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Conserved domains on  [gi|528518577|ref|XP_005166266|]
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integrator complex subunit 11 isoform X1 [Danio rerio]

Protein Classification

INTS11 family MBL fold metallo-hydrolase( domain architecture ID 11440945)

INTS11 family MBL fold metallo-hydrolase similar to metazoan Integrator complex subunit 11, which is part of the complex that is implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing

CATH:  3.60.15.10
EC:  3.-.-.-
Gene Ontology:  GO:0032039|GO:0004521|GO:0034243|GO:0016180
PubMed:  17597585|12177301|11471246|11513844
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 6-204 4.87e-161

Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a metazoan-specific multisubunit, multifunctional protein complex composed of 14 subunits named Int1-Int14 (Integrator subunits). This subgroup includes Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)). Integrator complex has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


:

Pssm-ID: 293849  Cd Length: 199  Bit Score: 457.88  E-value: 4.87e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   6 VTPLGAGQDVGRSCILVSIGGKNIMLDCGMHMGFNDDRRFPDFSYITQNGRLTEFLDCVIISHFHLDHCGALPYMSEMVG 85
Cdd:cd16291    1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  86 YDGPIYMTHPTKAICPILLEDFRKITVDKKGETNFFTSQMIKDCMKKVVPLNLHQTVQVDDELEIKAYYAGHVLGAAMVQ 165
Cdd:cd16291   81 YDGPIYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFY 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 528518577 166 IKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPDILISES 204
Cdd:cd16291  161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 5-416 1.05e-119

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


:

Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 360.27  E-value: 1.05e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   5 KVTPLGAGQDVGRSCILVSIGGKNIMLDCGMHMGFnDDRRFPDFsyitqnGRLTEFLDCVIISHFHLDHCGALPYMSEMv 84
Cdd:COG1236    2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGG-KERNWPPF------PFRPSDVDAVVLTHAHLDHSGALPLLVKE- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  85 GYDGPIYMTHPTKAICPILLEDFRKITVDKKGETNFFTSQMIKDCMKKVVPLNLHQTVQVDDeLEIKAYYAGHVLGAAMV 164
Cdd:COG1236   74 GFRGPIYATPATADLARILLGDSAKIQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577 165 QIKVGSESVVYTGDYNMTPDR-HLGAAWIDKCrpDILISESTYATTIRDSKRCRERDFLKKVHETVERGGKVLIPVFALG 243
Cdd:COG1236  153 ELEVGGKRIVFSGDYGREDDPlLAPPEPVPPA--DVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALG 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577 244 RAQE-LCILLETFWERMNLKAPIYFStGLTEKANHYYKLFITWTNQKIRKTFVQRNmfeFKHIKAFDRSYADN-PGPMVV 321
Cdd:COG1236  231 RAQElLYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHGEYLRDEAQDPFALPN---LRFVTSVEESKALNrKGPAII 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577 322 FATPGMLHAGQSLQIFKKWAGNEKNMVIMPGYCVQGTVGHKILNGQKKLEMEGRaTLDVKLQVE-YMSFSAHADAKGIMQ 400
Cdd:COG1236  307 IAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIFGE-EVPVRARVErLFGLSAHADWDELLE 385

                        410
                 ....*....|....*..
gi 528518577 401 LIR-MAEPRNMLLVHGE 416
Cdd:COG1236  386 WIKaTGKPERVFLVHGE 402
 
Name Accession Description Interval E-value
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 6-204 4.87e-161

Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a metazoan-specific multisubunit, multifunctional protein complex composed of 14 subunits named Int1-Int14 (Integrator subunits). This subgroup includes Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)). Integrator complex has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293849  Cd Length: 199  Bit Score: 457.88  E-value: 4.87e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   6 VTPLGAGQDVGRSCILVSIGGKNIMLDCGMHMGFNDDRRFPDFSYITQNGRLTEFLDCVIISHFHLDHCGALPYMSEMVG 85
Cdd:cd16291    1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  86 YDGPIYMTHPTKAICPILLEDFRKITVDKKGETNFFTSQMIKDCMKKVVPLNLHQTVQVDDELEIKAYYAGHVLGAAMVQ 165
Cdd:cd16291   81 YDGPIYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFY 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 528518577 166 IKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPDILISES 204
Cdd:cd16291  161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 5-416 1.05e-119

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 360.27  E-value: 1.05e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   5 KVTPLGAGQDVGRSCILVSIGGKNIMLDCGMHMGFnDDRRFPDFsyitqnGRLTEFLDCVIISHFHLDHCGALPYMSEMv 84
Cdd:COG1236    2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGG-KERNWPPF------PFRPSDVDAVVLTHAHLDHSGALPLLVKE- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  85 GYDGPIYMTHPTKAICPILLEDFRKITVDKKGETNFFTSQMIKDCMKKVVPLNLHQTVQVDDeLEIKAYYAGHVLGAAMV 164
Cdd:COG1236   74 GFRGPIYATPATADLARILLGDSAKIQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577 165 QIKVGSESVVYTGDYNMTPDR-HLGAAWIDKCrpDILISESTYATTIRDSKRCRERDFLKKVHETVERGGKVLIPVFALG 243
Cdd:COG1236  153 ELEVGGKRIVFSGDYGREDDPlLAPPEPVPPA--DVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALG 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577 244 RAQE-LCILLETFWERMNLKAPIYFStGLTEKANHYYKLFITWTNQKIRKTFVQRNmfeFKHIKAFDRSYADN-PGPMVV 321
Cdd:COG1236  231 RAQElLYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHGEYLRDEAQDPFALPN---LRFVTSVEESKALNrKGPAII 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577 322 FATPGMLHAGQSLQIFKKWAGNEKNMVIMPGYCVQGTVGHKILNGQKKLEMEGRaTLDVKLQVE-YMSFSAHADAKGIMQ 400
Cdd:COG1236  307 IAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIFGE-EVPVRARVErLFGLSAHADWDELLE 385

                        410
                 ....*....|....*..
gi 528518577 401 LIR-MAEPRNMLLVHGE 416
Cdd:COG1236  386 WIKaTGKPERVFLVHGE 402
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 245-363 3.81e-42

Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains.


Pssm-ID: 214983 [Multi-domain]  Cd Length: 126  Bit Score: 147.69  E-value: 3.81e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   245 AQELCILLETFWERMNL-KAPIYFSTGLTEKANHYYKLFITWTNQKIRKTFVQ-RNMFEFKHIKAFD-----RSYADNPG 317
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKsleesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 528518577   318 PMVVFATPGMLHAGQSLQIFKKWAGNEKNMVIMPGYCVQGTVGHKI 363
Cdd:smart01027  81 PKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 245-361 1.51e-29

Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains.


Pssm-ID: 463203  Cd Length: 109  Bit Score: 112.61  E-value: 1.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  245 AQELCILLETFWER-MNLKAPIYFSTGLTEKANHYYKLFITWTNQKIRKTfvqrnmfefkhIKAFDRSYADN--PGPMVV 321
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHF-----------VISKSESKAINegKGPKVI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 528518577  322 FATPGMLHAGQSLQIFKKWAGNEKNMVIMPGYCVQGTVGH 361
Cdd:pfam10996  70 IASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 21-201 2.24e-17

Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase superfamily.


Pssm-ID: 406948  Cd Length: 192  Bit Score: 80.72  E-value: 2.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   21 LVSIGGKNIMLDCGmhmgFNDDRRFPDFSYITQNgrLTEFLDCVIISHFHLDHCGALPYM----SEMVGYDGPIYMTHPT 96
Cdd:pfam16661   1 LLEFDNVRILLDPG----WDGSFSYESDLKYLEK--ILPEVDLILLSHPTLEHLGAYPLLyykfGSHLGSNIPVYATLPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   97 KAICPI-LLEDFRKITVDKKGETNFFTSQMIKDCMKKVVPLNLHQTVQV---DDELEIKAYYAGHVLGAAMVQIKVGSES 172
Cdd:pfam16661  75 ANLGRVsTYDLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkFDGLTITPYNSGHTLGGTIWKISKNSEK 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 528518577  173 VVYTGDYNMTPDRHL-GAAWIDKC--------RPDILI 201
Cdd:pfam16661 155 IVYAVDWNHTKDSHLnGASLLDSTgkpleslvRPTALI 192
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 18-184 1.40e-14

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: 72.20  E-value: 1.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577    18 SCILVSIGGKNIMLDCGMHMGFNDDRRFPDFSYITqngrltefLDCVIISHFHLDHCGALPYMSEMvgYDGPIYMTHPTK 97
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKK--------IDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577    98 AicpiLLEDFRKITVDKKGetnfftsqmIKDCMKKVVPLNLHQTVQVDDElEIKAYYA-GHVLGAAMVqiKVGSESVVYT 176
Cdd:smart00849  71 E----LLKDLLALLGELGA---------EAEPAPPDRTLKDGDELDLGGG-ELEVIHTpGHTPGSIVL--YLPEGKILFT 134


                   ....*...
gi 528518577   177 GDYNMTPD 184
Cdd:smart00849 135 GDLLFAGG 142
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
4-207 4.22e-14

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 72.54  E-value: 4.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   4 IKVTPLGAG---QDVGR--SCILVSIGGKNIMLDCG-------MHMGFNDDRrfpdfsyitqngrltefLDCVIISHFHL 71
Cdd:COG1234    1 MKLTFLGTGgavPTPGRatSSYLLEAGGERLLIDCGegtqrqlLRAGLDPRD-----------------IDAIFITHLHG 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  72 DHCGALPYMSEMVGYDG-----PIYMTHPTKAIcpilLEDFRKITvdkKGETNFFTsqmikdcmkKVVPLNLHQTVQVDD 146
Cdd:COG1234   64 DHIAGLPGLLSTRSLAGrekplTIYGPPGTKEF----LEALLKAS---GTDLDFPL---------EFHEIEPGEVFEIGG 127

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528518577 147 eLEIKAYYAGHVLGAAMVQIKVGSESVVYTGD--YNmtpdrhlgAAWIDKCR-PDILISESTYA 207
Cdd:COG1234  128 -FTVTAFPLDHPVPAYGYRFEEPGRSLVYSGDtrPC--------EALVELAKgADLLIHEATFL 182
PRK00055 PRK00055
ribonuclease Z; Reviewed
 4-217 2.64e-05

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 46.33  E-value: 2.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   4 IKVTPLGAGQ---DVGR--SCILVSIGGKNIMLDCG-------MHMGFnddrRFPDFSYItqngrlteFldcviISHFHL 71
Cdd:PRK00055   2 MELTFLGTGSgvpTPTRnvSSILLRLGGELFLFDCGegtqrqlLKTGI----KPRKIDKI--------F-----ITHLHG 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  72 DHCGALPYMSEMVGYDGpiyMTHPTKAICPILLEDF----RKIT------VDKKGETNFFTSQMIKDCMKKVVPL--NLH 139
Cdd:PRK00055  65 DHIFGLPGLLSTRSLSG---RTEPLTIYGPKGIKEFvetlLRASgslgyrIAEKDKPGKLDAEKLKALGVPPGPLfgKLK 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577 140 --QTVQVDDeleikayyaGHVLGAAMVqikVGSE----SVVYTGDynmT-PDRHLgAAWIDKCrpDILISESTYATTIRD 212
Cdd:PRK00055 142 rgEDVTLED---------GRIINPADV---LGPPrkgrKVAYCGD---TrPCEAL-VELAKGA--DLLVHEATFGDEDEE 203


                 ....*
gi 528518577 213 SKRCR 217
Cdd:PRK00055 204 LAKEY 208
 
Name Accession Description Interval E-value
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 6-204 4.87e-161

Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a metazoan-specific multisubunit, multifunctional protein complex composed of 14 subunits named Int1-Int14 (Integrator subunits). This subgroup includes Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)). Integrator complex has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293849  Cd Length: 199  Bit Score: 457.88  E-value: 4.87e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   6 VTPLGAGQDVGRSCILVSIGGKNIMLDCGMHMGFNDDRRFPDFSYITQNGRLTEFLDCVIISHFHLDHCGALPYMSEMVG 85
Cdd:cd16291    1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  86 YDGPIYMTHPTKAICPILLEDFRKITVDKKGETNFFTSQMIKDCMKKVVPLNLHQTVQVDDELEIKAYYAGHVLGAAMVQ 165
Cdd:cd16291   81 YDGPIYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFY 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 528518577 166 IKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPDILISES 204
Cdd:cd16291  161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 5-416 1.05e-119

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 360.27  E-value: 1.05e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   5 KVTPLGAGQDVGRSCILVSIGGKNIMLDCGMHMGFnDDRRFPDFsyitqnGRLTEFLDCVIISHFHLDHCGALPYMSEMv 84
Cdd:COG1236    2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGG-KERNWPPF------PFRPSDVDAVVLTHAHLDHSGALPLLVKE- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  85 GYDGPIYMTHPTKAICPILLEDFRKITVDKKGETNFFTSQMIKDCMKKVVPLNLHQTVQVDDeLEIKAYYAGHVLGAAMV 164
Cdd:COG1236   74 GFRGPIYATPATADLARILLGDSAKIQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577 165 QIKVGSESVVYTGDYNMTPDR-HLGAAWIDKCrpDILISESTYATTIRDSKRCRERDFLKKVHETVERGGKVLIPVFALG 243
Cdd:COG1236  153 ELEVGGKRIVFSGDYGREDDPlLAPPEPVPPA--DVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALG 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577 244 RAQE-LCILLETFWERMNLKAPIYFStGLTEKANHYYKLFITWTNQKIRKTFVQRNmfeFKHIKAFDRSYADN-PGPMVV 321
Cdd:COG1236  231 RAQElLYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHGEYLRDEAQDPFALPN---LRFVTSVEESKALNrKGPAII 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577 322 FATPGMLHAGQSLQIFKKWAGNEKNMVIMPGYCVQGTVGHKILNGQKKLEMEGRaTLDVKLQVE-YMSFSAHADAKGIMQ 400
Cdd:COG1236  307 IAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIFGE-EVPVRARVErLFGLSAHADWDELLE 385

                        410
                 ....*....|....*..
gi 528518577 401 LIR-MAEPRNMLLVHGE 416
Cdd:COG1236  386 WIKaTGKPERVFLVHGE 402
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 4-443 9.45e-117

Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General function prediction only];


Pssm-ID: 441388 [Multi-domain]  Cd Length: 460  Bit Score: 354.82  E-value: 9.45e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   4 IKVTPLGAGQDVGRSCILVSIGGKNIMLDCGMHMGFNDDRRfpdfsyitQNGRLTEF----LDCVIISHFHLDHCGALPY 79
Cdd:COG1782    1 MRITFLGAAREVTGSCHLLETGESRILLDCGLFQGGREERE--------RNNDAFPFdpeeLDAVVLTHAHLDHSGLLPL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  80 MSEMvGYDGPIYMTHPTKAICPILLEDFRKI------TVDKKGETN------FFTSQMIKDCMKKVVPLNLHQTVQVDDE 147
Cdd:COG1782   73 LVKY-GYRGPIYCTPPTRDLMALLLLDSAKIqeeeaeYANKKRYSGhppvepLYTEKDVEKALKHFITLDYGEVTDIAPD 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577 148 LEIKAYYAGHVLGAAMVQIKVGSE--SVVYTGDYNMTPDRHLGAAWIDKcRPDILISESTYATTIRDSKRCRERDFLKKV 225
Cdd:COG1782  152 IKLTFYNAGHILGSAIVHLHIGDGlhNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRLHPSREEAEEELAKVI 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577 226 HETVERGGKVLIPVFALGRAQELCILLETFWERMNL-KAPIYFSTGLTEKANHYYKLFITWTNQKIRKT-FVQRNMFEFK 303
Cdd:COG1782  231 NETIERGGKVLIPAFAVGRTQEILYVLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLiFKGENPFLFE 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577 304 HIKaFDRSY------ADNPGPMVVFATPGMLHAGQSLQIFKKWAGNEKNMVIMPGYCVQGTVGHKILNGQKKLEMEGRaT 377
Cdd:COG1782  311 NLH-YVESVeeskeiNDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFGE-T 388

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528518577 378 LDVKLQVEYM-SFSAHADAKGIMQLIRMAE--PRNMLLVHGEAKKMEFLKDKIEQEFSISCFMPANGET 443
Cdd:COG1782  389 IPVRAEVETIdGFSGHADRNELLNWLRRLKpkPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLET 457
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 7-204 2.44e-95

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


Pssm-ID: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 290.00  E-value: 2.44e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   7 TPLGAGQDVGRSCILVSIGGKNIMLDCGMHMGFNDDrrfpdFSYITQNGRLTEFLDCVIISHFHLDHCGALPYMSEMVGY 86
Cdd:cd07734    1 TPLGGGQEVGRSCFLVEFKGRTVLLDCGMNPGKEDP-----EACLPQFELLPPEIDAILISHFHLDHCGALPYLFRGFIF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  87 DGPIYMTHPTKAICPILLEDFRKITVDKKGETNFFTSQMIKDCMKKVVPLNLHQTVQVDDELEIKAYYAGHVLGAAMVQI 166
Cdd:cd07734   76 RGPIYATHPTVALGRLLLEDYVKSAERIGQDQSLYTPEDIEEALKHIVPLGYGQSIDLFPALSLTAYNAGHVLGAAMWEI 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 528518577 167 KVGSESVVYTGDYNMTPDRHLGAAWIDKCRPDILISES 204
Cdd:cd07734  156 QIYGEKLVYTGDFSNTEDRLLPAASILPPRPDLLITES 193
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 4-204 5.33e-71

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: 226.70  E-value: 5.33e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   4 IKVTPLGAGQDVGRSCILVSIGGKNIMLDCGMHMGFNDDRRFPDFSYItqngRLTEfLDCVIISHFHLDHCGALPYMSEM 83
Cdd:cd16292    1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEI----DLSE-IDLLLITHFHLDHCGALPYFLQK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  84 VGYDGPIYMTHPTKAICPILLEDFRKITvDKKGETNFFTSQMIKDCMKKVVPLNLHQTVQVDDeLEIKAYYAGHVLGAAM 163
Cdd:cd16292   76 TNFKGRVFMTHPTKAIYKWLLSDYVRVS-NISSDEMLYTETDLEASMDKIETIDFHQEVEVNG-IKFTAYNAGHVLGAAM 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 528518577 164 VQIKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPDILISES 204
Cdd:cd16292  154 FMVEIAGVRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 6-204 5.35e-65

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: 211.16  E-value: 5.35e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   6 VTPLGAGQDVGRSCILVSIGGKNIMLDCGMHMGFNDDRRFPDFSYITQNGRltefLDCVIISHFHLDHCGALPYMSEMvG 85
Cdd:cd16295    1 LTFLGAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNNEPFPFDPKE----IDAVILTHAHLDHSGRLPLLVKE-G 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  86 YDGPIYMTHPTKAICPILLEDFRKI---TVDKKGETNFFTSQMIKDCMKKVVPLNLHQTVQVDDELEIKAYYAGHVLGAA 162
Cdd:cd16295   76 FRGPIYATPATKDLAELLLLDSAKIqeeEAEHPPAEPLYTEEDVEKALKHFRPVEYGEPFEIGPGVKVTFYDAGHILGSA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 528518577 163 MVQIKVGSE-SVVYTGDYNMTPDRHLGA-AWIDKCrpDILISES 204
Cdd:cd16295  156 SVELEIGGGkRILFSGDLGRKNTPLLRDpAPPPEA--DYLIMES 197
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 245-363 3.81e-42

Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains.


Pssm-ID: 214983 [Multi-domain]  Cd Length: 126  Bit Score: 147.69  E-value: 3.81e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   245 AQELCILLETFWERMNL-KAPIYFSTGLTEKANHYYKLFITWTNQKIRKTFVQ-RNMFEFKHIKAFD-----RSYADNPG 317
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKFVKsleesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 528518577   318 PMVVFATPGMLHAGQSLQIFKKWAGNEKNMVIMPGYCVQGTVGHKI 363
Cdd:smart01027  81 PKVIIASSGMLTGGRSRHYLKRLAPDPRNTVILTGYQAEGTLGRKL 126
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 7-204 6.28e-30

cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; MBL-fold metallo-hydrolase domain; CPSF2, also known as cleavage and polyadenylation specificity factor 100 kDa subunit (CPSF-100), is a component of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. This subgroup includes Ydh1p, the yeast homolog of CPSF2. 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. 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: 293851  Cd Length: 199  Bit Score: 116.47  E-value: 6.28e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   7 TPLGAGQDVGRSCILVSIGGKNIMLDCGmhmgFNDDRRFPDFSYITqngRLTEFLDCVIISHFHLDHCGALPYMsemVGY 86
Cdd:cd16293    2 TPLSGAGDESPLCYLLEIDDVTILLDCG----WDESFDMEYLESLK---RIAPTIDAVLLSHPDLEHLGALPYL---VGK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  87 DG---PIYMTHPTKAICPILLEDF---RKITvdkkGETNFFTSQMIKDCMKKVVPLNLHQTVQV---DDELEIKAYYAGH 157
Cdd:cd16293   72 LGltcPVYATLPVHKMGRMFMYDLyqsRGLE----EDFNLFTLDDVDEAFDRITQLKYSQPVNLrgkGDGLTITAYNAGH 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 528518577 158 VLGAAMVQIKVGSESVVYTGDYNMTPDRHL-GAAWIDKC--RPDILISES 204
Cdd:cd16293  148 TLGGTIWKITKDSEDIVYAVDWNHKKERHLnGAVLDSFGglRPSLLITDA 197
Beta-Casp pfam10996
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 245-361 1.51e-29

Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains.


Pssm-ID: 463203  Cd Length: 109  Bit Score: 112.61  E-value: 1.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  245 AQELCILLETFWER-MNLKAPIYFSTGLTEKANHYYKLFITWTNQKIRKTfvqrnmfefkhIKAFDRSYADN--PGPMVV 321
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHF-----------VISKSESKAINegKGPKVI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 528518577  322 FATPGMLHAGQSLQIFKKWAGNEKNMVIMPGYCVQGTVGH 361
Cdd:pfam10996  70 IASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLGR 109
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 5-203 7.67e-20

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: 88.05  E-value: 7.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   5 KVTPLGAGQDVGRSCILVSIGGKNIMLDCGM-----------HMGFNDDRRFPDFS------YITQNGRLTE--FLDCVI 65
Cdd:cd07732    1 RITIHRGTNEIGGNCIEVETGGTRILLDFGLpldpeskyfdeVLDFLELGLLPDIVglyrdpLLLGGLRSEEdpSVDAVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  66 ISHFHLDHCGALPYMSEmvgyDGPIYMTHPTKAIcpilLEDFRKITVDKKGETNFFTsqmikdcmkkvvPLNLHQTVQVD 145
Cdd:cd07732   81 LSHAHLDHYGLLNYLRP----DIPVYMGEATKRI----LKALLPFFGEGDPVPRNIR------------VFESGKSFTIG 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528518577 146 DeLEIKAYYAGH-VLGAAMVQIKVGSESVVYTGDYNM-TPDRHLGAAWIDKCR--PDILISE 203
Cdd:cd07732  141 D-FTVTPYLVDHsAPGAYAFLIEAPGKRIFYTGDFRFhGRKPELTEAFVEKAPknIDVLLME 201
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 21-201 2.24e-17

Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase superfamily.


Pssm-ID: 406948  Cd Length: 192  Bit Score: 80.72  E-value: 2.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   21 LVSIGGKNIMLDCGmhmgFNDDRRFPDFSYITQNgrLTEFLDCVIISHFHLDHCGALPYM----SEMVGYDGPIYMTHPT 96
Cdd:pfam16661   1 LLEFDNVRILLDPG----WDGSFSYESDLKYLEK--ILPEVDLILLSHPTLEHLGAYPLLyykfGSHLGSNIPVYATLPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   97 KAICPI-LLEDFRKITVDKKGETNFFTSQMIKDCMKKVVPLNLHQTVQV---DDELEIKAYYAGHVLGAAMVQIKVGSES 172
Cdd:pfam16661  75 ANLGRVsTYDLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkFDGLTITPYNSGHTLGGTIWKISKNSEK 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 528518577  173 VVYTGDYNMTPDRHL-GAAWIDKC--------RPDILI 201
Cdd:pfam16661 155 IVYAVDWNHTKDSHLnGASLLDSTgkpleslvRPTALI 192
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 377-438 5.68e-15

Zn-dependent metallo-hydrolase RNA specificity domain; 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. This, the fifth motif, appears to be specific to Zn-dependent metallohydrolases such as ribonuclease J 2 which are involved in the processing of mRNA. This domain adds essential structural elements to the CASP-domain and is unique to RNA/DNA-processing nucleases, showing that they are pre-mRNA 3'-end-processing endonucleases.


Pssm-ID: 462191 [Multi-domain]  Cd Length: 63  Bit Score: 69.57  E-value: 5.68e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528518577  377 TLDVKLQVEYMS-FSAHADAKGIMQLIRMAEPRNMLLVHGEAKKMEFLKDKIEQEFSISCFMP 438
Cdd:pfam07521   1 GIPVRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEELGIEVFVP 63
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 6-204 1.10e-14

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: 72.30  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   6 VTPLGAG-----QDVGRSCILVSIGGKNIMLDCG-------MHMGFNDDRrfpdfsyitqngrltefLDCVIISHFHLDH 73
Cdd:cd16272    1 LTFLGTGgavpsLTRNTSSYLLETGGTRILLDCGegtvyrlLKAGVDPDK-----------------LDAIFLSHFHLDH 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  74 CGALPYMSEMVGYDGPiymTHPTKAICPILLEDFRKITVDKKGETNFFTSQMikdcmkKVVPLNLHQTVQVDDELEIKAY 153
Cdd:cd16272   64 IGGLPTLLFARRYGGR---KKPLTIYGPKGIKEFLEKLLNFPVEILPLGFPL------EIEELEEGGEVLELGDLKVEAF 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528518577 154 YAGHVLGAAMVQIKVGSESVVYTGDynMTPDRHLgAAWIDKCrpDILISES 204
Cdd:cd16272  135 PVKHSVESLGYRIEAEGKSIVYSGD--TGPCENL-VELAKGA--DLLIHEC 180
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 18-184 1.40e-14

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: 72.20  E-value: 1.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577    18 SCILVSIGGKNIMLDCGMHMGFNDDRRFPDFSYITqngrltefLDCVIISHFHLDHCGALPYMSEMvgYDGPIYMTHPTK 97
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKK--------IDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577    98 AicpiLLEDFRKITVDKKGetnfftsqmIKDCMKKVVPLNLHQTVQVDDElEIKAYYA-GHVLGAAMVqiKVGSESVVYT 176
Cdd:smart00849  71 E----LLKDLLALLGELGA---------EAEPAPPDRTLKDGDELDLGGG-ELEVIHTpGHTPGSIVL--YLPEGKILFT 134


                   ....*...
gi 528518577   177 GDYNMTPD 184
Cdd:smart00849 135 GDLLFAGG 142
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 7-179 1.45e-14

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: 73.59  E-value: 1.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   7 TPLGaGQD-VGRSCILVSIGGKNIMLDCGMHMGFND----DRRFPDFSYITQNGrltEFLDCVIISHFHLDHCGALPYMS 81
Cdd:cd07714    1 IPLG-GLGeIGKNMYVVEYDDDIIIIDCGLKFPDEDmpgvDYIIPDFSYLEENK---DKIKGIFITHGHEDHIGALPYLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  82 EMvgYDGPIYMTHPTKAICPILLEDFRKItvdkkGETNFftsqmikdcmkkvVPLNLHQTVQVDDeLEIKAYYAGH-VLG 160
Cdd:cd07714   77 PE--LNVPIYATPLTLALIKKKLEEFKLI-----KKVKL-------------NEIKPGERIKLGD-FEVEFFRVTHsIPD 135

                        170
                 ....*....|....*....
gi 528518577 161 AAMVQIKVGSESVVYTGDY 179
Cdd:cd07714  136 SVGLAIKTPEGTIVHTGDF 154
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
4-207 4.22e-14

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 72.54  E-value: 4.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   4 IKVTPLGAG---QDVGR--SCILVSIGGKNIMLDCG-------MHMGFNDDRrfpdfsyitqngrltefLDCVIISHFHL 71
Cdd:COG1234    1 MKLTFLGTGgavPTPGRatSSYLLEAGGERLLIDCGegtqrqlLRAGLDPRD-----------------IDAIFITHLHG 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  72 DHCGALPYMSEMVGYDG-----PIYMTHPTKAIcpilLEDFRKITvdkKGETNFFTsqmikdcmkKVVPLNLHQTVQVDD 146
Cdd:COG1234   64 DHIAGLPGLLSTRSLAGrekplTIYGPPGTKEF----LEALLKAS---GTDLDFPL---------EFHEIEPGEVFEIGG 127

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528518577 147 eLEIKAYYAGHVLGAAMVQIKVGSESVVYTGD--YNmtpdrhlgAAWIDKCR-PDILISESTYA 207
Cdd:COG1234  128 -FTVTAFPLDHPVPAYGYRFEEPGRSLVYSGDtrPC--------EALVELAKgADLLIHEATFL 182
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 17-206 1.08e-12

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 68.38  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  17 RSCILVSIGGKNIMLDCGmhmgfnddrrfPDFSYITQNGRLT-EFLDCVIISHFHLDHCGALPYMSEMVGYDG-PIYMTH 94
Cdd:COG1235   35 RSSILVEADGTRLLIDAG-----------PDLREQLLRLGLDpSKIDAILLTHEHADHIAGLDDLRPRYGPNPiPVYATP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  95 PTKAicpILLEDFRKITVDKKGETNFftsqmikdcmkkvVPLNLHQTVQVDDeLEIKAY----YAGHVLGaamVQIKVGS 170
Cdd:COG1235  104 GTLE---ALERRFPYLFAPYPGKLEF-------------HEIEPGEPFEIGG-LTVTPFpvphDAGDPVG---YRIEDGG 163

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 528518577 171 ESVVYTGDYNMTPDRHLgaAWIDKCrpDILISESTY 206
Cdd:COG1235  164 KKLAYATDTGYIPEEVL--ELLRGA--DLLILDATY 195
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
1-93 8.24e-12

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 67.78  E-value: 8.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   1 MPDIKVTPLGaGQD-VGRSCILVSIGGKNIMLDCGMhmGFNDDRRF------PDFSYITQNGrltEFLDCVIISHFHLDH 73
Cdd:COG0595    3 KDKLRIIPLG-GLGeIGKNMYVYEYDDDIIIVDCGL--KFPEDEMPgvdlviPDISYLEENK---DKIKGIVLTHGHEDH 76

                         90       100
                 ....*....|....*....|
gi 528518577  74 CGALPYMSEMVgyDGPIYMT 93
Cdd:COG0595   77 IGALPYLLKEL--NVPVYGT 94
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
18-178 5.11e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 62.39  E-value: 5.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   18 SCILVSIGGKNIMLDCGMhmgfndDRRFPDFSYITQNGRLTEFLDCVIISHFHLDHCGALPYMSEmvgydgpiymTHPTK 97
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGG------SAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAE----------ATDVP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   98 AICPILLEDFRKITVDKKGETNFFTSQMIKDCMKKVVPLNLHQTvqVDDELEIKAYYAGHVLGAAMVQIKVGSESVVYTG 177
Cdd:pfam00753  71 VIVVAEEARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDG--ILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTG 148


                  .
gi 528518577  178 D 178
Cdd:pfam00753 149 D 149
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 5-204 9.74e-11

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: 60.92  E-value: 9.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   5 KVTPLG-----AGQDVGRSCILVSIGGKNIMLDCGmhmgfnddrrfpdfsyitqNG---RLTEF-----LDCVIISHFHL 71
Cdd:cd07716    1 KLTVLGcsgsyPGPGGACSGYLLEADGFRILLDCG-------------------SGvlsRLQRYidpedLDAVVLSHLHP 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  72 DHC---GALPYMSEMVGYDGPiymTHPTKAICPILLEDFRKITVDKKGETNFFtsqmikdcmkkvvPLNLHQTVQVDDeL 148
Cdd:cd07716   62 DHCadlGVLQYARRYHPRGAR---KPPLPLYGPAGPAERLAALYGLEDVFDFH-------------PIEPGEPLEIGP-F 124

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528518577 149 EIKAYYAGHVLGAAMVQIKVGSESVVYTGDYNMTPdrhlgaAWIDKCR-PDILISES 204
Cdd:cd07716  125 TITFFRTVHPVPCYAMRIEDGGKVLVYTGDTGYCD------ELVEFARgADLLLCEA 175
Int9-like_MBL-fold cd16294
integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ...
 12-175 3.82e-08

integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a metazoan-specific multisubunit, multifunctional protein complex composed of 14 subunits named Int1-Int14 (Integrator subunits). This subgroup includes Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74). Integrator complex has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293852 [Multi-domain]  Cd Length: 166  Bit Score: 53.27  E-value: 3.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  12 GQDVGRSCILVSIGGKNIMLDCGMhmGFNDDRRFPDFSYItqngrlteflDCVIISHFHldHCGALPYMSEMVGYDGPIY 91
Cdd:cd16294    7 SGHPTLPCNVLKFKSTTIMLDCGL--DCPPETELIDLSTV----------DVILISNYH--CMLALPFITEYTGFTGVVY 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  92 MTHPTKAICPILLEDfrkitvdkkgetnfftsqmIKDCMKKVVPLNLHQTVQVDDELEIKAYYAGHVLGAAMVQIKVGSE 171
Cdd:cd16294   73 ATEPTVQIGRLLMEE-------------------LVQALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYE 133


                 ....
gi 528518577 172 SVVY 175
Cdd:cd16294  134 KISY 137
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 18-207 1.02e-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: 53.22  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  18 SCILVSIGGKNIMLDCG-------MHMGFnddrRFPDfsyitqngrltefLDCVIISHFHLDHCGALP----YMSeMVGY 86
Cdd:cd07717   18 SSIALRLEGELWLFDCGegtqrqlLRAGL----SPSK-------------IDRIFITHLHGDHILGLPgllsTMS-LLGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  87 DGP--IYMTHPTKAIcpilLEDFRKITvdkKGETNFftsqmikdcmkkvvPLNLH------QTVQVDDELEIKAYYAGHV 158
Cdd:cd07717   80 TEPltIYGPKGLKEF----LETLLRLS---ASRLPY--------------PIEVHelepdpGLVFEDDGFTVTAFPLDHR 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 528518577 159 LGAAMVQIKVGSeSVVYTGDyNMTPDRHLGAAWidkcRPDILISESTYA 207
Cdd:cd07717  139 VPCFGYRFEEGR-KIAYLGD-TRPCEGLVELAK----GADLLIHEATFL 181
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 19-178 1.97e-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: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  19 CILVSIG-GKNIMLDCGMhmGFNDDRRfpdfSYITQNGrLTefLDCVIISHFHLDHCGALPYMSEMvgYDGPIYMTHPTK 97
Cdd:cd06262   12 CYLVSDEeGEAILIDPGA--GALEKIL----EAIEELG-LK--IKAILLTHGHFDHIGGLAELKEA--PGAPVYIHEADA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  98 AicpiLLEDfrkitvdkKGETNFFTSQMIKDCMKKVVPLNLHQTVQVDDeLEIKAYYA-GHVLGaaMVQIKVGSESVVYT 176
Cdd:cd06262   81 E----LLED--------PELNLAFFGGGPLPPPEPDILLEDGDTIELGG-LELEVIHTpGHTPG--SVCFYIEEEGVLFT 145


                 ..
gi 528518577 177 GD 178
Cdd:cd06262  146 GD 147
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 5-185 2.21e-07

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: 52.60  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   5 KVTPLGA--GQDVGR-SCILVSIGGKN--IMLDCGMHMG---FNDDRRFPDFSYITQNGRLTEFLDCVIISHFHLDHCGA 76
Cdd:cd07735    2 ELVVLGCsgGPDEGNtSSFLLDPAGSDgdILLDAGTGVGalsLEEMFNDILFPSQKAAYELYQRIRHYLITHAHLDHIAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  77 LPYMSEMVGYDGpiymtHPTKAICPIlledfrKITVDKKGETNF-------FTSQMIKDCM-KKVVPLNLHQTVQVDDeL 148
Cdd:cd07735   82 LPLLSPNDGGQR-----GSPKTIYGL------PETIDALKKHIFnwviwpdFTSIPSGKYPyLRLEPIEPEYPIALTG-L 149

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 528518577 149 EIKAYYAGH-VLGAAMVQIKVGSESVVYTGDynMTPDR 185
Cdd:cd07735  150 SVTAFPVSHgVPVSTAFLIRDGGDSFLFFGD--TGPDS 185
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 14-79 3.15e-06

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 47.90  E-value: 3.15e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528518577  14 DVGRS-CILVSIGGKNIMLDCGMHMGFNDDRRFPdfsYITQNGRLTefLDCVIISHFHLDHCGALPY 79
Cdd:cd07731    6 DVGQGdAILIQTPGKTILIDTGPRDSFGEDVVVP---YLKARGIKK--LDYLILTHPDADHIGGLDA 67
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 14-79 6.57e-06

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: 47.93  E-value: 6.57e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528518577  14 DVGR-SCILV-SIGGKNIMLDCGMHMGFNDDRRFPDfSYITQNGRLTefLDCVIISHFHLDHCGALPY 79
Cdd:COG2333    7 DVGQgDAILIrTPDGKTILIDTGPRPSFDAGERVVL-PYLRALGIRR--LDLLVLTHPDADHIGGLAA 71
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 5-78 1.04e-05

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: 46.36  E-value: 1.04e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528518577   5 KVTPLGAG---QDVGR--SCILVSIGGKNIMLDCGMHMGfnddRRFpdfsyiTQNGRLTEFLDCVIISHFHLDHCGALP 78
Cdd:cd07719    1 RVTLLGTGgpiPDPDRagPSTLVVVGGRVYLVDAGSGVV----RRL------AQAGLPLGDLDAVFLTHLHSDHVADLP 69
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 67-206 2.04e-05

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: 45.22  E-value: 2.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  67 SHFHLDHcgalpYMsemvGYD-----GPIYMTHPTKaicpILLEDfrKITVDKKgetnfftsqmikdcmkKVVPLNLHQT 141
Cdd:cd16273   43 SHFHSDH-----YG----GLTkswshGPIYCSEITA----NLVKL--KLKVDEE----------------YIVVLPMNTP 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528518577 142 VQVDDELEIKAYYAGHVLGAAMVQIKV-GSESVVYTGDYNMTPDRHLGAAWIDKCRPDILISESTY 206
Cdd:cd16273   92 VEIDGDVSVTLLDANHCPGAVMFLFELpDGRRILHTGDFRANPEMLEHPLLLGKRRIDTVYLDTTY 157
PRK00055 PRK00055
ribonuclease Z; Reviewed
 4-217 2.64e-05

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 46.33  E-value: 2.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   4 IKVTPLGAGQ---DVGR--SCILVSIGGKNIMLDCG-------MHMGFnddrRFPDFSYItqngrlteFldcviISHFHL 71
Cdd:PRK00055   2 MELTFLGTGSgvpTPTRnvSSILLRLGGELFLFDCGegtqrqlLKTGI----KPRKIDKI--------F-----ITHLHG 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  72 DHCGALPYMSEMVGYDGpiyMTHPTKAICPILLEDF----RKIT------VDKKGETNFFTSQMIKDCMKKVVPL--NLH 139
Cdd:PRK00055  65 DHIFGLPGLLSTRSLSG---RTEPLTIYGPKGIKEFvetlLRASgslgyrIAEKDKPGKLDAEKLKALGVPPGPLfgKLK 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577 140 --QTVQVDDeleikayyaGHVLGAAMVqikVGSE----SVVYTGDynmT-PDRHLgAAWIDKCrpDILISESTYATTIRD 212
Cdd:PRK00055 142 rgEDVTLED---------GRIINPADV---LGPPrkgrKVAYCGD---TrPCEAL-VELAKGA--DLLVHEATFGDEDEE 203


                 ....*
gi 528518577 213 SKRCR 217
Cdd:PRK00055 204 LAKEY 208
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 19-95 2.69e-05

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293799  Cd Length: 269  Bit Score: 46.08  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  19 CILVSIGGKNIMLDCGM---------HMGFNDDRrfpdfsyitqngrltefLDCVIISHFHLDHCGALPYMSEMVGyDGP 89
Cdd:cd07713   22 SLLIETEGKKILFDTGQsgvllhnakKLGIDLSD-----------------IDAVVLSHGHYDHTGGLKALLELNP-KAP 83


                 ....*.
gi 528518577  90 IYMtHP 95
Cdd:cd07713   84 VYA-HP 88
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 19-178 3.25e-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: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  19 CILVSIGGKNIMLDCGMhmGFNDDRRFPDfsYITQNGRLtefLDCVIISHFHLDHCGALPYMSEmvGYDGPIYMTHPTKA 98
Cdd:COG0491   17 SYLIVGGDGAVLIDTGL--GPADAEALLA--ALAALGLD---IKAVLLTHLHPDHVGGLAALAE--AFGAPVYAHAAEAE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  99 IcpilledfrkitVDKKGETNFFTSQMIKDcmkkVVPLNLHQTVQVDDeLEIKAYYA-GHVLGaaMVQIKVGSESVVYTG 177
Cdd:COG0491   88 A------------LEAPAAGALFGREPVPP----DRTLEDGDTLELGG-PGLEVIHTpGHTPG--HVSFYVPDEKVLFTG 148


                 .
gi 528518577 178 D 178
Cdd:COG0491  149 D 149
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 18-79 4.63e-05

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 45.28  E-value: 4.63e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528518577  18 SCILVSIGGKNIMLDCGMHMGFNDDRRFPDFSY---ITQNGRLTEFL----------DCVIISHFHLDHCGALPY 79
Cdd:cd07729   33 YAYLIEHPEGTILVDTGFHPDAADDPGGLELAFppgVTEEQTLEEQLarlgldpediDYVILSHLHFDHAGGLDL 107
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 17-96 6.18e-05

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: 44.39  E-value: 6.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  17 RSCILVSIGGKNIMLDCGmhmgfnddrrfPDFSY------ITQngrltefLDCVIISHFHLDHCGALP---YMSEMVGYD 87
Cdd:cd16279   35 RSSILIETGGKNILIDTG-----------PDFRQqalragIRK-------LDAVLLTHAHADHIHGLDdlrPFNRLQQRP 96


                 ....*....
gi 528518577  88 GPIYMTHPT 96
Cdd:cd16279   97 IPVYASEET 105
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 18-205 1.02e-04

Ribonuclease Z ELAC1, C-terminus of ELAC2, 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. 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 eukaryotic subgroup includes short forms (ELAC1) and the C-terminus of long forms including human ELAC2. 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: 293804 [Multi-domain]  Cd Length: 204  Bit Score: 43.69  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  18 SCILVSI-GGKNIMLDCG------MHmgfnddRRFPDFsyiTQNGRLTEfLDCVIISHFHLDHCGALPYM-----SEMVG 85
Cdd:cd07718   18 SGILLRIpGDGSILLDCGegtlgqLR------RHYGPE---EADEVLRN-LKCIFISHLHADHHLGLIRLlaerkKLFKP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  86 YDGPIYMTHPTK---------AICPILLEDFRKITV---DKKGETNFFTSQMIKDCMKKVVPLNLHQTVQVDdeleikay 153
Cdd:cd07718   88 PSPPLYVVAPRQlrrwlreysSLEDLGLHDISFISNrvsQSLPESDDPLSRDLLSNLLEELGLKSIETVPVI-------- 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528518577 154 yagHVLGAAMVQIKVGSE-SVVYTGDynmtpdrhlgaawidkCRP-----------DILISEST 205
Cdd:cd07718  160 ---HCPDAYGIVLTHEDGwKIVYSGD----------------TRPcealveagkgaDLLIHEAT 204
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 19-75 6.61e-04

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


Pssm-ID: 293839  Cd Length: 252  Bit Score: 41.71  E-value: 6.61e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528518577  19 CILVSIGGKNIMLDCGMhmGFNDDRRFPDFSYITQNGRLTEFL----------DCVIISHFHLDHCG 75
Cdd:cd16281   45 CLLIETGGRNILIDTGI--GDKQDPKFRSIYVQHSEHSLLKSLarlglspediTDVILTHLHFDHCG 109
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
19-95 1.84e-03

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 40.64  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  19 CILVSIGGKNIMLDCG-----MH----MGFNddrrfpdfsyitqngrLTEfLDCVIISHFHLDHCGALPYMSEMVGyDGP 89
Cdd:COG1237   24 SALIETEGKRILFDTGqsdvlLKnaekLGID----------------LSD-IDAVVLSHGHYDHTGGLPALLELNP-KAP 85


                 ....*.
gi 528518577  90 IYMtHP 95
Cdd:COG1237   86 VYA-HP 90
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 18-178 2.58e-03

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. 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: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 39.84  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  18 SCILVSIGGKNIMLDCGM--HMGFNDdrrfpdfsyitqnGRLTEFL----------DCVIISHFHLDHCGALpymseMVG 85
Cdd:cd07720   50 NAFLVRTGGRLILVDTGAggLFGPTA-------------GKLLANLaaagidpediDDVLLTHLHPDHIGGL-----VDA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  86 YDGPIYmthpTKAicpilledfrKITVDKKgETNFFTS------------QMIKDCMKKVVPLNLHQTVQVDDEL--EIK 151
Cdd:cd07720  112 GGKPVF----PNA----------EVHVSEA-EWDFWLDdanaakapegakRFFDAARDRLRPYAAAGRFEDGDEVlpGIT 176

                        170       180
                 ....*....|....*....|....*...
gi 528518577 152 AYYA-GHVLGAAMVQIKVGSESVVYTGD 178
Cdd:cd07720  177 AVPApGHTPGHTGYRIESGGERLLIWGD 204
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 18-206 3.79e-03

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


Pssm-ID: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 39.02  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  18 SCILVSIGGKNIMLDCGMhmGFnddRRFPDfsYITQNGRLTEFLdcVIISHFHLDH-CGaLPYMsemvgydGPIYMTHpt 96
Cdd:cd07715   24 SCVEVRAGGELLILDAGT--GI---RELGN--ELMKEGPPGEAH--LLLSHTHWDHiQG-FPFF-------APAYDPG-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  97 kaicpilledfRKITV-----DKKGETNFFTSQM--------IKDCMKKV--VPLNLHQTVQVDDeLEIKAYYAGHVLGA 161
Cdd:cd07715   85 -----------NRIHIygphkDGGSLEEVLRRQMsppyfpvpLEELLAAIefHDLEPGEPFSIGG-VTVTTIPLNHPGGA 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 528518577 162 AMVQIKVGSESVVYTGDYNMTP-DRHLGAAWIDKCR-PDILISESTY 206
Cdd:cd07715  153 LGYRIEEDGKSVVYATDTEHYPdDGESDEALLEFARgADLLIHDAQY 199
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 28-189 5.17e-03

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 38.44  E-value: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577   28 NIMLDCGMhmgfndDRRFPDFSYITQNGRLTEFLDCVIISHFHLDHCGALPYMSEmvGYDGPIYMTHPTKAicpILLEDF 107
Cdd:pfam12706   2 RILIDPGP------DLRQQALPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLRE--GRPRPLYAPLGVLA---HLRRNF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  108 RKITVDKKGETNfftsqmikdcmkkVVPLNLHQTVQVDDE-LEIKA------------YYAGHVLGAAmvqIKVGSESVV 174
Cdd:pfam12706  71 PYLFLLEHYGVR-------------VHEIDWGESFTVGDGgLTVTAtparhgsprgldPNPGDTLGFR---IEGPGKRVY 134

                         170
                  ....*....|....*
gi 528518577  175 YTGDYNMTPDrHLGA 189
Cdd:pfam12706 135 YAGDTGYFPD-EIGE 148
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 18-186 9.43e-03

Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase domain; Includes Dictyostelium discoideum cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A (also known as cyclic GMP-binding protein A, phosphodiesterase 5, phosphodiesterase D, and PDE5) and cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B (also known as cyclic GMP-binding protein B, phosphodiesterase 6, phosphodiesterase E, and PDE6. 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: 293824  Cd Length: 189  Bit Score: 37.66  E-value: 9.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  18 SCILVSIGGKNIMLDCGMHMGfnddrrfpdfSYITQNGRLTEFLDCVIISHFHLDHCGALPYMSeMVGYDGPIYMThptk 97
Cdd:cd07738   16 SGFIIWINGRGIMVDPPVNST----------SYLRQNGISPRLVDHVILTHCHADHDAGTFQKI-LEEEKITLYTT---- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528518577  98 aicPILLEDF-RKITVDKKGETNF------FTSQMIKDcmkkvvPLNLHQTvqvddelEIKAYYAGHVLGAAMVQIKVGS 170
Cdd:cd07738   81 ---RTINESFlRKYAALTGLPPDFleelfdFRPVIIGE------KTKINGA-------EFEFDYSFHSIPTIRFKVSYGG 144

                        170
                 ....*....|....*.
gi 528518577 171 ESVVYTGDYNMTPDRH 186
Cdd:cd07738  145 KSIAYSGDTRYDPDGL 160
 
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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