NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1940735536|gb|KAG0010020|]
View 

DNA break repair nuclease [Entomortierella chlamydospora]

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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; ...
 348-507 1.87e-94

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: 291.37  E-value: 1.87e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 348 KKFKPKASKPCPFYKKLPDTSFTVDAFCYGAIDGCDVYFLSHFHSDHYGGLTSSWNHGPIYCSSITANLVISRLNVDPQY 427
Cdd:cd16273     3 SKKKPKRKKPCPFYKIIPGTSFVVDAFKYGKIPGISAYFLSHFHSDHYGGLTKSWSHGPIYCSEITANLVKLKLKVDEEY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 428 VKRLPMYEPT-IVNGVTVRLMDANHCPGSVLFVFDLQNpQRRYLHTGDFRACREMVSHPVLRQPSntPIDILYLDTTYIN 506
Cdd:cd16273    83 IVVLPMNTPVeIDGDVSVTLLDANHCPGAVMFLFELPD-GRRILHTGDFRANPEMLEHPLLLGKR--RIDTVYLDTTYCN 159


                  .
gi 1940735536 507 P 507
Cdd:cd16273   160 P 160
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 633-763 1.06e-31

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: 119.30  E-value: 1.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 633 PELSEMLTSNRLEAQVHLVHMGsEMSPENLQDYLDSLSPTFTRLIAIRPTGWTFtggtkkytpgnggsvnaddqvqATPT 712
Cdd:pfam07522   1 PEILSLLTTDPLSTQIHVVPMP-KLSYEALLDYLTARKDHFDSVLAIRPTGWTY----------------------RPPK 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1940735536 713 PTALELKPSFTSSTIKIYPVPYSEHSSFNELAGFVRSLDIVKIIPTVGVGS 763
Cdd:pfam07522  58 TEVSDRIGPSIRGRITIYGVPYSEHSSFDELKEFVQFLRPKKIIPTVNVGG 108
MSCRAMM_ClfA super family cl41352
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 40-252 8.57e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


The actual alignment was detected with superfamily member NF033609:

Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 39.89  E-value: 8.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536  40 SDPLFDptTGADRQNSNIPAATAADATTEPASISVSQQDFAQHnqlSKYFTDSEACiipTKSSEPQEPLSVPDYEDQNER 119
Cdd:NF033609  563 SDPGSD--SGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASD---SDSASDSDSA---SDSDSASDSDSASDSDSASDS 634

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 120 SVQENDHSETDGTSSAFFAEAPERICHSSITSGTTNDTAEPKQTDGCVNGCYEGPS-ALKDVEHDGTKAVEKSSNSVLCH 198
Cdd:NF033609  635 DSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDS 714

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1940735536 199 QPQADPYSDSIRDLNPDSEFDEGIESGEFPDIDEIQDCDFD-DFQEGTESTLNAD 252
Cdd:NF033609  715 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSD 769
 
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; ...
 348-507 1.87e-94

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: 291.37  E-value: 1.87e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 348 KKFKPKASKPCPFYKKLPDTSFTVDAFCYGAIDGCDVYFLSHFHSDHYGGLTSSWNHGPIYCSSITANLVISRLNVDPQY 427
Cdd:cd16273     3 SKKKPKRKKPCPFYKIIPGTSFVVDAFKYGKIPGISAYFLSHFHSDHYGGLTKSWSHGPIYCSEITANLVKLKLKVDEEY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 428 VKRLPMYEPT-IVNGVTVRLMDANHCPGSVLFVFDLQNpQRRYLHTGDFRACREMVSHPVLRQPSntPIDILYLDTTYIN 506
Cdd:cd16273    83 IVVLPMNTPVeIDGDVSVTLLDANHCPGAVMFLFELPD-GRRILHTGDFRANPEMLEHPLLLGKR--RIDTVYLDTTYCN 159


                  .
gi 1940735536 507 P 507
Cdd:cd16273   160 P 160
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 633-763 1.06e-31

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: 119.30  E-value: 1.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 633 PELSEMLTSNRLEAQVHLVHMGsEMSPENLQDYLDSLSPTFTRLIAIRPTGWTFtggtkkytpgnggsvnaddqvqATPT 712
Cdd:pfam07522   1 PEILSLLTTDPLSTQIHVVPMP-KLSYEALLDYLTARKDHFDSVLAIRPTGWTY----------------------RPPK 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1940735536 713 PTALELKPSFTSSTIKIYPVPYSEHSSFNELAGFVRSLDIVKIIPTVGVGS 763
Cdd:pfam07522  58 TEVSDRIGPSIRGRITIYGVPYSEHSSFDELKEFVQFLRPKKIIPTVNVGG 108
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 386-527 7.08e-10

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 61.74  E-value: 7.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 386 FLSHFHSDHYGG---LTSSWNHGPIYCSSITANLVISRL-----------NVDPQY-----------VKRLPMYEPTIVN 440
Cdd:COG1236    55 VLTHAHLDHSGAlplLVKEGFRGPIYATPATADLARILLgdsakiqeeeaEAEPLYteedaeralelFQTVDYGEPFEIG 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 441 GVTVRLMDANHCPGSVLFVFDLQNpqRRYLHTGDFraCREmvSHPVLRQPS-NTPIDILYLDTTYINPRYtfPSQDLVIK 519
Cdd:COG1236   135 GVRVTFHPAGHILGSAQVELEVGG--KRIVFSGDY--GRE--DDPLLAPPEpVPPADVLITESTYGDRLH--PPREEVEA 206


                  ....*...
gi 1940735536 520 EVANLVSR 527
Cdd:COG1236   207 ELAEWVRE 214
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 386-475 6.96e-08

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: 52.94  E-value: 6.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536  386 FLSHFHSDHYGGLTS--SWNHGPIYCSSITANLVISRLNVDPQYVKRLPMYEPTIV--NGVTVRLMD--------ANHCP 453
Cdd:smart00849  40 ILTHGHPDHIGGLPEllEAPGAPVYAPEGTAELLKDLLALLGELGAEAEPAPPDRTlkDGDELDLGGgelevihtPGHTP 119

                           90       100
                   ....*....|....*....|..
gi 1940735536  454 GSVLFVFdlqnPQRRYLHTGDF 475
Cdd:smart00849 120 GSIVLYL----PEGKILFTGDL 137
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
386-475 2.92e-04

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 42.74  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 386 FLSHFHSDHYGG---LTSSWNHGPIYCSSITANLVISRLNVDPQYVKRLPMYEPTIVNGVTVR--------------LMD 448
Cdd:pfam00753  48 ILTHGHFDHIGGlgeLAEATDVPVIVVAEEARELLDEELGLAASRLGLPGPPVVPLPPDVVLEegdgilggglgllvTHG 127

                          90       100
                  ....*....|....*....|....*..
gi 1940735536 449 ANHCPGSVLFVFdlqnPQRRYLHTGDF 475
Cdd:pfam00753 128 PGHGPGHVVVYY----GGGKVLFTGDL 150
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 40-252 8.57e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 39.89  E-value: 8.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536  40 SDPLFDptTGADRQNSNIPAATAADATTEPASISVSQQDFAQHnqlSKYFTDSEACiipTKSSEPQEPLSVPDYEDQNER 119
Cdd:NF033609  563 SDPGSD--SGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASD---SDSASDSDSA---SDSDSASDSDSASDSDSASDS 634

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 120 SVQENDHSETDGTSSAFFAEAPERICHSSITSGTTNDTAEPKQTDGCVNGCYEGPS-ALKDVEHDGTKAVEKSSNSVLCH 198
Cdd:NF033609  635 DSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDS 714

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1940735536 199 QPQADPYSDSIRDLNPDSEFDEGIESGEFPDIDEIQDCDFD-DFQEGTESTLNAD 252
Cdd:NF033609  715 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSD 769
 
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; ...
 348-507 1.87e-94

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: 291.37  E-value: 1.87e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 348 KKFKPKASKPCPFYKKLPDTSFTVDAFCYGAIDGCDVYFLSHFHSDHYGGLTSSWNHGPIYCSSITANLVISRLNVDPQY 427
Cdd:cd16273     3 SKKKPKRKKPCPFYKIIPGTSFVVDAFKYGKIPGISAYFLSHFHSDHYGGLTKSWSHGPIYCSEITANLVKLKLKVDEEY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 428 VKRLPMYEPT-IVNGVTVRLMDANHCPGSVLFVFDLQNpQRRYLHTGDFRACREMVSHPVLRQPSntPIDILYLDTTYIN 506
Cdd:cd16273    83 IVVLPMNTPVeIDGDVSVTLLDANHCPGAVMFLFELPD-GRRILHTGDFRANPEMLEHPLLLGKR--RIDTVYLDTTYCN 159


                  .
gi 1940735536 507 P 507
Cdd:cd16273   160 P 160
SNM1A-like_MBL-fold cd16298
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ...
 352-507 3.88e-63

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: 208.52  E-value: 3.88e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 352 PKASKPCPFYKKLPDTSFTVDAFCYGAIDGCDVYFLSHFHSDHYGGLTSSWNHgPIYCSSITANLVISRLNVDPQYVKRL 431
Cdd:cd16298     7 GKRKKTCPFYKKIPGTGFTVDAFQYGVIEGCTAYFLTHFHSDHYCGLTKKFKF-PIYCSKITGNLVKSKLKVEEQYINVL 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1940735536 432 PMYEPTIVNGVTVRLMDANHCPGSVLFVFDLQNpQRRYLHTGDFRACREMVSHPVLRqpsNTPIDILYLDTTYINP 507
Cdd:cd16298    86 PMNTECIVNGVKVVLLDANHCPGAVMILFRLPS-GTLVLHTGDFRADPSMERYPELI---GQKIHTLYLDTTYCSP 157
DRMBL pfam07522
DNA repair metallo-beta-lactamase; The metallo-beta-lactamase fold contains five sequence ...
 633-763 1.06e-31

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: 119.30  E-value: 1.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 633 PELSEMLTSNRLEAQVHLVHMGsEMSPENLQDYLDSLSPTFTRLIAIRPTGWTFtggtkkytpgnggsvnaddqvqATPT 712
Cdd:pfam07522   1 PEILSLLTTDPLSTQIHVVPMP-KLSYEALLDYLTARKDHFDSVLAIRPTGWTY----------------------RPPK 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1940735536 713 PTALELKPSFTSSTIKIYPVPYSEHSSFNELAGFVRSLDIVKIIPTVGVGS 763
Cdd:pfam07522  58 TEVSDRIGPSIRGRITIYGVPYSEHSSFDELKEFVQFLRPKKIIPTVNVGG 108
artemis-SNM1C-like_MBL-fold cd16297
artemis-SNM1C and related proteins; MBL-fold metallo-hydrolase domain; Includes the nuclease ...
 385-507 4.03e-13

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: 67.92  E-value: 4.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 385 YFLSHFHSDHYGGLtsswnHGP-------------IYCSSITANLVISrlnvDPQY------VKRLPMYEPT---IVNGV 442
Cdd:cd16297    29 YFLSHCHKDHMKGL-----RAPglkrrlkaslkvkLYCSPVTKELLLT----NPKYafwenhIVSLEIDTPTqisLVDEA 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1940735536 443 T-------VRLMDANHCPGSVLFVFdlQNPQRRYLHTGDFRACREMVSHPVLRQPSNTPIDI--LYLDTTYINP 507
Cdd:cd16297   100 TgekedvvVTLLPAGHCPGSVMFLF--QGNNGTVLYTGDFRLAVGEAARMELLHSGDRVKDIqsVYLDTTFCDP 171
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 386-527 7.08e-10

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 61.74  E-value: 7.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 386 FLSHFHSDHYGG---LTSSWNHGPIYCSSITANLVISRL-----------NVDPQY-----------VKRLPMYEPTIVN 440
Cdd:COG1236    55 VLTHAHLDHSGAlplLVKEGFRGPIYATPATADLARILLgdsakiqeeeaEAEPLYteedaeralelFQTVDYGEPFEIG 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 441 GVTVRLMDANHCPGSVLFVFDLQNpqRRYLHTGDFraCREmvSHPVLRQPS-NTPIDILYLDTTYINPRYtfPSQDLVIK 519
Cdd:COG1236   135 GVRVTFHPAGHILGSAQVELEVGG--KRIVFSGDY--GRE--DDPLLAPPEpVPPADVLITESTYGDRLH--PPREEVEA 206


                  ....*...
gi 1940735536 520 EVANLVSR 527
Cdd:COG1236   207 ELAEWVRE 214
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 386-475 6.96e-08

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: 52.94  E-value: 6.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536  386 FLSHFHSDHYGGLTS--SWNHGPIYCSSITANLVISRLNVDPQYVKRLPMYEPTIV--NGVTVRLMD--------ANHCP 453
Cdd:smart00849  40 ILTHGHPDHIGGLPEllEAPGAPVYAPEGTAELLKDLLALLGELGAEAEPAPPDRTlkDGDELDLGGgelevihtPGHTP 119

                           90       100
                   ....*....|....*....|..
gi 1940735536  454 GSVLFVFdlqnPQRRYLHTGDF 475
Cdd:smart00849 120 GSIVLYL----PEGKILFTGDL 137
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 386-476 1.97e-07

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: 52.79  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 386 FLSHFHSDHYGGLTSSWNHG--PIYCSSITANLVISRLN----VDPQYVKRLPMYEPTIVNGVTVRLMDANHC-PGSVLF 458
Cdd:cd07714    60 FITHGHEDHIGALPYLLPELnvPIYATPLTLALIKKKLEefklIKKVKLNEIKPGERIKLGDFEVEFFRVTHSiPDSVGL 139

                          90
                  ....*....|....*...
gi 1940735536 459 VFdlQNPQRRYLHTGDFR 476
Cdd:cd07714   140 AI--KTPEGTIVHTGDFK 155
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 386-498 5.59e-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: 50.92  E-value: 5.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 386 FLSHFHSDHYGG---LTSSWNHGPIYCSSITANLV--------------ISRLNVDPQY-----------VKRLPMYEPT 437
Cdd:cd16295    56 ILTHAHLDHSGRlplLVKEGFRGPIYATPATKDLAelllldsakiqeeeAEHPPAEPLYteedvekalkhFRPVEYGEPF 135

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1940735536 438 -IVNGVTVRLMDANHCPGSVLFVFDLQNPqRRYLHTGDFraCREmvSHPVLRQPSNTP-IDIL 498
Cdd:cd16295   136 eIGPGVKVTFYDAGHILGSASVELEIGGG-KRILFSGDL--GRK--NTPLLRDPAPPPeADYL 193
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
386-504 4.79e-06

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 48.65  E-value: 4.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 386 FLSHFHSDHYGGLT----SSWNHG-----PIYCSSITANLV---ISRLNVDPQY---VKRLPMYEPTIVNGVTVRLMDAN 450
Cdd:COG1234    57 FITHLHGDHIAGLPgllsTRSLAGrekplTIYGPPGTKEFLealLKASGTDLDFpleFHEIEPGEVFEIGGFTVTAFPLD 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1940735536 451 HCPGSVLFVFDLqnPQRRYLHTGDFRACREMVshPVLRQPsntpiDILYLDTTY 504
Cdd:COG1234   137 HPVPAYGYRFEE--PGRSLVYSGDTRPCEALV--ELAKGA-----DLLIHEATF 181
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 386-477 1.57e-05

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: 46.45  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 386 FLSHFHSDHYgGLTSSWNHG-PIYCSSITANLVISRLNVDPQYVKRLPMYEP-----TIVNG---VTVRLMDanH-CPGS 455
Cdd:cd07732    80 LLSHAHLDHY-GLLNYLRPDiPVYMGEATKRILKALLPFFGEGDPVPRNIRVfesgkSFTIGdftVTPYLVD--HsAPGA 156

                          90       100
                  ....*....|....*....|..
gi 1940735536 456 VLFVfdLQNPQRRYLHTGDFRA 477
Cdd:cd07732   157 YAFL--IEAPGKRIFYTGDFRF 176
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 386-474 4.75e-05

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: 45.45  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 386 FLSHFHSDHYGG---LTSSWNhGPIYCSSITANLVISRlnvDPQYVKRLPMYEPTI---------VNGVTVRLMDAN-HC 452
Cdd:COG0491    56 LLTHLHPDHVGGlaaLAEAFG-APVYAHAAEAEALEAP---AAGALFGREPVPPDRtledgdtleLGGPGLEVIHTPgHT 131

                          90       100
                  ....*....|....*....|..
gi 1940735536 453 PGSVLFVFdlqnPQRRYLHTGD 474
Cdd:COG0491   132 PGHVSFYV----PDEKVLFTGD 149
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 386-507 6.22e-05

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 45.27  E-value: 6.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 386 FLSHFHSDHYGGLTS-----SWNHGPIYCSSITANLVISRLNVDPQY------VKRLPMYEPTIVNGVTVRLMDANH-CP 453
Cdd:COG1235    73 LLTHEHADHIAGLDDlrpryGPNPIPVYATPGTLEALERRFPYLFAPypgkleFHEIEPGEPFEIGGLTVTPFPVPHdAG 152

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1940735536 454 GSVLFVFDlqNPQRRYLHTGDFracrEMVSHPVLRQPSNtpIDILYLDTTYINP 507
Cdd:COG1235   153 DPVGYRIE--DGGKKLAYATDT----GYIPEEVLELLRG--ADLLILDATYDDP 198
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 386-475 9.38e-05

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: 44.20  E-value: 9.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 386 FLSHFHSDHYGGLT--SSWNHGPIYCSSITANLVIS-RLNVDPQYVKRLPMYEPTI---------VNGVTVRLMDA-NHC 452
Cdd:cd06262    50 LLTHGHFDHIGGLAelKEAPGAPVYIHEADAELLEDpELNLAFFGGGPLPPPEPDIlledgdtieLGGLELEVIHTpGHT 129

                          90       100
                  ....*....|....*....|...
gi 1940735536 453 PGSVLFVFdlqnPQRRYLHTGDF 475
Cdd:cd06262   130 PGSVCFYI----EEEGVLFTGDT 148
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
386-475 2.92e-04

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 42.74  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 386 FLSHFHSDHYGG---LTSSWNHGPIYCSSITANLVISRLNVDPQYVKRLPMYEPTIVNGVTVR--------------LMD 448
Cdd:pfam00753  48 ILTHGHFDHIGGlgeLAEATDVPVIVVAEEARELLDEELGLAASRLGLPGPPVVPLPPDVVLEegdgilggglgllvTHG 127

                          90       100
                  ....*....|....*....|....*..
gi 1940735536 449 ANHCPGSVLFVFdlqnPQRRYLHTGDF 475
Cdd:pfam00753 128 PGHGPGHVVVYY----GGGKVLFTGDL 150
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
386-476 4.43e-04

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 43.51  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 386 FLSHFHSDHYGGLTSSWNHG--PIYCSSITANLVISRL---NVDPQyVKRLPMYEPTIVN--GVTVRLMDANH-CPGSVL 457
Cdd:COG0595    68 VLTHGHEDHIGALPYLLKELnvPVYGTPLTLALLEAKLkehGLLKK-VKLHVVKPGDRIKfgPFKVEFFRVTHsIPDSLG 146

                          90
                  ....*....|....*....
gi 1940735536 458 FVFdlQNPQRRYLHTGDFR 476
Cdd:COG0595   147 LAI--RTPAGTIVHTGDFK 163
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 379-461 1.73e-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: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 379 IDGCdvyFLSHFHSDHYGGLT--SSWN-----HGPIYCSSITANLVISRLNVDPQY----------VKRLPMYEPTIVNG 441
Cdd:cd16279    67 LDAV---LLTHAHADHIHGLDdlRPFNrlqqrPIPVYASEETLDDLKRRFPYFFAAtggggvpkldLHIIEPDEPFTIGG 143

                          90       100
                  ....*....|....*....|.
gi 1940735536 442 VTVRLMDANHCPGSVL-FVFD 461
Cdd:cd16279   144 LEITPLPVLHGKLPSLgFRFG 164
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 386-480 2.22e-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: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 386 FLSHFHSDHYGGLTS---SWNHGP------IYCSSITANLV---------ISRLNVDPQYVKRLPMYEPTIVNGVTVRLM 447
Cdd:cd16272    55 FLSHFHLDHIGGLPTllfARRYGGrkkpltIYGPKGIKEFLekllnfpveILPLGFPLEIEELEEGGEVLELGDLKVEAF 134

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1940735536 448 DANHCPGSVLFVFDLQNPQRRYlhTGDFRACRE 480
Cdd:cd16272   135 PVKHSVESLGYRIEAEGKSIVY--SGDTGPCEN 165
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 40-252 8.57e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 39.89  E-value: 8.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536  40 SDPLFDptTGADRQNSNIPAATAADATTEPASISVSQQDFAQHnqlSKYFTDSEACiipTKSSEPQEPLSVPDYEDQNER 119
Cdd:NF033609  563 SDPGSD--SGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASD---SDSASDSDSA---SDSDSASDSDSASDSDSASDS 634

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 120 SVQENDHSETDGTSSAFFAEAPERICHSSITSGTTNDTAEPKQTDGCVNGCYEGPS-ALKDVEHDGTKAVEKSSNSVLCH 198
Cdd:NF033609  635 DSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDS 714

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1940735536 199 QPQADPYSDSIRDLNPDSEFDEGIESGEFPDIDEIQDCDFD-DFQEGTESTLNAD 252
Cdd:NF033609  715 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSD 769
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 384-475 9.51e-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: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 37.95  E-value: 9.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940735536 384 VYflSHFHSDHYGGlTSSWN-HGPIYCSS-ITANLVISRLnvDPqyvkRLPMyePTI---------VNGVTVRLM--DAN 450
Cdd:cd16276    50 VY--SHNHADHIGG-ASIFKdEGATIIAHeATAELLKRNP--DP----KRPV--PTVtfddeytleVGGQTLELSyfGPN 118

                          90       100
                  ....*....|....*....|....*
gi 1940735536 451 HCPGSVLFVFdlqnPQRRYLHTGDF 475
Cdd:cd16276   119 HGPGNIVIYL----PKQKVLMAVDL 139
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH