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Conserved domains on  [gi|21357063|ref|NP_649548|]
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Snm1 [Drosophila melanogaster]

Protein Classification

DNA cross-link repair protein( domain architecture ID 10888615)

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

CATH:  3.60.15.10|3.40.50.12650
Gene Ontology:  GO:0003684|GO:0046872|GO:0006281|GO:0035312|GO:0036297
PubMed:  12177301|11471246|11513844|17597585|20528238

Graphical summary

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List of domain hits

 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; ...
 252-408 8.64e-82

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: 257.85  E-value: 8.64e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 252 KGTVRKQRKPKPCPPYKVVEGTSFCVDGFQFGEIEGVTHYFLTHFHADHYIGLTKKFCH-PLYVSPISARLVRTFIKLDE 330
Cdd:cd16273   1 KSSKKKPKRKKPCPFYKIIPGTSFVVDAFKYGKIPGISAYFLSHFHSDHYGGLTKSWSHgPIYCSEITANLVKLKLKVDE 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21357063 331 THIHEIDVDQTLDVDG-VQVTALEANHCPGALMFFFKLSSGECILHTGDFRASADMESLPIFWNHSNIDLLYLDTTYMN 408
Cdd:cd16273  81 EYIVVLPMNTPVEIDGdVSVTLLDANHCPGAVMFLFELPDGRRILHTGDFRANPEMLEHPLLLGKRRIDTVYLDTTYCN 159
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 481-578 1.03e-37

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: 136.25  E-value: 1.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063   481 PDLDSVLTEDRSGANLHVIAMGKISYPSLVDYFTEFEDQYDMLLGIRPSGWEKNS---------KPSYGKRISTIGIEYS 551
Cdd:pfam07522   1 PEILSLLTTDPLSTQIHVVPMPKLSYEALLDYLTARKDHFDSVLAIRPTGWTYRPpktevsdriGPSIRGRITIYGVPYS 80

                          90       100
                  ....*....|....*....|....*..
gi 21357063   552 EHSSYKELERFVRFLKPKRVISTVPVG 578
Cdd:pfam07522  81 EHSSFDELKEFVQFLRPKKIIPTVNVG 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; ...
 252-408 8.64e-82

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: 257.85  E-value: 8.64e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 252 KGTVRKQRKPKPCPPYKVVEGTSFCVDGFQFGEIEGVTHYFLTHFHADHYIGLTKKFCH-PLYVSPISARLVRTFIKLDE 330
Cdd:cd16273   1 KSSKKKPKRKKPCPFYKIIPGTSFVVDAFKYGKIPGISAYFLSHFHSDHYGGLTKSWSHgPIYCSEITANLVKLKLKVDE 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21357063 331 THIHEIDVDQTLDVDG-VQVTALEANHCPGALMFFFKLSSGECILHTGDFRASADMESLPIFWNHSNIDLLYLDTTYMN 408
Cdd:cd16273  81 EYIVVLPMNTPVEIDGdVSVTLLDANHCPGAVMFLFELPDGRRILHTGDFRANPEMLEHPLLLGKRRIDTVYLDTTYCN 159
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 481-578 1.03e-37

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: 136.25  E-value: 1.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063   481 PDLDSVLTEDRSGANLHVIAMGKISYPSLVDYFTEFEDQYDMLLGIRPSGWEKNS---------KPSYGKRISTIGIEYS 551
Cdd:pfam07522   1 PEILSLLTTDPLSTQIHVVPMPKLSYEALLDYLTARKDHFDSVLAIRPTGWTYRPpktevsdriGPSIRGRITIYGVPYS 80

                          90       100
                  ....*....|....*....|....*..
gi 21357063   552 EHSSYKELERFVRFLKPKRVISTVPVG 578
Cdd:pfam07522  81 EHSSFDELKEFVQFLRPKKIIPTVNVG 107
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
270-417 8.09e-14

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 71.76  E-value: 8.09e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 270 VEGTSFCVDgfqFGE------------IEGVTHYFLTHFHADHYIGL------------TKKFchPLYVSPISARLVRTF 325
Cdd:COG1234  26 AGGERLLID---CGEgtqrqllragldPRDIDAIFITHLHGDHIAGLpgllstrslagrEKPL--TIYGPPGTKEFLEAL 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 326 IKLDETH------IHEIDVDQTLDVDGVQVTALEANHCPGALMFFFKlSSGECILHTGDFRASADMESLpifwnHSNIDL 399
Cdd:COG1234 101 LKASGTDldfpleFHEIEPGEVFEIGGFTVTAFPLDHPVPAYGYRFE-EPGRSLVYSGDTRPCEALVEL-----AKGADL 174

                       170
                ....*....|....*...
gi 21357063 400 LYLDTTYMNKNYDFCHQS 417
Cdd:COG1234 175 LIHEATFLDEEAELAKET 192
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 292-379 3.00e-09

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: 57.18  E-value: 3.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063    292 FLTHFHADHYIG---LTKKFCHPLYVSPISARLVRTFIKL---------DETHIHEIDVDQTLDVDGVQVTALEA-NHCP 358
Cdd:smart00849  40 ILTHGHPDHIGGlpeLLEAPGAPVYAPEGTAELLKDLLALlgelgaeaePAPPDRTLKDGDELDLGGGELEVIHTpGHTP 119

                           90       100
                   ....*....|....*....|.
gi 21357063    359 GALMFFFKlssGECILHTGDF 379
Cdd:smart00849 120 GSIVLYLP---EGKILFTGDL 137
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 285-356 5.50e-05

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: 44.61  E-value: 5.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063   285 IEGVthyFLTHFHADHYIGLT--KKFC-HPLYVSP-ISARLVRTFIKL-----DETHIHEIDVDQTLDVD--GVQVTALE 353
Cdd:pfam12706  29 IDAV---LLTHDHYDHLAGLLdlREGRpRPLYAPLgVLAHLRRNFPYLfllehYGVRVHEIDWGESFTVGdgGLTVTATP 105


                  ...
gi 21357063   354 ANH 356
Cdd:pfam12706 106 ARH 108
 
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; ...
 252-408 8.64e-82

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: 257.85  E-value: 8.64e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 252 KGTVRKQRKPKPCPPYKVVEGTSFCVDGFQFGEIEGVTHYFLTHFHADHYIGLTKKFCH-PLYVSPISARLVRTFIKLDE 330
Cdd:cd16273   1 KSSKKKPKRKKPCPFYKIIPGTSFVVDAFKYGKIPGISAYFLSHFHSDHYGGLTKSWSHgPIYCSEITANLVKLKLKVDE 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21357063 331 THIHEIDVDQTLDVDG-VQVTALEANHCPGALMFFFKLSSGECILHTGDFRASADMESLPIFWNHSNIDLLYLDTTYMN 408
Cdd:cd16273  81 EYIVVLPMNTPVEIDGdVSVTLLDANHCPGAVMFLFELPDGRRILHTGDFRANPEMLEHPLLLGKRRIDTVYLDTTYCN 159
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 259-408 6.63e-58

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: 193.89  E-value: 6.63e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 259 RKPKPCPPYKVVEGTSFCVDGFQFGEIEGVTHYFLTHFHADHYIGLTKKFCHPLYVSPISARLVRTFIKLDETHIHEIDV 338
Cdd:cd16298   8 KRKKTCPFYKKIPGTGFTVDAFQYGVIEGCTAYFLTHFHSDHYCGLTKKFKFPIYCSKITGNLVKSKLKVEEQYINVLPM 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 339 DQTLDVDGVQVTALEANHCPGALMFFFKLSSGECILHTGDFRASADMESLPIFWNHsNIDLLYLDTTYMN 408
Cdd:cd16298  88 NTECIVNGVKVVLLDANHCPGAVMILFRLPSGTLVLHTGDFRADPSMERYPELIGQ-KIHTLYLDTTYCS 156
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 481-578 1.03e-37

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: 136.25  E-value: 1.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063   481 PDLDSVLTEDRSGANLHVIAMGKISYPSLVDYFTEFEDQYDMLLGIRPSGWEKNS---------KPSYGKRISTIGIEYS 551
Cdd:pfam07522   1 PEILSLLTTDPLSTQIHVVPMPKLSYEALLDYLTARKDHFDSVLAIRPTGWTYRPpktevsdriGPSIRGRITIYGVPYS 80

                          90       100
                  ....*....|....*....|....*..
gi 21357063   552 EHSSYKELERFVRFLKPKRVISTVPVG 578
Cdd:pfam07522  81 EHSSFDELKEFVQFLRPKKIIPTVNVG 107
artemis-SNM1C-like_MBL-fold cd16297
artemis-SNM1C and related proteins; MBL-fold metallo-hydrolase domain; Includes the nuclease ...
 291-406 1.01e-14

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: 72.54  E-value: 1.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 291 YFLTHFHADHYIGLTKKFCHP---------LYVSPISARLVRTFIKLD--ETHIHEIDVDQ----------TLDVDGVQV 349
Cdd:cd16297  29 YFLSHCHKDHMKGLRAPGLKRrlkaslkvkLYCSPVTKELLLTNPKYAfwENHIVSLEIDTptqislvdeaTGEKEDVVV 108

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21357063 350 TALEANHCPGALMFFFKLSSGeCILHTGDFR----ASADMESLpifwnHS-----NIDLLYLDTTY 406
Cdd:cd16297 109 TLLPAGHCPGSVMFLFQGNNG-TVLYTGDFRlavgEAARMELL-----HSgdrvkDIQSVYLDTTF 168
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
270-417 8.09e-14

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 71.76  E-value: 8.09e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 270 VEGTSFCVDgfqFGE------------IEGVTHYFLTHFHADHYIGL------------TKKFchPLYVSPISARLVRTF 325
Cdd:COG1234  26 AGGERLLID---CGEgtqrqllragldPRDIDAIFITHLHGDHIAGLpgllstrslagrEKPL--TIYGPPGTKEFLEAL 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 326 IKLDETH------IHEIDVDQTLDVDGVQVTALEANHCPGALMFFFKlSSGECILHTGDFRASADMESLpifwnHSNIDL 399
Cdd:COG1234 101 LKASGTDldfpleFHEIEPGEVFEIGGFTVTAFPLDHPVPAYGYRFE-EPGRSLVYSGDTRPCEALVEL-----AKGADL 174

                       170
                ....*....|....*...
gi 21357063 400 LYLDTTYMNKNYDFCHQS 417
Cdd:COG1234 175 LIHEATFLDEEAELAKET 192
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 265-381 1.54e-09

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: 58.39  E-value: 1.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 265 PPYKVVEGTSFCVDGFQFGEIEGVTHYFLTHFHADHYiGLTkKFCH---PLYVSPISARL----VRTFIKLDETH--IHE 335
Cdd:cd07732  53 PDIVGLYRDPLLLGGLRSEEDPSVDAVLLSHAHLDHY-GLL-NYLRpdiPVYMGEATKRIlkalLPFFGEGDPVPrnIRV 130

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 21357063 336 IDVDQTLDVDGVQVTALEANH-CPGALMFFFKlSSGECILHTGDFRA 381
Cdd:cd07732 131 FESGKSFTIGDFTVTPYLVDHsAPGAYAFLIE-APGKRIFYTGDFRF 176
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 285-380 1.55e-09

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: 59.34  E-value: 1.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 285 IEGVthyFLTHFHADHyIG----LTKKFCHPLYVSPISARLVRTFIK----LDETHIHEIDVDQTLDVDGVQVTALEANH 356
Cdd:cd07714  56 IKGI---FITHGHEDH-IGalpyLLPELNVPIYATPLTLALIKKKLEefklIKKVKLNEIKPGERIKLGDFEVEFFRVTH 131

                        90       100
                ....*....|....*....|....*
gi 21357063 357 C-PGALMFFFKLSSGEcILHTGDFR 380
Cdd:cd07714 132 SiPDSVGLAIKTPEGT-IVHTGDFK 155
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
285-380 2.14e-09

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 60.85  E-value: 2.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 285 IEGVthyFLTHFHADHyIG----LTKKFCHPLYVSPISARLVRTFIK----LDETHIHEIDVDQTLDVDGVQVTALEANH 356
Cdd:COG0595  64 IKGI---VLTHGHEDH-IGalpyLLKELNVPVYGTPLTLALLEAKLKehglLKKVKLHVVKPGDRIKFGPFKVEFFRVTH 139

                        90       100
                ....*....|....*....|....*
gi 21357063 357 -CPGALMFFFKLSSGEcILHTGDFR 380
Cdd:COG0595 140 sIPDSLGLAIRTPAGT-IVHTGDFK 163
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 292-379 3.00e-09

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: 57.18  E-value: 3.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063    292 FLTHFHADHYIG---LTKKFCHPLYVSPISARLVRTFIKL---------DETHIHEIDVDQTLDVDGVQVTALEA-NHCP 358
Cdd:smart00849  40 ILTHGHPDHIGGlpeLLEAPGAPVYAPEGTAELLKDLLALlgelgaeaePAPPDRTLKDGDELDLGGGELEVIHTpGHTP 119

                           90       100
                   ....*....|....*....|.
gi 21357063    359 GALMFFFKlssGECILHTGDF 379
Cdd:smart00849 120 GSIVLYLP---EGKILFTGDL 137
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 266-440 4.28e-09

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 57.62  E-value: 4.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 266 PYKVVEGTSFCVDGFQFGEIEGVTHYFLTHFHADHY----IGLTKKFCHPLYVSPISARLVRtfiKLDETHIHEIDVDQT 341
Cdd:COG2220  27 PVFSGRASPVNPLPLDPEDLPKIDAVLVTHDHYDHLddatLRALKRTGATVVAPLGVAAWLR---AWGFPRVTELDWGES 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 342 LDVDGVQVTALEANHCPG--------ALMFFFKlSSGECILHTGDFRASADMESLPifwNHSNIDLLYLdttymnkNYDF 413
Cdd:COG2220 104 VELGGLTVTAVPARHSSGrpdrngglWVGFVIE-TDGKTIYHAGDTGYFPEMKEIG---ERFPIDVALL-------PIGA 172

                       170       180
                ....*....|....*....|....*..
gi 21357063 414 CHQSESVDRAVDLVRAFleknAAKRIL 440
Cdd:COG2220 173 YPFTMGPEEAAEAARDL----KPKVVI 195
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 292-384 8.44e-09

cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; MBL-fold metallo-hydrolase domain; CPSF3 (also known as cleavage and polyadenylation specificity factor 73 kDa subunit/CPSF-73) functions as a 3' endonuclease in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and in 3' end processing of metazoan histone pre-mRNAs. This subgroup also contains the yeast homolog of CPSF-73, Ysh1/Brr5 which has roles in mRNA and snoRNA synthesis. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain, and a RMMBL domain (RNA-metabolizing metallo-beta-lactamase). Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293850  Cd Length: 194  Bit Score: 56.05  E-value: 8.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 292 FLTHFHADHYIGL------------------TKKFCHPLY-----VSPISAR--------LVRTFIKldethIHEIDVDQ 340
Cdd:cd16292  57 LITHFHLDHCGALpyflqktnfkgrvfmthpTKAIYKWLLsdyvrVSNISSDemlytetdLEASMDK-----IETIDFHQ 131

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 21357063 341 TLDVDGVQVTALEANHCPGALMFFFKLsSGECILHTGDFRASAD 384
Cdd:cd16292 132 EVEVNGIKFTAYNAGHVLGAAMFMVEI-AGVRVLYTGDYSREED 174
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 279-406 1.67e-08

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 56.06  E-value: 1.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 279 GFQFGEIEGVthyFLTHFHADHYIG---LTKKFCH---PLYVSP-----ISARLVRTFIKLDET-HIHEIDVDQTLDVDG 346
Cdd:COG1235  63 GLDPSKIDAI---LLTHEHADHIAGlddLRPRYGPnpiPVYATPgtleaLERRFPYLFAPYPGKlEFHEIEPGEPFEIGG 139

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21357063 347 VQVTALEANH-CPGALMFFFKlSSGECILHTGDFRASADmESLPIFwnhSNIDLLYLDTTY 406
Cdd:COG1235 140 LTVTPFPVPHdAGDPVGYRIE-DGGKKLAYATDTGYIPE-EVLELL---RGADLLILDATY 195
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 279-379 2.10e-07

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 52.08  E-value: 2.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 279 GFQFGEIEGVthyFLTHFHADHyIG----LTKKFCH-PLYVSPISARLVRT----FIKLDET------------------ 331
Cdd:cd16295  46 PFDPKEIDAV---ILTHAHLDH-SGrlplLVKEGFRgPIYATPATKDLAELllldSAKIQEEeaehppaeplyteedvek 121

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 21357063 332 ---HIHEIDVDQTLDV-DGVQVTALEANHCPGALMFFFKLSSGECILHTGDF 379
Cdd:cd16295 122 alkHFRPVEYGEPFEIgPGVKVTFYDAGHILGSASVELEIGGGKRILFSGDL 173
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 288-382 2.47e-07

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: 51.52  E-value: 2.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 288 VTHYFLTHFHADHYIGLT--KKFCH-PLYVSPISARLVRT------FIKLDETHIHEIDV----DQTLDVDGVQVTALEA 354
Cdd:cd06262  46 IKAILLTHGHFDHIGGLAelKEAPGaPVYIHEADAELLEDpelnlaFFGGGPLPPPEPDIlledGDTIELGGLELEVIHT 125

                        90       100       110
                ....*....|....*....|....*....|.
gi 21357063 355 -NHCPGALMFFFKlssGECILHTGD--FRAS 382
Cdd:cd06262 126 pGHTPGSVCFYIE---EEGVLFTGDtlFAGS 153
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 288-378 2.62e-07

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: 52.00  E-value: 2.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 288 VTHYFLTHFHADHYIG---LTKKFCHPLYVSPISARLVRTFIKLDETHIHEIDVDQ------TLDVDGVQVTALEAN-HC 357
Cdd:COG0491  52 IKAVLLTHLHPDHVGGlaaLAEAFGAPVYAHAAEAEALEAPAAGALFGREPVPPDRtledgdTLELGGPGLEVIHTPgHT 131

                        90       100
                ....*....|....*....|.
gi 21357063 358 PGALMFFFKlssGECILHTGD 378
Cdd:COG0491 132 PGHVSFYVP---DEKVLFTGD 149
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 288-408 2.73e-07

Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; 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. 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. 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; this subgroup includes the short form (ELAC1). Only the short form exists in bacteria. 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: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 52.45  E-value: 2.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 288 VTHYFLTHFHADHYIGL-----TKKFC---HPLYV-SPISAR-LVRTFIKLDETH------IHEIDVDQTL--DVDGVQV 349
Cdd:cd07717  51 IDRIFITHLHGDHILGLpgllsTMSLLgrtEPLTIyGPKGLKeFLETLLRLSASRlpypieVHELEPDPGLvfEDDGFTV 130

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21357063 350 TALEANHCPGALMFFFKLssGECILHTGDfraSADMESLPIFWnhSNIDLLYLDTTYMN 408
Cdd:cd07717 131 TAFPLDHRVPCFGYRFEE--GRKIAYLGD---TRPCEGLVELA--KGADLLIHEATFLD 182
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 285-378 3.19e-07

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: 51.11  E-value: 3.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 285 IEGVTHYFLTHFHADHYIGL--------TKKFCHPL--YVSPISARLVRTFIKLDET--------HIHEIDVDQ-TLDVD 345
Cdd:cd16272  48 PDKLDAIFLSHFHLDHIGGLptllfarrYGGRKKPLtiYGPKGIKEFLEKLLNFPVEilplgfplEIEELEEGGeVLELG 127

                        90       100       110
                ....*....|....*....|....*....|...
gi 21357063 346 GVQVTALEANHCPGALMFFFKlSSGECILHTGD 378
Cdd:cd16272 128 DLKVEAFPVKHSVESLGYRIE-AEGKSIVYSGD 159
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 269-356 3.86e-07

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 50.98  E-value: 3.86e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 269 VVEGTSFCVD------------GFQFGEIEGVthyFLTHFHADHYIGL-----------------------TKKFCHPL- 312
Cdd:cd07719  24 VVGGRVYLVDagsgvvrrlaqaGLPLGDLDAV---FLTHLHSDHVADLpallltawlagrktplpvygppgTRALVDGLl 100

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 21357063 313 --YVSPISAR-LVRTFIKLDE---THIHEIDVDQT-LDVDGVQVTALEANH 356
Cdd:cd07719 101 aaYALDIDYRaRIGDEGRPDPgalVEVHEIAAGGVvYEDDGVKVTAFLVDH 151
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 284-450 3.47e-06

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 50.19  E-value: 3.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 284 EIEGVthyFLTHFHADHyIG----LTKKFCH-PLYVSPISARLVRTFIKlDETHIHEIDV-------------------- 338
Cdd:COG1236  50 DVDAV---VLTHAHLDH-SGalplLVKEGFRgPIYATPATADLARILLG-DSAKIQEEEAeaeplyteedaeralelfqt 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 339 ---DQTLDVDGVQVTALEANHCPGALMFFFKLsSGECILHTGDF-----RASADMESLPifwnhsNIDLLYLDTTYMNKN 410
Cdd:COG1236 125 vdyGEPFEIGGVRVTFHPAGHILGSAQVELEV-GGKRIVFSGDYgreddPLLAPPEPVP------PADVLITESTYGDRL 197

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 21357063 411 YDfcHQSESVDRAVDLVRAFLEKnaaKRILIVcGSYVIGK 450
Cdd:COG1236 198 HP--PREEVEAELAEWVRETLAR---GGTVLI-PAFALGR 231
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 286-408 7.23e-06

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: 48.36  E-value: 7.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 286 EGVTHYFLTHFHADHYIGL------------TKKfchPLYVSPISARLVRTFI---------------KLDETHIHEIDV 338
Cdd:cd07735  64 QRIRHYLITHAHLDHIAGLpllspndggqrgSPK---TIYGLPETIDALKKHIfnwviwpdftsipsgKYPYLRLEPIEP 140

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 339 DQTLDVDGVQVTALEANH-CPGALMFFFKlSSGECILHTGDFraSADMES----LPIFWNH------SNIDLLYLDTTYM 407
Cdd:cd07735 141 EYPIALTGLSVTAFPVSHgVPVSTAFLIR-DGGDSFLFFGDT--GPDSVSksprLDALWRAlaplipKKLKAIIIECSFP 217


                .
gi 21357063 408 N 408
Cdd:cd07735 218 N 218
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 290-406 1.25e-05

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: 47.11  E-value: 1.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 290 HYFLTHFHADHYIGLTkkFCHPLYV--------------SPISARLVRTF------IKLDE----THIHEIDVDQTLDVD 345
Cdd:cd07715  60 HLLLSHTHWDHIQGFP--FFAPAYDpgnrihiygphkdgGSLEEVLRRQMsppyfpVPLEEllaaIEFHDLEPGEPFSIG 137

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21357063 346 GVQVTALEANHCPGALMFFFKlSSGECILHTGD----FRASADMESLPIFWNHSniDLLYLDTTY 406
Cdd:cd07715 138 GVTVTTIPLNHPGGALGYRIE-EDGKSVVYATDtehyPDDGESDEALLEFARGA--DLLIHDAQY 199
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 281-378 4.53e-05

uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. Members of this bacterial subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 44.74  E-value: 4.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 281 QFGEIEGVTHYFLTHFHADHY-----------IGLTKKFCH--PLYVSPISARLVRTFIKL-DETHIHEIDVDQTLDVDG 346
Cdd:cd07716  44 RYIDPEDLDAVVLSHLHPDHCadlgvlqyarrYHPRGARKPplPLYGPAGPAERLAALYGLeDVFDFHPIEPGEPLEIGP 123

                        90       100       110
                ....*....|....*....|....*....|....
gi 21357063 347 VQVTALEANH-CPGALMfffKLSSGE-CILHTGD 378
Cdd:cd07716 124 FTITFFRTVHpVPCYAM---RIEDGGkVLVYTGD 154
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 285-356 5.50e-05

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: 44.61  E-value: 5.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063   285 IEGVthyFLTHFHADHYIGLT--KKFC-HPLYVSP-ISARLVRTFIKL-----DETHIHEIDVDQTLDVD--GVQVTALE 353
Cdd:pfam12706  29 IDAV---LLTHDHYDHLAGLLdlREGRpRPLYAPLgVLAHLRRNFPYLfllehYGVRVHEIDWGESFTVGdgGLTVTATP 105


                  ...
gi 21357063   354 ANH 356
Cdd:pfam12706 106 ARH 108
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 292-358 1.19e-04

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: 43.62  E-value: 1.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 292 FLTHFHADHYIGLT--KKFCH------PLYVSPIS-ARLVRTFIKLDET---------HIHEIDVDQTLDVDGVQVTALE 353
Cdd:cd16279  71 LLTHAHADHIHGLDdlRPFNRlqqrpiPVYASEETlDDLKRRFPYFFAAtggggvpklDLHIIEPDEPFTIGGLEITPLP 150


                ....*
gi 21357063 354 ANHCP 358
Cdd:cd16279 151 VLHGK 155
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 279-378 5.12e-04

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: 41.90  E-value: 5.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357063 279 GFQFGEIEGVthyFLTHFHADHyIGLTKKFCHplyvspisaRLVRTFIKLDEThihEIDVDQTLDVDGVQVTALEA-NHC 357
Cdd:cd07725  50 GLKPSDIDRV---LLTHHHPDH-IGLAGKLQE---------KSGATVYILDVT---PVKDGDKIDLGGLRLKVIETpGHT 113

                        90       100
                ....*....|....*....|.
gi 21357063 358 PGALMFFFklsSGECILHTGD 378
Cdd:cd07725 114 PGHIVLYD---EDRRELFVGD 131
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 288-359 4.59e-03

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: 38.67  E-value: 4.59e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21357063 288 VTHYFLTHFHADHyIGLTKKFCH----PLYVSPISARlvrtFIKLDETHIHEIDVDQTLDVDGVQVTALeanHCPG 359
Cdd:cd16275  48 LTGILLTHSHFDH-VNLVEPLLAkydaPVYMSKEEID----YYGFRCPNLIPLEDGDTIKIGDTEITCL---LTPG 115
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 284-352 6.49e-03

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 39.07  E-value: 6.49e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21357063 284 EIEGVthyFLTHFHADHYIGLT--------KKFCHPLYVSPISA-RLVRTFIKLDETHIHEIDVDQTLDVDGVQVTAL 352
Cdd:COG2333  52 RLDLL---VLTHPDADHIGGLAavleafpvGRVLVSGPPDTSETyERLLEALKEKGIPVRPCRAGDTWQLGGVRFEVL 126
 
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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