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Conserved domains on  [gi|18394685|ref|NP_564070|]
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DNA repair metallo-beta-lactamase family protein [Arabidopsis thaliana]

Protein Classification

DNA cross-link repair protein( domain architecture ID 11039898)

DNA cross-link repair protein similar to Arabidopsis thaliana SNM1, which is involved in the repair of DNA lesions formed by oxidative stress

Gene Ontology:  GO:0006974|GO:0005634
PubMed:  12177301|20528238

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 7-159 3.42e-31

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


The actual alignment was detected with superfamily member cd16273:

Pssm-ID: 451500  Cd Length: 160  Bit Score: 118.41  E-value: 3.42e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685   7 RGLPFAVDTFGpYtETKRRKRHHFLTHAHKDHTVGVSPSnivvF---PIYSTSLTISLLLQRFpQLDESYFVRVEIGQSV 83
Cdd:cd16273  20 PGTSFVVDAFK-Y-GKIPGISAYFLSHFHSDHYGGLTKS----WshgPIYCSEITANLVKLKL-KVDEEYIVVLPMNTPV 92

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18394685  84 IVDDPdgeFKVTAFDANHCPGAVMFLFEGSFG-NILHTGDCRLTLDcLHSLPEKyvgrshgmKPKCSLGYIFLDCTF 159
Cdd:cd16273  93 EIDGD---VSVTLLDANHCPGAVMFLFELPDGrRILHTGDFRANPE-MLEHPLL--------LGKRRIDTVYLDTTY 157
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 232-347 4.01e-27

DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in pfam00753 and are common to all metallo-beta-lactamases. The fifth motif appears to be specific to function. This entry represents the fifth motif from metallo-beta-lactamases involved in DNA repair.


:

Pssm-ID: 429512  Cd Length: 108  Bit Score: 105.44  E-value: 4.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685   232 IVPEIVSEDPSSRFHIFsGFPKLYERTSAKLAEARSKLQSEPLIIRPSAqwYVCDDEDDWKSGSIQKQRKVRFSeavkde 311
Cdd:pfam07522   3 ILSLLTTDPLSTQIHVV-PMPKLSYEALLDYLTARKDHFDSVLAIRPTG--WTYRPPKTEVSDRIGPSIRGRIT------ 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 18394685   312 fgLWHVCYSMHSSRAELESAMQLLSPKWVVSTVPSC 347
Cdd:pfam07522  74 --IYGVPYSEHSSFDELKEFVQFLRPKKIIPTVNVG 107
 
Name Accession Description Interval E-value
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 7-159 3.42e-31

SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) and Saccharomyces cerevisiae Pso2 protein (PSOralen derivative sensitive 2, also known as SNM1, sensitive to nitrogen mustard 1), both proteins are 5'-exonucleases and function in interstrand cross-links (ICL) repair. Also includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein, and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. 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: 293831  Cd Length: 160  Bit Score: 118.41  E-value: 3.42e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685   7 RGLPFAVDTFGpYtETKRRKRHHFLTHAHKDHTVGVSPSnivvF---PIYSTSLTISLLLQRFpQLDESYFVRVEIGQSV 83
Cdd:cd16273  20 PGTSFVVDAFK-Y-GKIPGISAYFLSHFHSDHYGGLTKS----WshgPIYCSEITANLVKLKL-KVDEEYIVVLPMNTPV 92

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18394685  84 IVDDPdgeFKVTAFDANHCPGAVMFLFEGSFG-NILHTGDCRLTLDcLHSLPEKyvgrshgmKPKCSLGYIFLDCTF 159
Cdd:cd16273  93 EIDGD---VSVTLLDANHCPGAVMFLFELPDGrRILHTGDFRANPE-MLEHPLL--------LGKRRIDTVYLDTTY 157
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 232-347 4.01e-27

DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in pfam00753 and are common to all metallo-beta-lactamases. The fifth motif appears to be specific to function. This entry represents the fifth motif from metallo-beta-lactamases involved in DNA repair.


Pssm-ID: 429512  Cd Length: 108  Bit Score: 105.44  E-value: 4.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685   232 IVPEIVSEDPSSRFHIFsGFPKLYERTSAKLAEARSKLQSEPLIIRPSAqwYVCDDEDDWKSGSIQKQRKVRFSeavkde 311
Cdd:pfam07522   3 ILSLLTTDPLSTQIHVV-PMPKLSYEALLDYLTARKDHFDSVLAIRPTG--WTYRPPKTEVSDRIGPSIRGRIT------ 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 18394685   312 fgLWHVCYSMHSSRAELESAMQLLSPKWVVSTVPSC 347
Cdd:pfam07522  74 --IYGVPYSEHSSFDELKEFVQFLRPKKIIPTVNVG 107
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 30-135 1.30e-11

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 64.92  E-value: 1.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  30 FLTHAHKDHTVGV-------SPSNIvvfPIYSTSLTISLLLQRFPQLDESY-----FVRVEIGQSVIVDDpdgeFKVTAF 97
Cdd:COG1235  73 LLTHEHADHIAGLddlrpryGPNPI---PVYATPGTLEALERRFPYLFAPYpgkleFHEIEPGEPFEIGG----LTVTPF 145

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 18394685  98 DANH-CPGAVMFLFEGSFGNILHTGDCR---------------LTLDCLHSLPE 135
Cdd:COG1235 146 PVPHdAGDPVGYRIEDGGKKLAYATDTGyipeevlellrgadlLILDATYDDPE 199
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 30-135 2.37e-06

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: 47.93  E-value: 2.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685     30 FLTHAHKDHTVGVSP----SNIvvfPIYSTSLTISLLLQRFPQLDESYFVRVEIGQSVIVDDPD----GEFKVTAFDA-N 100
Cdd:smart00849  40 ILTHGHPDHIGGLPElleaPGA---PVYAPEGTAELLKDLLALLGELGAEAEPAPPDRTLKDGDeldlGGGELEVIHTpG 116

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 18394685    101 HCPGAVMFLFEGsfGNILHTGDCRLTLDCLHSLPE 135
Cdd:smart00849 117 HTPGSIVLYLPE--GKILFTGDLLFAGGDGRTLVD 149
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 30-126 4.83e-06

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 47.30  E-value: 4.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685    30 FLTHAHKDHTVGVsPS--NIVVFPIYSTSLTISLLLQRFPQ--LDESYFVRV---EIGQSVIVDDPDgeFKVTAFDANH- 101
Cdd:pfam12706  33 LLTHDHYDHLAGL-LDlrEGRPRPLYAPLGVLAHLRRNFPYlfLLEHYGVRVheiDWGESFTVGDGG--LTVTATPARHg 109

                          90       100       110
                  ....*....|....*....|....*....|...
gi 18394685   102 -------CPGAVM-FLFEGSFGNILHTGDCRLT 126
Cdd:pfam12706 110 sprgldpNPGDTLgFRIEGPGKRVYYAGDTGYF 142
 
Name Accession Description Interval E-value
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 7-159 3.42e-31

SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) and Saccharomyces cerevisiae Pso2 protein (PSOralen derivative sensitive 2, also known as SNM1, sensitive to nitrogen mustard 1), both proteins are 5'-exonucleases and function in interstrand cross-links (ICL) repair. Also includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein, and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. 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: 293831  Cd Length: 160  Bit Score: 118.41  E-value: 3.42e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685   7 RGLPFAVDTFGpYtETKRRKRHHFLTHAHKDHTVGVSPSnivvF---PIYSTSLTISLLLQRFpQLDESYFVRVEIGQSV 83
Cdd:cd16273  20 PGTSFVVDAFK-Y-GKIPGISAYFLSHFHSDHYGGLTKS----WshgPIYCSEITANLVKLKL-KVDEEYIVVLPMNTPV 92

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18394685  84 IVDDPdgeFKVTAFDANHCPGAVMFLFEGSFG-NILHTGDCRLTLDcLHSLPEKyvgrshgmKPKCSLGYIFLDCTF 159
Cdd:cd16273  93 EIDGD---VSVTLLDANHCPGAVMFLFELPDGrRILHTGDFRANPE-MLEHPLL--------LGKRRIDTVYLDTTY 157
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 232-347 4.01e-27

DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in pfam00753 and are common to all metallo-beta-lactamases. The fifth motif appears to be specific to function. This entry represents the fifth motif from metallo-beta-lactamases involved in DNA repair.


Pssm-ID: 429512  Cd Length: 108  Bit Score: 105.44  E-value: 4.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685   232 IVPEIVSEDPSSRFHIFsGFPKLYERTSAKLAEARSKLQSEPLIIRPSAqwYVCDDEDDWKSGSIQKQRKVRFSeavkde 311
Cdd:pfam07522   3 ILSLLTTDPLSTQIHVV-PMPKLSYEALLDYLTARKDHFDSVLAIRPTG--WTYRPPKTEVSDRIGPSIRGRIT------ 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 18394685   312 fgLWHVCYSMHSSRAELESAMQLLSPKWVVSTVPSC 347
Cdd:pfam07522  74 --IYGVPYSEHSSFDELKEFVQFLRPKKIIPTVNVG 107
artemis-SNM1C-like_MBL-fold cd16297
artemis-SNM1C and related proteins; MBL-fold metallo-hydrolase domain; Includes the nuclease ...
 25-125 1.28e-15

artemis-SNM1C and related proteins; MBL-fold metallo-hydrolase domain; Includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. Inactivation of Artemis causes severe combined immunodeficiency (SCID). 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: 293855  Cd Length: 171  Bit Score: 74.85  E-value: 1.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  25 RKRHHFLTHAHKDHTVGV-SPS------NIVVFPIYSTSLTISLLLQRfPQLD--ESYFVRVEIG---QSVIVDDPDGE- 91
Cdd:cd16297  25 RARAYFLSHCHKDHMKGLrAPGlkrrlkASLKVKLYCSPVTKELLLTN-PKYAfwENHIVSLEIDtptQISLVDEATGEk 103

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 18394685  92 --FKVTAFDANHCPGAVMFLFEGSFGNILHTGDCRL 125
Cdd:cd16297 104 edVVVTLLPAGHCPGSVMFLFQGNNGTVLYTGDFRL 139
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 8-124 4.58e-15

5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) which is a 5'-exonuclease and functions in interstrand cross-links (ICL) repair. 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: 293856 [Multi-domain]  Cd Length: 157  Bit Score: 72.93  E-value: 4.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685   8 GLPFAVDTFgPYTETKRRKRHhFLTHAHKDHTVGVSPSniVVFPIYSTSLTISLLLQRFpQLDESYFVRVEIGQSVIVDD 87
Cdd:cd16298  21 GTGFTVDAF-QYGVIEGCTAY-FLTHFHSDHYCGLTKK--FKFPIYCSKITGNLVKSKL-KVEEQYINVLPMNTECIVNG 95

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 18394685  88 pdgeFKVTAFDANHCPGAVMFLFEGSFGN-ILHTGDCR 124
Cdd:cd16298  96 ----VKVVLLDANHCPGAVMILFRLPSGTlVLHTGDFR 129
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 21-122 3.93e-13

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: 69.36  E-value: 3.93e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  21 ETKRRKRHHFLTHAHKDHtVGVSP--SNIVVFPIYSTSLTISLL---LQRFPQLDESYFVRVEIGQSVIVddpdGEFKVT 95
Cdd:cd07714  51 ENKDKIKGIFITHGHEDH-IGALPylLPELNVPIYATPLTLALIkkkLEEFKLIKKVKLNEIKPGERIKL----GDFEVE 125

                        90       100
                ....*....|....*....|....*...
gi 18394685  96 AFDANHC-PGAVMFLFEGSFGNILHTGD 122
Cdd:cd07714 126 FFRVTHSiPDSVGLAIKTPEGTIVHTGD 153
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 30-135 1.30e-11

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 64.92  E-value: 1.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  30 FLTHAHKDHTVGV-------SPSNIvvfPIYSTSLTISLLLQRFPQLDESY-----FVRVEIGQSVIVDDpdgeFKVTAF 97
Cdd:COG1235  73 LLTHEHADHIAGLddlrpryGPNPI---PVYATPGTLEALERRFPYLFAPYpgkleFHEIEPGEPFEIGG----LTVTPF 145

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 18394685  98 DANH-CPGAVMFLFEGSFGNILHTGDCR---------------LTLDCLHSLPE 135
Cdd:COG1235 146 PVPHdAGDPVGYRIEDGGKKLAYATDTGyipeevlellrgadlLILDATYDDPE 199
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
23-122 3.10e-11

mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 65.85  E-value: 3.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  23 KRRKR--HHFLTHAHKDH---------TVGVspsnivvfPIYSTSLTISLL---LQRFPQLDESYFVRVEIGQSVIVddp 88
Cdd:COG0595  59 ENKDKikGIVLTHGHEDHigalpyllkELNV--------PVYGTPLTLALLeakLKEHGLLKKVKLHVVKPGDRIKF--- 127

                        90       100       110
                ....*....|....*....|....*....|....*
gi 18394685  89 dGEFKVTAFDANH-CPGAVMFLFEGSFGNILHTGD 122
Cdd:COG0595 128 -GPFKVEFFRVTHsIPDSLGLAIRTPAGTIVHTGD 161
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 30-149 6.85e-11

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


Pssm-ID: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 61.86  E-value: 6.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  30 FLTHAHKDHT--VGVSPSNIvvfPIYSTSLTISLLLQRFPQLDESYfvrvEIGQSVIVDDPD-----GEFKVTAFDANH- 101
Cdd:cd07732  80 LLSHAHLDHYglLNYLRPDI---PVYMGEATKRILKALLPFFGEGD----PVPRNIRVFESGksftiGDFTVTPYLVDHs 152

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 18394685 102 CPGAVMFLFEGSFGNILHTGDCRLtldclhslpekyvgrsHGMKPKCS 149
Cdd:cd07732 153 APGAYAFLIEAPGKRIFYTGDFRF----------------HGRKPELT 184
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 30-135 2.37e-06

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: 47.93  E-value: 2.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685     30 FLTHAHKDHTVGVSP----SNIvvfPIYSTSLTISLLLQRFPQLDESYFVRVEIGQSVIVDDPD----GEFKVTAFDA-N 100
Cdd:smart00849  40 ILTHGHPDHIGGLPElleaPGA---PVYAPEGTAELLKDLLALLGELGAEAEPAPPDRTLKDGDeldlGGGELEVIHTpG 116

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 18394685    101 HCPGAVMFLFEGsfGNILHTGDCRLTLDCLHSLPE 135
Cdd:smart00849 117 HTPGSIVLYLPE--GKILFTGDLLFAGGDGRTLVD 149
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 30-122 3.74e-06

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: 47.67  E-value: 3.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  30 FLTHAHKDHTVGVSP----SNIvvfPIYSTSLTISLLLQRFPQLDESYFVR-VEIGQSVIVDDPD----GEFKVTAFDA- 99
Cdd:cd06262  50 LLTHGHFDHIGGLAElkeaPGA---PVYIHEADAELLEDPELNLAFFGGGPlPPPEPDILLEDGDtielGGLELEVIHTp 126

                        90       100
                ....*....|....*....|...
gi 18394685 100 NHCPGAVMFLFEGsfGNILHTGD 122
Cdd:cd06262 127 GHTPGSVCFYIEE--EGVLFTGD 147
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 30-126 4.83e-06

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 47.30  E-value: 4.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685    30 FLTHAHKDHTVGVsPS--NIVVFPIYSTSLTISLLLQRFPQ--LDESYFVRV---EIGQSVIVDDPDgeFKVTAFDANH- 101
Cdd:pfam12706  33 LLTHDHYDHLAGL-LDlrEGRPRPLYAPLGVLAHLRRNFPYlfLLEHYGVRVheiDWGESFTVGDGG--LTVTATPARHg 109

                          90       100       110
                  ....*....|....*....|....*....|...
gi 18394685   102 -------CPGAVM-FLFEGSFGNILHTGDCRLT 126
Cdd:pfam12706 110 sprgldpNPGDTLgFRIEGPGKRVYYAGDTGYF 142
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 31-122 8.27e-06

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


Pssm-ID: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 46.56  E-value: 8.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  31 LTHAHKDHtVGVSP----SNIVVFPIYSTSLTISLL----------LQRFPQLDESY-----------FVRVEIGQSViv 85
Cdd:cd07734  55 ISHFHLDH-CGALPylfrGFIFRGPIYATHPTVALGrllledyvksAERIGQDQSLYtpedieealkhIVPLGYGQSI-- 131

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 18394685  86 dDPDGEFKVTAFDANHCPGAVMFLFEGSFGNILHTGD 122
Cdd:cd07734 132 -DLFPALSLTAYNAGHVLGAAMWEIQIYGEKLVYTGD 167
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 27-122 1.06e-05

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. 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: 293821  Cd Length: 259  Bit Score: 47.21  E-value: 1.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  27 RHHFLTHAHKDHTVG---VSPSNIVVF----PIYSTSLTISLL------------LQRFPQLDESYFVRVEIGQSVIVdd 87
Cdd:cd07735  67 RHYLITHAHLDHIAGlplLSPNDGGQRgspkTIYGLPETIDALkkhifnwviwpdFTSIPSGKYPYLRLEPIEPEYPI-- 144

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 18394685  88 PDGEFKVTAFDANH-CPGAVMFLFEGSFGNILHTGD 122
Cdd:cd07735 145 ALTGLSVTAFPVSHgVPVSTAFLIRDGGDSFLFFGD 180
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 30-122 2.37e-05

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 46.72  E-value: 2.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  30 FLTHAHKDHtVGVSPSNIVVF---PIYSTSLTISLLLQRFP-----QLDE----------------SYFVRVEIGQSVIV 85
Cdd:COG1236  55 VLTHAHLDH-SGALPLLVKEGfrgPIYATPATADLARILLGdsakiQEEEaeaeplyteedaeralELFQTVDYGEPFEI 133

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 18394685  86 DDpdgeFKVTAFDANHCPGAVMFLFEGSFGNILHTGD 122
Cdd:COG1236 134 GG----VRVTFHPAGHILGSAQVELEVGGKRIVFSGD 166
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 30-122 2.97e-05

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 45.29  E-value: 2.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  30 FLTHAHKDH-----TVGVSPSNIVVFpiysTSLTISLLLQR--FPQldesyFVRVEIGQSVIVDDpdgeFKVTAFDANHC 102
Cdd:COG2220  53 LVTHDHYDHlddatLRALKRTGATVV----APLGVAAWLRAwgFPR-----VTELDWGESVELGG----LTVTAVPARHS 119

                        90       100
                ....*....|....*....|....*...
gi 18394685 103 PG--------AVMFLFEGSFGNILHTGD 122
Cdd:COG2220 120 SGrpdrngglWVGFVIETDGKTIYHAGD 147
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
30-178 3.11e-05

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 45.57  E-value: 3.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  30 FLTHAHKDHTVGVSPsnIVVF----------PIYSTSLTISLL--LQRFPQLDESYFVRV-EIGQSVIVDdpDGEFKVTA 96
Cdd:COG1234  57 FITHLHGDHIAGLPG--LLSTrslagrekplTIYGPPGTKEFLeaLLKASGTDLDFPLEFhEIEPGEVFE--IGGFTVTA 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  97 FDANHCPGAVMFLFEGSFGNILHTGDCRLTldclhslpEKYVGRSHGmkpkCSLGYIflDCTFGKSSHSQRFPTKHSAIR 176
Cdd:COG1234 133 FPLDHPVPAYGYRFEEPGRSLVYSGDTRPC--------EALVELAKG----ADLLIH--EATFLDEEAELAKETGHSTAK 198


                ..
gi 18394685 177 QI 178
Cdd:COG1234 199 EA 200
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 27-122 6.34e-04

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 41.21  E-value: 6.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  27 RHHFLTHAHKDHTVGVSP----SNIvvfPIYSTSLTISLLLQRFPQldeSYFVRVEIGQSVIVDDPD----GEFKVTAFD 98
Cdd:COG0491  53 KAVLLTHLHPDHVGGLAAlaeaFGA---PVYAHAAEAEALEAPAAG---ALFGREPVPPDRTLEDGDtlelGGPGLEVIH 126

                        90       100
                ....*....|....*....|....*
gi 18394685  99 AN-HCPGAVMFLFEGsfGNILHTGD 122
Cdd:COG0491 127 TPgHTPGHVSFYVPD--EKVLFTGD 149
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 30-136 1.42e-03

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


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 40.15  E-value: 1.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  30 FLTHAHKDHTVG---VSPSNIVV---FPIYSTSLTISLLLQRFPQLDESY---------FVRVEIGQSVIVddpdGEFKV 94
Cdd:cd16279  71 LLTHAHADHIHGlddLRPFNRLQqrpIPVYASEETLDDLKRRFPYFFAATggggvpkldLHIIEPDEPFTI----GGLEI 146

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 18394685  95 TAFDANHCPGAVM-FLfegsFGNILHTGDCrltldclHSLPEK 136
Cdd:cd16279 147 TPLPVLHGKLPSLgFR----FGDFAYLTDV-------SEIPEE 178
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 30-123 1.52e-03

Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 39.94  E-value: 1.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  30 FLTHAHKDHTVGVSPsnIVVF---PIYSTSLTI-----------SLLLQRFPQLDESYFVRV-EIGQSVIVDDpDGEFKV 94
Cdd:cd16272  55 FLSHFHLDHIGGLPT--LLFArryGGRKKPLTIygpkgikefleKLLNFPVEILPLGFPLEIeELEEGGEVLE-LGDLKV 131

                        90       100       110
                ....*....|....*....|....*....|
gi 18394685  95 TAFDANHCPGAVMFLFEgSFGNIL-HTGDC 123
Cdd:cd16272 132 EAFPVKHSVESLGYRIE-AEGKSIvYSGDT 160
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 30-111 5.01e-03

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 38.63  E-value: 5.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  30 FLTHAHKDHTVGV-------SPSNIVVfpIYSTSLTISLLLQRF-PQLDESYF-VRVEI------------GQSVIVddp 88
Cdd:cd07715  62 LLSHTHWDHIQGFpffapayDPGNRIH--IYGPHKDGGSLEEVLrRQMSPPYFpVPLEEllaaiefhdlepGEPFSI--- 136

                        90       100
                ....*....|....*....|...
gi 18394685  89 dGEFKVTAFDANHCPGAVMFLFE 111
Cdd:cd07715 137 -GGVTVTTIPLNHPGGALGYRIE 158
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 13-122 8.01e-03

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 37.93  E-value: 8.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  13 VDTFGPYTETKR-----RK------RHHFLTHAHKDHTVGVSpsnivVF-----PIYSTSLTISLLLQRFPQLDESY--F 74
Cdd:cd16282  29 IDTGASPRLARAllaaiRKvtdkpvRYVVNTHYHGDHTLGNA-----AFadagaPIIAHENTREELAARGEAYLELMrrL 103

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394685  75 VRVEIGQSVI------VDDP------DGEFKVTAFDANHCPGAVMFLFEGSfgNILHTGD 122
Cdd:cd16282 104 GGDAMAGTELvlpdrtFDDGltldlgGRTVELIHLGPAHTPGDLVVWLPEE--GVLFAGD 161
 
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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