINIPLSSLPDAlALSeeefekkYGfpkpsKDKELIFYCKAGVRSKAAAELARSLGYENVGN 96
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 55-129 4.34e-08

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: 54.01  E-value: 4.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  55 THIHADFASGIRDVAKRLNANIYVSGEGEDAL-------------GYKNMPSKT-QFVKHGDIIQVGNVKLEVLHTPGHT 120
Cdd:cd16308   67 TQAHYDHVGAMAAIKQQTGAKMMVDEKDAKVLadggksdyemggyGSTFAPVKAdKLLHDGDTIKLGGTKLTLLHHPGHT 146


                 ....*....
gi 612903821 121 PESISFLLT 129
Cdd:cd16308  147 KGSCSFLFD 155
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 366-431 5.49e-08

3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 53.64  E-value: 5.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 366 VLDVRNDEEWN---------NGHLYQAVNIPYGKLLNENIPF---------------NKEDKIYVHCQSGVRSSIAVGIL 421
Cdd:COG2897  156 LVDARSPERYRgevepidprAGHIPGAVNLPWTDLLDEDGTFksaeelralfaalgiDPDKPVITYCGSGVRAAHTWLAL 235

                         90
                 ....*....|
gi 612903821 422 ESKGFENVVN 431
Cdd:COG2897  236 ELLGYPNVRL 245
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 55-165 6.57e-08

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: 53.32  E-value: 6.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  55 THIHADFASGIRDVAKRLN-ANIYVSGEGEDALGYKNMPS-------KTQFVKHGDIIQVGNVKLEVLHTPGHTPE---- 122
Cdd:COG2333   59 THPDADHIGGLAAVLEAFPvGRVLVSGPPDTSETYERLLEalkekgiPVRPCRAGDTWQLGGVRFEVLWPPEDLLEgsde 138

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 612903821 123 ---SISFLLTDlGGGSsvpmglfsgdFIFVGDIGRP---DLLEKSVQIK 165
Cdd:COG2333  139 nnnSLVLRLTY-GGFS----------FLLTGDAEAEaeaALLARGPDLK 176
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 55-195 7.17e-08

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 53.29  E-value: 7.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  55 THIHADFASGIRDVAKRL-NANIYVSGEGEDAlgyknmpSKTQFVKHGDIIQVGNVKLEVLHTPGHTPESISFLltdlgg 133
Cdd:PRK10241  52 THHHHDHVGGVKELVEKFpQIVVYGPQETQDK-------GTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF------ 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612903821 134 gsSVPMgLFSGDFIFVGDIGRpdLLEKSvqikgsteisAKQMYESVQNIKNLPDYVQIWPGH 195
Cdd:PRK10241 119 --SKPY-LFCGDTLFSGGCGR--LFEGT----------ASQMYQSLKKINALPDDTLICCAH 165
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
366-437 1.29e-07

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 53.48  E-value: 1.29e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612903821 366 VLDVRNDEEWNNGHLYQAVNIPYGKL---LNENIPfNKEDKIYVHCQSGVRSSIAVGILESKGFENVVNIREGYQ 437
Cdd:PRK08762  20 LIDVREAHERASGQAEGALRIPRGFLelrIETHLP-DRDREIVLICASGTRSAHAAATLRELGYTRVASVAGGFS 93
PLN02160 PLN02160
thiosulfate sulfurtransferase
 367-436 2.45e-07

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 49.70  E-value: 2.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 367 LDVRNDEEWNNGHLYQA--VNIPY------GKLLNENIP------FNKEDKIYVHCQSGVRSSIAVGILESKGFENVVNI 432
Cdd:PLN02160  33 LDVRTQDEFRRGHCEAAkiVNIPYmlntpqGRVKNQEFLeqvsslLNPADDILVGCQSGARSLKATTELVAAGYKKVRNK 112


                 ....
gi 612903821 433 REGY 436
Cdd:PLN02160 113 GGGY 116
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 55-127 3.96e-07

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: 51.05  E-value: 3.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  55 THIHADFASGIRDVAKRLNANIYVSGEGEDAL----------GYKNMPSKTQFVKHGDIIQVGNVKLEVLHTPGHTPESI 124
Cdd:cd16280   68 THGHGDHYGGAAYLKDLYGAKVVMSEADWDMMeeppeegdnpRWGPPPERDIVIKDGDTLTLGDTTITVYLTPGHTPGTL 147


                 ...
gi 612903821 125 SFL 127
Cdd:cd16280  148 SLI 150
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 362-431 4.34e-07

Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the second repeat. Only the second repeat contains the catalytically active Cys residue.


Pssm-ID: 238726 [Multi-domain]  Cd Length: 118  Bit Score: 48.40  E-value: 4.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 362 KEEHVLDVRNDEEWN-----------NGHLYQAVNIPYGKLLNEN---------------IPFNKEDKIYVHCQSGVRSS 415
Cdd:cd01449   13 GDVQLVDARSPERFRgevpeprpglrSGHIPGAVNIPWTSLLDEDgtfkspeelralfaaLGITPDKPVIVYCGSGVTAC 92

                         90
                 ....*....|....*.
gi 612903821 416 IAVGILESKGFENVVN 431
Cdd:cd01449   93 VLLLALELLGYKNVRL 108
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 366-441 4.81e-07

Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as a polysulfide binding and transferase domain in anaerobic gram-negative bacteria, functioning in oxidative phosphorylation with polysulfide-sulfur as a terminal electron acceptor. The active site contains the same conserved cysteine that is the catalytic residue in other Rhodanese Homology Domain proteins.


Pssm-ID: 238724 [Multi-domain]  Cd Length: 103  Bit Score: 47.81  E-value: 4.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 366 VLDVRN-DEEWNNGHLYQAVNIPYGKL---LNENIPFNK----EDKIYV-HCQSGVRSSIAVGILESKGFENVVNIREGY 436
Cdd:cd01447   17 LVDVRDpRELERTGMIPGAFHAPRGMLefwADPDSPYHKpafaEDKPFVfYCASGWRSALAGKTLQDMGLKPVYNIEGGF 96


                 ....*
gi 612903821 437 QDFPE 441
Cdd:cd01447   97 KDWKE 101
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 360-435 7.61e-07

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 50.86  E-value: 7.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 360 TGKEEHVLDVRNDEEWNNGHLYQAVNIPYGKLLN----ENIPFNKedKIYVHCQSGVRSSIAVGILESKGFENVVNIREG 435
Cdd:PRK07878 300 SGKKIALIDVREPVEWDIVHIPGAQLIPKSEILSgealAKLPQDR--TIVLYCKTGVRSAEALAALKKAGFSDAVHLQGG 377
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 55-159 1.37e-06

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: 49.47  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  55 THIHADFASGIRDVAKRLNANIYVSGEGEDAL--GYKNMP-------------SKTQFVKHGDIIQVGNVKLEVLHTPGH 119
Cdd:cd07708   67 SHAHFDHAGGSAEIKKQTGAKVMAGAEDVSLLlsGGSSDFhyandsstyfpqsTVDRAVHDGERVTLGGTVLTAHATPGH 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 612903821 120 TPESISFLLTDLGGGSSVPMGLF-----SGDFIFVGDIGRPDLLE 159
Cdd:cd07708  147 TPGCTTWTMTLKDHGKQYQVVFAdsltvNPGYRLVDNPTYPKIVE 191
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 349-435 1.86e-06

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, Bacillus subtilis YbfQ, and similar uncharacterized proteins.


Pssm-ID: 238776 [Multi-domain]  Cd Length: 101  Bit Score: 46.03  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 349 ISTQSVHsADMTGKEEHVLDVRNDEEWNNGHLYQAVNIPYGKL------LNENIPFNKEDKIYVHCQSGVRSSIAVGILE 422
Cdd:cd01518    4 LSPAEWN-ELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFrefpfwLDENLDLLKGKKVLMYCTGGIRCEKASAYLK 82

                         90
                 ....*....|...
gi 612903821 423 SKGFENVVNIREG 435
Cdd:cd01518   83 ERGFKNVYQLKGG 95
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 367-437 2.71e-06

Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative rhodanese-related sulfurtransferases of several uncharacterized proteins.


Pssm-ID: 238780 [Multi-domain]  Cd Length: 117  Bit Score: 46.17  E-value: 2.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 367 LDVRNDEEWNN-GHLYQAVNIPYGKLLNENIPFN----------KEDKIYVHCQSGVRSSIAVGILESKGFENVVNIREG 435
Cdd:cd01522   19 VDVRTEAEWKFvGGVPDAVHVAWQVYPDMEINPNflaeleekvgKDRPVLLLCRSGNRSIAAAEAAAQAGFTNVYNVLEG 98


                 ..
gi 612903821 436 YQ 437
Cdd:cd01522   99 FE 100
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 55-145 3.58e-06

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. 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: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 47.13  E-value: 3.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  55 THIHADFASGIRDVAKRLN-ANIYVSGEGEDALGYKNMPS-------KTQFVKHGDIIQVGNVKLEVLHTPGHTPE---- 122
Cdd:cd07731   55 THPDADHIGGLDAVLKNFPvKEVYMPGVTHTTKTYEDLLDaikekgiPVTPCKAGDRWQLGGVSFEVLSPPKDDYDdlnn 134

                         90       100
                 ....*....|....*....|....
gi 612903821 123 -SISFLLTDlgGGSSVpmgLFSGD 145
Cdd:cd07731  135 nSCVLRLTY--GGTSF---LLTGD 153
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 ...
 55-125 5.86e-06

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: 47.73  E-value: 5.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  55 THIHADFASGIRDVAKRLNANIYVSGEGEDAL-GYKNMPSKTQF--------------VKHGDIIQVGNVKLEVLHTPGH 119
Cdd:cd16290   67 SHAHFDHAGGIAALQRDSGATVAASPAGAAALrSGGVDPDDPQAgaadpfppvakvrvVADGEVVKLGPLAVTAHATPGH 146


                 ....*.
gi 612903821 120 TPESIS 125
Cdd:cd16290  147 TPGGTS 152
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 55-157 9.50e-06

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: 46.90  E-value: 9.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  55 THIHADFASGIRDVAKRLNANIYVSGE----------GEDALGYKNMP-------SKTQFVKHGDIIQVGNVKLEVLHTP 117
Cdd:cd16312   67 SHAHWDHAGGIAALQKASGATVAASAHgaqvlqsgtnGKDDPQYQAKPvvhvakvAKVKEVGEGDTLKVGPLRLTAHMTP 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 612903821 118 GHTPESISFLLTDLGGGSSVPM-------GLFSGDFIFVGDIGRPDL 157
Cdd:cd16312  147 GHTPGGTTWTWTSCEGQRCLDVvyadslnPYSSGDFYYTGKGGYPDI 193
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 55-159 1.13e-05

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: 46.55  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  55 THIHADFASGIRDVAKRLNANIYVS----------GEGEDALGYKNM---PSKT-QFVKHGDIIQVGNVKLEVLHTPGHT 120
Cdd:cd16288   67 SHAHLDHAGGLAALKKLTGAKLMASaedaallasgGKSDFHYGDDSLafpPVKVdRVLKDGDRVTLGGTTLTAHLTPGHT 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 612903821 121 PESISFLLTDLGGGSS-----VPMGLFSGDFIFVGDIGRPDLLE 159
Cdd:cd16288  147 RGCTTWTMTVKDDGKVyqvvfADSLTVNPGYKLVGNPTYPGIAE 190
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 364-431 1.20e-05

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 44.07  E-value: 1.20e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612903821 364 EHVLDVRNDEEWNNGHLYQAVNIPYGKL---LNENIPfNKEDKIYVHCQSGVRSSIAVGILESKGFENVVN 431
Cdd:PRK10287  21 EHWIDVRVPEQYQQEHVQGAINIPLKEVkerIATAVP-DKNDTVKLYCNAGRQSGQAKEILSEMGYTHAEN 90
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 24-160 1.46e-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: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 45.60  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  24 GEAIIIDP------VRDLSKYIEvadSEGLTITQATETHIHADFASGIRDVAKRLNANIYVSgEGEDAL----------- 86
Cdd:cd07743   18 KEALLIDSgldedaGRKIRKILE---ELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAP-KIEKAFienpllepsyl 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  87 ----GYKNM--------PSKTQFVKHGDIIQVGNVKLEVLHTPGHTPESISFlLTDLGggssVpmgLFSGDFIFvgdigR 154
Cdd:cd07743   94 ggayPPKELrnkflmakPSKVDDIIEEGELELGGVGLEIIPLPGHSFGQIGI-LTPDG----V---LFAGDALF-----G 160


                 ....*.
gi 612903821 155 PDLLEK 160
Cdd:cd07743  161 EEVLEK 166
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 27-197 1.90e-05

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 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: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 45.27  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  27 IIIDP--VRDLSKYIEVADSEGLTITQATE---THIHADFASGIRDVAkrlNANIYVsgeGEDALGYKNMPSktqfvkhg 101
Cdd:cd07711   34 ILVDTgtPWDRDLLLKALAEHGLSPEDIDYvvlTHGHPDHIGNLNLFP---NATVIV---GWDICGDSYDDH-------- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 102 DIIQVGNVKL----EVLHTPGHTPESISFLLTDlgggssVPMGLfsgdFIFVGDI--GRPDLLEKSVQIKGSTEIsaKQM 175
Cdd:cd07711  100 SLEEGDGYEIdenvEVIPTPGHTPEDVSVLVET------EKKGT----VAVAGDLfeREEDLEDPILWDPLSEDP--ELQ 167

                        170       180
                 ....*....|....*....|..
gi 612903821 176 YESVQNIKNLPDYvqIWPGHGA 197
Cdd:cd07711  168 EESRKRILALADW--IIPGHGP 187
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 55-195 2.97e-05

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: 45.28  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  55 THIHADFASGIRDVAkrlNANIYVS---------GEGEDALGYKNMPSKTQFVKHGDIIQV-GNVKL----EVLHTPGHT 120
Cdd:cd07729   95 SHLHFDHAGGLDLFP---NATIIVQraeleyatgPDPLAAGYYEDVLALDDDLPGGRVRLVdGDYDLfpgvTLIPTPGHT 171

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612903821 121 PESISFLLtDLGGGSsvpmglfsgdFIFVGDIG--RPDLLEKSVQIKGSTEISAKQMYESVQNIKNLPDyVQIWPGH 195
Cdd:cd07729  172 PGHQSVLV-RLPEGT----------VLLAGDAAytYENLEEGRPPGINYDPEAALASLERLKALAEREG-ARVIPGH 236
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 15-146 6.38e-05

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: 44.02  E-value: 6.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  15 SYLVgcqRTGEAIIIDPVRD---------LSKYIEVADSEGLTITqatetHIHADFASGIRDVAKRL-NANIYVSGEGED 84
Cdd:cd07709   34 SYLI---KDEKTALIDTVKEpffdeflenLEEVIDPRKIDYIVVN-----HQEPDHSGSLPELLELApNAKIVCSKKAAR 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612903821  85 ALG--YKNMPSKTQFVKHGDIIQVGNVKLEVLHTPG-HTPESISFLLTDLGggssVpmgLFSGDF 146
Cdd:cd07709  106 FLKhfYPGIDERFVVVKDGDTLDLGKHTLKFIPAPMlHWPDTMVTYDPEDK----I---LFSGDA 163
NorV COG0426
Flavorubredoxin [Energy production and conversion];
15-146 7.85e-05

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 44.82  E-value: 7.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  15 SYLVgcqRTGEAIIIDPV---------RDLSKYIEVADSEGLTITqatetHIHADFASGIRDVAKRL-NANIYVSGEGED 84
Cdd:COG0426   36 SYLI---VDEKTALIDTVgesffeeflENLSKVIDPKKIDYIIVN-----HQEPDHSGSLPELLELApNAKIVCSKKAAR 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612903821  85 ALG--YKNMPSKTQFVKHGDIIQVGNVKLEVLHTPG-HTPESISFLLTdlggGSSVpmgLFSGDF 146
Cdd:COG0426  108 FLPhfYGIPDFRFIVVKEGDTLDLGGHTLQFIPAPMlHWPDTMFTYDP----EDKI---LFSGDA 165
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 58-197 9.06e-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) 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: 43.32  E-value: 9.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  58 HADFASGIRDVAKRLNANIYVSGEGEDALGYKNMPSKTqfVKHGDIIQVGNVKLEVLHT-PGHTPESISFLLTDlgggSS 136
Cdd:cd16282   82 HENTREELAARGEAYLELMRRLGGDAMAGTELVLPDRT--FDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPE----EG 155

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612903821 137 VpmgLFSGDFIFVGDIgrPDLLEKSVqikgsteisaKQMYESVQNIKNLpDYVQIWPGHGA 197
Cdd:cd16282  156 V---LFAGDLVFNGRI--PFLPDGSL----------AGWIAALDRLLAL-DATVVVPGHGP 200
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
366-429 1.10e-04

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 44.07  E-value: 1.10e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 366 VLDVRNDEEWNNGHLYQAVNIP------YGKLLNENIPFNKEDKIYVHCQSGVRSSIAVGILESKGFENV 429
Cdd:PRK00142 130 FIDMRNDYEYEIGHFENAIEPDietfreFPPWVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEV 199
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 55-139 1.17e-04

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: 43.27  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  55 THIHADFASGIRDVAKRLNANIYVSGE--------GEDALGYKNM----PSKT-QFVKHGDIIQVGNVKLEVLHTPGHTP 121
Cdd:cd16289   67 SHAHADHAGPLAALKRATGARVAANAEsavllargGSDDIHFGDGitfpPVQAdRIVMDGEVVTLGGVTFTAHFTPGHTP 146

                         90
                 ....*....|....*...
gi 612903821 122 ESISFLLTDLGGGSSVPM 139
Cdd:cd16289  147 GSTSWTWTDTRDGKPVRI 164
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 55-148 1.29e-04

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 43.16  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  55 THIHADFASGIRDVAKRLNANIYVS----GEGEDALGYKNMPSKTQF--VKHGDIIQVGNVKLEVLHTPGHTPESISFLL 128
Cdd:cd07714   62 THGHEDHIGALPYLLPELNVPIYATpltlALIKKKLEEFKLIKKVKLneIKPGERIKLGDFEVEFFRVTHSIPDSVGLAI 141

                         90       100
                 ....*....|....*....|.
gi 612903821 129 -TDLGggsSVpmgLFSGDFIF 148
Cdd:cd07714  142 kTPEG---TI---VHTGDFKF 156
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
332-435 1.94e-04

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 43.57  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821 332 QLIGFDKVAGYRLPKSGISTQSVHSADMT----------GKEEHVL-DVRNDEEWNNGHLYQAVNIPYGKLLNEN-IPFN 399
Cdd:PRK07411 257 KLIDYEQFCGIPQAKAAEAAQKAEIPEMTvtelkalldsGADDFVLiDVRNPNEYEIARIPGSVLVPLPDIENGPgVEKV 336

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 612903821 400 KE----DKIYVHCQSGVRSSIAVGILESKGFENvVNIREG 435
Cdd:PRK07411 337 KEllngHRLIAHCKMGGRSAKALGILKEAGIEG-TNVKGG 375
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 366-413 1.63e-03

Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain superfamily. Included in this CD is the Saccharomyces cerevisiae arsenate reductase protein, Acr2p, and other yeast and plant homologs.


Pssm-ID: 238789 [Multi-domain]  Cd Length: 113  Bit Score: 38.16  E-value: 1.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 612903821 366 VLDVRnDEEWNNGHLYQAVNIPYGKL------LNENIPFNKEDKIYVHC-QSGVR 413
Cdd:cd01531   22 VVDVR-DEDYAGGHIKGSWHYPSTRFkaqlnqLVQLLSGSKKDTVVFHCaLSQVR 75
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 13-196 2.17e-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: 39.10  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  13 QASYLVgcQRTGEAIIIDPVR---DLSKYIEV---ADSEGLTitqatethiHADFASGIRDVAKRLNANIYVSgegEDAL 86
Cdd:cd07727   15 AASYLI--LRPEGNILVDSPRyspPLAKRIEAlggIRYIFLT---------HRDDVADHAKWAERFGAKRIIH---EDDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  87 GYKNMPSKTQFVKHGDIIQVGNvKLEVLHTPGHTPESISFLLTDLGggssvpmGLFSGDFIFVgDIGRPDLLEKSVQIKG 166
Cdd:cd07727   81 NAVTRPDEVIVLWGGDPWELDP-DLTLIPVPGHTRGSVVLLYKEKG-------VLFTGDHLAW-SRRRGWLSAFRYVCWY 151

                        170       180       190
                 ....*....|....*....|....*....|
gi 612903821 167 STEISAkqmyESVQNIKNLpDYVQIWPGHG 196
Cdd:cd07727  152 SWPEQA----ESVERLADL-DFEWVLPGHG 176
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 55-126 2.51e-03

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: 39.46  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  55 THIHADFASGIRDVAKRLNANIYVSGEGEDAL-------------GYKNMP--SKTQFVKHGDIIQVGNVKLEVLHTPGH 119
Cdd:cd16313   67 SHDHWDHAGGIAALQKLTGAQVLASPATVAVLrsgsmgkddpqfgGLTPMPpvASVRAVRDGEVVKLGPLAVTAHATPGH 146


                 ....*..
gi 612903821 120 TPESISF 126
Cdd:cd16313  147 TTGGTSW 153
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 55-125 5.19e-03

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: 38.48  E-value: 5.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  55 THIHADFASGIRDVAKRLNANIYVSGEGEDAL--GyKNMPSKTQF--------------VKHGDIIQVGNVKLEVLHTPG 118
Cdd:cd16315   67 SHEHFDHVGGLAALQRATGARVAASAAAAPVLesG-KPAPDDPQAglhepfppvrvdriVEDGDTVALGSLRLTAHATPG 145


                 ....*..
gi 612903821 119 HTPESIS 125
Cdd:cd16315  146 HTPGALS 152
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 54-121 8.74e-03

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: 37.82  E-value: 8.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612903821  54 ETHIHADFASGIRDVAKRLNANIYVS-----------GEGEDALGYKNMPSKT--QFVKHGDIIQVGNVKLEVLHTPGHT 120
Cdd:cd16310   66 NTHAHYDHAGGLAQLKADTGAKLWASrgdrpaleagkHIGDNITQPAPFPAVKvdRILGDGEKIKLGDITLTATLTPGHT 145


                 .
gi 612903821 121 P 121
Cdd:cd16310  146 K 146
 
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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