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Conserved domains on  [gi|440801023|gb|ELR22048|]
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cleavage and polyadenylation specific factor 3like, putative [Acanthamoeba castellanii str. Neff]

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

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; ...
 5-203 4.43e-164

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: 467.89  E-value: 4.43e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   5 VTPLGAGQDVGRSCILVSLGGKNIMFDCGMHMGYDDARRFPDFNFISKSGNFTNAIDCIIITHFHLDHCGALPYFTEMCG 84
Cdd:cd16291    1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  85 YDGPIYMTHPTKAICPILLEDYRKITVERKGETNFFTSQMIKDCMKKVVGLNVHQTVQVDEELEIRAYYAGHVLGAAMFY 164
Cdd:cd16291   81 YDGPIYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFY 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 440801023 165 VRVGDQSVVYTGDYNMTPDRHLGAAWIEKLRPDVLITES 203
Cdd:cd16291  161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 4-418 4.37e-116

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


:

Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 352.95  E-value: 4.37e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   4 KVTPLGAGQDVGRSCILVSLGGKNIMFDCGMHMGYDDaRRFPDFNFISKSgnftnaIDCIIITHFHLDHCGALPYFTEMc 83
Cdd:COG1236    2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKE-RNWPPFPFRPSD------VDAVVLTHAHLDHSGALPLLVKE- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  84 GYDGPIYMTHPTKAICPILLEDYRKITVERKGETNFFTSQMIKDCMKKVVGLNVHQTVQVDEeLEIRAYYAGHVLGAAMF 163
Cdd:COG1236   74 GFRGPIYATPATADLARILLGDSAKIQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023 164 YVRVGDQSVVYTGDYNMTPDR-HLGAAWIEKlrPDVLITESTYATTIRDSKRWRERDFLKRVHSCVEKGGKVLIPVFALG 242
Cdd:COG1236  153 ELEVGGKRIVFSGDYGREDDPlLAPPEPVPP--ADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALG 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023 243 RAQE-LCILLETYWERMNLTVPIYFSaGLTEKATNYYKLFIHWTNEKIkrtfvhRNMFDFKHI----STFERGLADQPGP 317
Cdd:COG1236  231 RAQElLYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHGEYLRDEA------QDPFALPNLrfvtSVEESKALNRKGP 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023 318 MVLFATPGMLHAGTSLEVFKKWAPNEKNLVIIPGYCVVGTVGNKLAAGRKgsfKVDLDSRTsLEVRCKVKNL-SFSAHAD 396
Cdd:COG1236  304 AIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAK---EVKIFGEE-VPVRARVERLfGLSAHAD 379

                        410       420
                 ....*....|....*....|...
gi 440801023 397 AKGIMQLIK-MSQPANVILVHGE 418
Cdd:COG1236  380 WDELLEWIKaTGKPERVFLVHGE 402
 
Name Accession Description Interval E-value
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 5-203 4.43e-164

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: 467.89  E-value: 4.43e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   5 VTPLGAGQDVGRSCILVSLGGKNIMFDCGMHMGYDDARRFPDFNFISKSGNFTNAIDCIIITHFHLDHCGALPYFTEMCG 84
Cdd:cd16291    1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  85 YDGPIYMTHPTKAICPILLEDYRKITVERKGETNFFTSQMIKDCMKKVVGLNVHQTVQVDEELEIRAYYAGHVLGAAMFY 164
Cdd:cd16291   81 YDGPIYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFY 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 440801023 165 VRVGDQSVVYTGDYNMTPDRHLGAAWIEKLRPDVLITES 203
Cdd:cd16291  161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 4-418 4.37e-116

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 352.95  E-value: 4.37e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   4 KVTPLGAGQDVGRSCILVSLGGKNIMFDCGMHMGYDDaRRFPDFNFISKSgnftnaIDCIIITHFHLDHCGALPYFTEMc 83
Cdd:COG1236    2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKE-RNWPPFPFRPSD------VDAVVLTHAHLDHSGALPLLVKE- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  84 GYDGPIYMTHPTKAICPILLEDYRKITVERKGETNFFTSQMIKDCMKKVVGLNVHQTVQVDEeLEIRAYYAGHVLGAAMF 163
Cdd:COG1236   74 GFRGPIYATPATADLARILLGDSAKIQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023 164 YVRVGDQSVVYTGDYNMTPDR-HLGAAWIEKlrPDVLITESTYATTIRDSKRWRERDFLKRVHSCVEKGGKVLIPVFALG 242
Cdd:COG1236  153 ELEVGGKRIVFSGDYGREDDPlLAPPEPVPP--ADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALG 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023 243 RAQE-LCILLETYWERMNLTVPIYFSaGLTEKATNYYKLFIHWTNEKIkrtfvhRNMFDFKHI----STFERGLADQPGP 317
Cdd:COG1236  231 RAQElLYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHGEYLRDEA------QDPFALPNLrfvtSVEESKALNRKGP 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023 318 MVLFATPGMLHAGTSLEVFKKWAPNEKNLVIIPGYCVVGTVGNKLAAGRKgsfKVDLDSRTsLEVRCKVKNL-SFSAHAD 396
Cdd:COG1236  304 AIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAK---EVKIFGEE-VPVRARVERLfGLSAHAD 379

                        410       420
                 ....*....|....*....|...
gi 440801023 397 AKGIMQLIK-MSQPANVILVHGE 418
Cdd:COG1236  380 WDELLEWIKaTGKPERVFLVHGE 402
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 244-362 1.20e-41

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: 147.30  E-value: 1.20e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   244 AQELCILLETYWERMNL-TVPIYFSAGLTEKATNYYKLFIHWTNEKIKRTFV-HRNMFDFKHISTFE-----RGLADQPG 316
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEqGRNPFDFKNLKFVKsleesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 440801023   317 PMVLFATPGMLHAGTSLEVFKKWAPNEKNLVIIPGYCVVGTVGNKL 362
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 ...
 244-359 2.80e-32

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: 120.31  E-value: 2.80e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  244 AQELCILLETYWER-MNLTVPIYFSAGLTEKATNYYKLFIHWTNEKIKRTFVHRNMfdfkhistfERGLADQPGPMVLFA 322
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFVISKSE---------SKAINEGKGPKVIIA 71

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 440801023  323 TPGMLHAGTSLEVFKKWAPNEKNLVIIPGYCVVGTVG 359
Cdd:pfam10996  72 SSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLG 108
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 17-183 6.63e-18

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: 81.83  E-value: 6.63e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023    17 SCILVSLGGKNIMFDCGMHMGYDDARRFPDFNFisksgnftNAIDCIIITHFHLDHCGALPYFTEMcgYDGPIYMTHPTK 96
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGP--------KKIDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023    97 AicpiLLEDYRKITVERKGetnfftsqmIKDCMKKVVGLNVHQTVQV-DEELEIRaYYAGHVLGAAMFYVRvgDQSVVYT 175
Cdd:smart00849  71 E----LLKDLLALLGELGA---------EAEPAPPDRTLKDGDELDLgGGELEVI-HTPGHTPGSIVLYLP--EGKILFT 134


                   ....*...
gi 440801023   176 GDYNMTPD 183
Cdd:smart00849 135 GDLLFAGG 142
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
3-235 1.00e-15

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 77.16  E-value: 1.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   3 IKVTPLGAG---QDVGR--SCILVSLGGKNIMFDCG-------MHMGYDDARrfpdfnfisksgnftnaIDCIIITHFHL 70
Cdd:COG1234    1 MKLTFLGTGgavPTPGRatSSYLLEAGGERLLIDCGegtqrqlLRAGLDPRD-----------------IDAIFITHLHG 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  71 DHCGALPYFTEMCGYDG-----PIYMTHPTKAIcpilLEDYRKITVERkgeTNFFTsqmikdcmkKVVGLNVHQTVQvDE 145
Cdd:COG1234   64 DHIAGLPGLLSTRSLAGrekplTIYGPPGTKEF----LEALLKASGTD---LDFPL---------EFHEIEPGEVFE-IG 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023 146 ELEIRAYYAGHVLGAAMFYVRVGDQSVVYTGD--YNmtpdrhlgAAWIEKLR-PDVLITESTYATtirdskrWRERDFLK 222
Cdd:COG1234  127 GFTVTAFPLDHPVPAYGYRFEEPGRSLVYSGDtrPC--------EALVELAKgADLLIHEATFLD-------EEAELAKE 191

                        250
                 ....*....|...
gi 440801023 223 RVHSCVEKGGKVL 235
Cdd:COG1234  192 TGHSTAKEAAELA 204
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 20-200 1.09e-15

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 75.71  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   20 LVSLGGKNIMFDCGMH--MGYDDARRFPDfNFISKsgnftnaIDCIIITHFHLDHCGALPY----FTEMCGYDGPIYMTH 93
Cdd:pfam16661   1 LLEFDNVRILLDPGWDgsFSYESDLKYLE-KILPE-------VDLILLSHPTLEHLGAYPLlyykFGSHLGSNIPVYATL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   94 PTKAICPI-LLEDYRKITVERKGETNFFTSQMIKDCMKKVVGLNVHQTVQV---DEELEIRAYYAGHVLGAAMFYVRVGD 169
Cdd:pfam16661  73 PVANLGRVsTYDLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkFDGLTITPYNSGHTLGGTIWKISKNS 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 440801023  170 QSVVYTGDYNMTPDRHL-GAAWIEK--------LRPDVLI 200
Cdd:pfam16661 153 EKIVYAVDWNHTKDSHLnGASLLDStgkpleslVRPTALI 192
PRK00055 PRK00055
ribonuclease Z; Reviewed
 3-206 1.34e-08

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 56.34  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   3 IKVTPLGAGQ---DVGR--SCILVSLGGKNIMFDCG-------MHMGYddarrfpdfnfisksgNFTNaIDCIIITHFHL 70
Cdd:PRK00055   2 MELTFLGTGSgvpTPTRnvSSILLRLGGELFLFDCGegtqrqlLKTGI----------------KPRK-IDKIFITHLHG 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  71 DHCGALPYFTEMCGYDGpiyMTHPTKAICPILLEDY----RKIT------VERKGETNFFTSQMIKDcmKKVVGLNVHQT 140
Cdd:PRK00055  65 DHIFGLPGLLSTRSLSG---RTEPLTIYGPKGIKEFvetlLRASgslgyrIAEKDKPGKLDAEKLKA--LGVPPGPLFGK 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023 141 VQVDEELEiraYYAGHVLGAAMFY--VRVGdQSVVYTGDYNMTPDrhlgaawIEKL--RPDVLITESTYA 206
Cdd:PRK00055 140 LKRGEDVT---LEDGRIINPADVLgpPRKG-RKVAYCGDTRPCEA-------LVELakGADLLVHEATFG 198
 
Name Accession Description Interval E-value
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 5-203 4.43e-164

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: 467.89  E-value: 4.43e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   5 VTPLGAGQDVGRSCILVSLGGKNIMFDCGMHMGYDDARRFPDFNFISKSGNFTNAIDCIIITHFHLDHCGALPYFTEMCG 84
Cdd:cd16291    1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  85 YDGPIYMTHPTKAICPILLEDYRKITVERKGETNFFTSQMIKDCMKKVVGLNVHQTVQVDEELEIRAYYAGHVLGAAMFY 164
Cdd:cd16291   81 YDGPIYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFY 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 440801023 165 VRVGDQSVVYTGDYNMTPDRHLGAAWIEKLRPDVLITES 203
Cdd:cd16291  161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 4-418 4.37e-116

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 352.95  E-value: 4.37e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   4 KVTPLGAGQDVGRSCILVSLGGKNIMFDCGMHMGYDDaRRFPDFNFISKSgnftnaIDCIIITHFHLDHCGALPYFTEMc 83
Cdd:COG1236    2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKE-RNWPPFPFRPSD------VDAVVLTHAHLDHSGALPLLVKE- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  84 GYDGPIYMTHPTKAICPILLEDYRKITVERKGETNFFTSQMIKDCMKKVVGLNVHQTVQVDEeLEIRAYYAGHVLGAAMF 163
Cdd:COG1236   74 GFRGPIYATPATADLARILLGDSAKIQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023 164 YVRVGDQSVVYTGDYNMTPDR-HLGAAWIEKlrPDVLITESTYATTIRDSKRWRERDFLKRVHSCVEKGGKVLIPVFALG 242
Cdd:COG1236  153 ELEVGGKRIVFSGDYGREDDPlLAPPEPVPP--ADVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALG 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023 243 RAQE-LCILLETYWERMNLTVPIYFSaGLTEKATNYYKLFIHWTNEKIkrtfvhRNMFDFKHI----STFERGLADQPGP 317
Cdd:COG1236  231 RAQElLYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHGEYLRDEA------QDPFALPNLrfvtSVEESKALNRKGP 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023 318 MVLFATPGMLHAGTSLEVFKKWAPNEKNLVIIPGYCVVGTVGNKLAAGRKgsfKVDLDSRTsLEVRCKVKNL-SFSAHAD 396
Cdd:COG1236  304 AIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAK---EVKIFGEE-VPVRARVERLfGLSAHAD 379

                        410       420
                 ....*....|....*....|...
gi 440801023 397 AKGIMQLIK-MSQPANVILVHGE 418
Cdd:COG1236  380 WDELLEWIKaTGKPERVFLVHGE 402
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 3-448 2.79e-109

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: 337.49  E-value: 2.79e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   3 IKVTPLGAGQDVGRSCILVSLGGKNIMFDCGMHMGYDDARR-----FPdFNFisksgnftNAIDCIIITHFHLDHCGALP 77
Cdd:COG1782    1 MRITFLGAAREVTGSCHLLETGESRILLDCGLFQGGREERErnndaFP-FDP--------EELDAVVLTHAHLDHSGLLP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  78 YFTEMcGYDGPIYMTHPTKAICPILLEDYRKITVE------RKGETN------FFTSQMIKDCMKKVVGLNVHQTVQVDE 145
Cdd:COG1782   72 LLVKY-GYRGPIYCTPPTRDLMALLLLDSAKIQEEeaeyanKKRYSGhppvepLYTEKDVEKALKHFITLDYGEVTDIAP 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023 146 ELEIRAYYAGHVLGAAMFYVRVGD--QSVVYTGDYNMTPDRHLGAAWIEKlRPDVLITESTYATTIRDSKRWRERDFLKR 223
Cdd:COG1782  151 DIKLTFYNAGHILGSAIVHLHIGDglHNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRLHPSREEAEEELAKV 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023 224 VHSCVEKGGKVLIPVFALGRAQELCILLETYWERMNL-TVPIYFSAGLTEKATNYYKLFIHWTNEKIKRT-FVHRNMFDF 301
Cdd:COG1782  230 INETIERGGKVLIPAFAVGRTQEILYVLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLiFKGENPFLF 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023 302 KH---ISTFE--RGLADQPGPMVLFATPGMLHAGTSLEVFKKWAPNEKNLVIIPGYCVVGTVGNKLAAGRKgsfKVDLDS 376
Cdd:COG1782  310 ENlhyVESVEesKEINDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAK---EVKIFG 386

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 440801023 377 RTsLEVRCKVKNL-SFSAHADAKGIMQLIK--MSQPANVILVHGEKGKMQSLKQRVIREFEIPCFDPPNGSTVTI 448
Cdd:COG1782  387 ET-IPVRAEVETIdGFSGHADRNELLNWLRrlKPKPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETIRL 460
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 6-203 1.66e-86

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: 268.82  E-value: 1.66e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   6 TPLGAGQDVGRSCILVSLGGKNIMFDCGMHMGYDD-ARRFPDFNFIsksgnfTNAIDCIIITHFHLDHCGALPYFTEMCG 84
Cdd:cd07734    1 TPLGGGQEVGRSCFLVEFKGRTVLLDCGMNPGKEDpEACLPQFELL------PPEIDAILISHFHLDHCGALPYLFRGFI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  85 YDGPIYMTHPTKAICPILLEDYRKITVERKGETNFFTSQMIKDCMKKVVGLNVHQTVQVDEELEIRAYYAGHVLGAAMFY 164
Cdd:cd07734   75 FRGPIYATHPTVALGRLLLEDYVKSAERIGQDQSLYTPEDIEEALKHIVPLGYGQSIDLFPALSLTAYNAGHVLGAAMWE 154

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 440801023 165 VRVGDQSVVYTGDYNMTPDRHLGAAWIEKLRPDVLITES 203
Cdd:cd07734  155 IQIYGEKLVYTGDFSNTEDRLLPAASILPPRPDLLITES 193
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 3-203 4.56e-75

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: 239.02  E-value: 4.56e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   3 IKVTPLGAGQDVGRSCILVSLGGKNIMFDCGMHMGYDDARRFPDFNFISKSgnftnAIDCIIITHFHLDHCGALPYFTEM 82
Cdd:cd16292    1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSGLASLPFFDEIDLS-----EIDLLLITHFHLDHCGALPYFLQK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  83 CGYDGPIYMTHPTKAICPILLEDYRKITVErKGETNFFTSQMIKDCMKKVVGLNVHQTVQVDeELEIRAYYAGHVLGAAM 162
Cdd:cd16292   76 TNFKGRVFMTHPTKAIYKWLLSDYVRVSNI-SSDEMLYTETDLEASMDKIETIDFHQEVEVN-GIKFTAYNAGHVLGAAM 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 440801023 163 FYVRVGDQSVVYTGDYNMTPDRHLGAAWIEKLRPDVLITES 203
Cdd:cd16292  154 FMVEIAGVRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 5-203 1.15e-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: 214.25  E-value: 1.15e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   5 VTPLGAGQDVGRSCILVSLGGKNIMFDCGMHMGYDDARRFPDFNFisksGNFTNAIDCIIITHFHLDHCGALPYFTEMcG 84
Cdd:cd16295    1 LTFLGAAREVTGSCYLLETGGKRILLDCGLFQGGKELEELNNEPF----PFDPKEIDAVILTHAHLDHSGRLPLLVKE-G 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  85 YDGPIYMTHPTKAICPILLEDYRKI---TVERKGETNFFTSQMIKDCMKKVVGLNVHQTVQVDEELEIRAYYAGHVLGAA 161
Cdd:cd16295   76 FRGPIYATPATKDLAELLLLDSAKIqeeEAEHPPAEPLYTEEDVEKALKHFRPVEYGEPFEIGPGVKVTFYDAGHILGSA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 440801023 162 MFYVRVG-DQSVVYTGDYNMTPDRHLGA-AWIEklRPDVLITES 203
Cdd:cd16295  156 SVELEIGgGKRILFSGDLGRKNTPLLRDpAPPP--EADYLIMES 197
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 244-362 1.20e-41

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: 147.30  E-value: 1.20e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   244 AQELCILLETYWERMNL-TVPIYFSAGLTEKATNYYKLFIHWTNEKIKRTFV-HRNMFDFKHISTFE-----RGLADQPG 316
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEqGRNPFDFKNLKFVKsleesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 440801023   317 PMVLFATPGMLHAGTSLEVFKKWAPNEKNLVIIPGYCVVGTVGNKL 362
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 ...
 244-359 2.80e-32

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: 120.31  E-value: 2.80e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  244 AQELCILLETYWER-MNLTVPIYFSAGLTEKATNYYKLFIHWTNEKIKRTFVHRNMfdfkhistfERGLADQPGPMVLFA 322
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFVISKSE---------SKAINEGKGPKVIIA 71

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 440801023  323 TPGMLHAGTSLEVFKKWAPNEKNLVIIPGYCVVGTVG 359
Cdd:pfam10996  72 SSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLG 108
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 6-203 1.82e-28

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: 112.61  E-value: 1.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   6 TPLGAGQDVGRSCILVSLGGKNIMFDCGmhmgYDDARRFPDFNFISKsgnFTNAIDCIIITHFHLDHCGALPYfteMCGY 85
Cdd:cd16293    2 TPLSGAGDESPLCYLLEIDDVTILLDCG----WDESFDMEYLESLKR---IAPTIDAVLLSHPDLEHLGALPY---LVGK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  86 DG---PIYMTHPTKAICPI-LLEDYRKITVErkGETNFFTSQMIKDCMKKVVGLNVHQTVQV---DEELEIRAYYAGHVL 158
Cdd:cd16293   72 LGltcPVYATLPVHKMGRMfMYDLYQSRGLE--EDFNLFTLDDVDEAFDRITQLKYSQPVNLrgkGDGLTITAYNAGHTL 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 440801023 159 GAAMFYVRVGDQSVVYTGDYNMTPDRHL-GAAWIE--KLRPDVLITES 203
Cdd:cd16293  150 GGTIWKITKDSEDIVYAVDWNHKKERHLnGAVLDSfgGLRPSLLITDA 197
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 17-183 6.63e-18

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: 81.83  E-value: 6.63e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023    17 SCILVSLGGKNIMFDCGMHMGYDDARRFPDFNFisksgnftNAIDCIIITHFHLDHCGALPYFTEMcgYDGPIYMTHPTK 96
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGP--------KKIDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023    97 AicpiLLEDYRKITVERKGetnfftsqmIKDCMKKVVGLNVHQTVQV-DEELEIRaYYAGHVLGAAMFYVRvgDQSVVYT 175
Cdd:smart00849  71 E----LLKDLLALLGELGA---------EAEPAPPDRTLKDGDELDLgGGELEVI-HTPGHTPGSIVLYLP--EGKILFT 134


                   ....*...
gi 440801023   176 GDYNMTPD 183
Cdd:smart00849 135 GDLLFAGG 142
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 4-202 9.42e-17

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: 79.19  E-value: 9.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   4 KVTPLGAGQDVGRSCILVSLGGKNIMFDCGM-----------HMGYDDARRFPDFNFISKSGNFTN--------AIDCII 64
Cdd:cd07732    1 RITIHRGTNEIGGNCIEVETGGTRILLDFGLpldpeskyfdeVLDFLELGLLPDIVGLYRDPLLLGglrseedpSVDAVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  65 ITHFHLDHCGALPYFTEmcgyDGPIYMTHPTKAIcpilLEDYRKITVERKGETNFFTsqmikdcmkkvvGLNVHQTVQVD 144
Cdd:cd07732   81 LSHAHLDHYGLLNYLRP----DIPVYMGEATKRI----LKALLPFFGEGDPVPRNIR------------VFESGKSFTIG 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 440801023 145 eELEIRAYYAGH-VLGAAMFYVRVGDQSVVYTGDYNM-TPDRHLGAAWIEKLR--PDVLITE 202
Cdd:cd07732  141 -DFTVTPYLVDHsAPGAYAFLIEAPGKRIFYTGDFRFhGRKPELTEAFVEKAPknIDVLLME 201
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
3-235 1.00e-15

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 77.16  E-value: 1.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   3 IKVTPLGAG---QDVGR--SCILVSLGGKNIMFDCG-------MHMGYDDARrfpdfnfisksgnftnaIDCIIITHFHL 70
Cdd:COG1234    1 MKLTFLGTGgavPTPGRatSSYLLEAGGERLLIDCGegtqrqlLRAGLDPRD-----------------IDAIFITHLHG 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  71 DHCGALPYFTEMCGYDG-----PIYMTHPTKAIcpilLEDYRKITVERkgeTNFFTsqmikdcmkKVVGLNVHQTVQvDE 145
Cdd:COG1234   64 DHIAGLPGLLSTRSLAGrekplTIYGPPGTKEF----LEALLKASGTD---LDFPL---------EFHEIEPGEVFE-IG 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023 146 ELEIRAYYAGHVLGAAMFYVRVGDQSVVYTGD--YNmtpdrhlgAAWIEKLR-PDVLITESTYATtirdskrWRERDFLK 222
Cdd:COG1234  127 GFTVTAFPLDHPVPAYGYRFEEPGRSLVYSGDtrPC--------EALVELAKgADLLIHEATFLD-------EEAELAKE 191

                        250
                 ....*....|...
gi 440801023 223 RVHSCVEKGGKVL 235
Cdd:COG1234  192 TGHSTAKEAAELA 204
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 20-200 1.09e-15

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 75.71  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   20 LVSLGGKNIMFDCGMH--MGYDDARRFPDfNFISKsgnftnaIDCIIITHFHLDHCGALPY----FTEMCGYDGPIYMTH 93
Cdd:pfam16661   1 LLEFDNVRILLDPGWDgsFSYESDLKYLE-KILPE-------VDLILLSHPTLEHLGAYPLlyykFGSHLGSNIPVYATL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   94 PTKAICPI-LLEDYRKITVERKGETNFFTSQMIKDCMKKVVGLNVHQTVQV---DEELEIRAYYAGHVLGAAMFYVRVGD 169
Cdd:pfam16661  73 PVANLGRVsTYDLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkFDGLTITPYNSGHTLGGTIWKISKNS 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 440801023  170 QSVVYTGDYNMTPDRHL-GAAWIEK--------LRPDVLI 200
Cdd:pfam16661 153 EKIVYAVDWNHTKDSHLnGASLLDStgkpleslVRPTALI 192
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 6-178 6.51e-15

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: 74.75  E-value: 6.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   6 TPLGaGQD-VGRSCILVSLGGKNIMFDCGMHMGYDDARR----FPDFNFISKsgnFTNAIDCIIITHFHLDHCGALPYFT 80
Cdd:cd07714    1 IPLG-GLGeIGKNMYVVEYDDDIIIIDCGLKFPDEDMPGvdyiIPDFSYLEE---NKDKIKGIFITHGHEDHIGALPYLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  81 EMcgYDGPIYMTHPTKAICPILLEDYRKItverkGETNFFTsqmikdcmkkvvgLNVHQTVQVDeELEIRAYYAGH-VLG 159
Cdd:cd07714   77 PE--LNVPIYATPLTLALIKKKLEEFKLI-----KKVKLNE-------------IKPGERIKLG-DFEVEFFRVTHsIPD 135

                        170
                 ....*....|....*....
gi 440801023 160 AAMFYVRVGDQSVVYTGDY 178
Cdd:cd07714  136 SVGLAIKTPEGTIVHTGDF 154
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 16-205 6.61e-15

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 74.93  E-value: 6.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  16 RSCILVSLGGKNIMFDCGmhmgyddarrfPDF-NFISKSGNFTNAIDCIIITHFHLDHCGALPYFTEMCGYDG-PIYMTH 93
Cdd:COG1235   35 RSSILVEADGTRLLIDAG-----------PDLrEQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYGPNPiPVYATP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  94 PTKAicpILLEDYRKITVERKGETNFFTsqmikdcmkkvvgLNVHQTVQVDeELEIRAYYAGHVLGAAMFY-VRVGDQSV 172
Cdd:COG1235  104 GTLE---ALERRFPYLFAPYPGKLEFHE-------------IEPGEPFEIG-GLTVTPFPVPHDAGDPVGYrIEDGGKKL 166

                        170       180       190
                 ....*....|....*....|....*....|....
gi 440801023 173 VYTGDYNMTPDrhlgaAWIEKLR-PDVLITESTY 205
Cdd:COG1235  167 AYATDTGYIPE-----EVLELLRgADLLILDATY 195
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 379-440 7.45e-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: 69.19  E-value: 7.45e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 440801023  379 SLEVRCKVKNLS-FSAHADAKGIMQLIKMSQPANVILVHGEKGKMQSLKQRVIREFEIPCFDP 440
Cdd:pfam07521   1 GIPVRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEELGIEVFVP 63
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 5-203 2.42e-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: 71.53  E-value: 2.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   5 VTPLGAG-----QDVGRSCILVSLGGKNIMFDCGmhmgyddarrFPDFNFISKSGNFTNAIDCIIITHFHLDHCGALPYF 79
Cdd:cd16272    1 LTFLGTGgavpsLTRNTSSYLLETGGTRILLDCG----------EGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  80 TEMCGYDG-----PIYMTHPTKAicpiLLEDYRKITVERKGETNFFtsqmikdcmkKVVGLNVHQTVQVDEELEIRAYYA 154
Cdd:cd16272   71 LFARRYGGrkkplTIYGPKGIKE----FLEKLLNFPVEILPLGFPL----------EIEELEEGGEVLELGDLKVEAFPV 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 440801023 155 GHVLGAAMFYVRVGDQSVVYTGDynMTPDRHL-----GAawieklrpDVLITES 203
Cdd:cd16272  137 KHSVESLGYRIEAEGKSIVYSGD--TGPCENLvelakGA--------DLLIHEC 180
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
17-177 1.58e-13

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 69.70  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   17 SCILVSLGGKNIMFDCGMHMGYDDARRFPDFNFISKSgnftnaIDCIIITHFHLDHCGALPYFTEmcgydgpiymTHPTK 96
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLGPKD------IDAVILTHGHFDHIGGLGELAE----------ATDVP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   97 AICPIllEDYRKITVERKGETNFFTSQMIKDCMKKVVGLNVHQTVQVDEELEIRAYYAGHVLGAAMFYVRVGDQSVVYTG 176
Cdd:pfam00753  71 VIVVA--EEARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTG 148


                  .
gi 440801023  177 D 177
Cdd:pfam00753 149 D 149
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 17-206 2.37e-10

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: 61.31  E-value: 2.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  17 SCILVSLGGKNIMFDCG-------MHMGYddarRFpdfnfisksgnftNAIDCIIITHFHLDHCGALPYF---TEMCGYD 86
Cdd:cd07717   18 SSIALRLEGELWLFDCGegtqrqlLRAGL----SP-------------SKIDRIFITHLHGDHILGLPGLlstMSLLGRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  87 GP--IYMTHPTKAIcpilLEDYRKITVERKGETnfftsqmikdcmkkvvgLNVH------QTVQVDEELEIRAYYAGHVL 158
Cdd:cd07717   81 EPltIYGPKGLKEF----LETLLRLSASRLPYP-----------------IEVHelepdpGLVFEDDGFTVTAFPLDHRV 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 440801023 159 GAAMFYVRVGdQSVVYTGDyNMTPDRHLGAAWieklRPDVLITESTYA 206
Cdd:cd07717  140 PCFGYRFEEG-RKIAYLGD-TRPCEGLVELAK----GADLLIHEATFL 181
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 18-177 2.69e-09

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: 57.30  E-value: 2.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  18 CILVSLG-GKNIMFDCGMhmGYDDARRfpdfNFISKSGNftnAIDCIIITHFHLDHCGALPYFTEMcgYDGPIYMTHPTK 96
Cdd:cd06262   12 CYLVSDEeGEAILIDPGA--GALEKIL----EAIEELGL---KIKAILLTHGHFDHIGGLAELKEA--PGAPVYIHEADA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  97 AicpiLLEDyrkitverKGETNFFTSQMIKDCMKKVVGLNVHQTVQVDeELEIRAYYA-GHVLGAAMFYvrVGDQSVVYT 175
Cdd:cd06262   81 E----LLED--------PELNLAFFGGGPLPPPEPDILLEDGDTIELG-GLELEVIHTpGHTPGSVCFY--IEEEGVLFT 145


                 ..
gi 440801023 176 GD 177
Cdd:cd06262  146 GD 147
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 8-203 3.21e-09

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 56.88  E-value: 3.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   8 LGAGQDVG-----RSCILVSLGGKNIMFDCGmhmgyddARRFPDFNfisKSGNFTNAIDCIIITHFHLDHCGALPYFTEM 82
Cdd:cd07740    3 LGSGDAFGsggrlNTCFHVASEAGRFLIDCG-------ASSLIALK---RAGIDPNAIDAIFITHLHGDHFGGLPFFLLD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  83 C----GYDGPIYMTHPtkaicPILLEDYRKITverkgETNFFTSQMIKDCMK-KVVGLNVHQTVQVDeELEIRAYYAGHV 157
Cdd:cd07740   73 AqfvaKRTRPLTIAGP-----PGLRERLRRAM-----EALFPGSSKVPRRFDlEVIELEPGEPTTLG-GVTVTAFPVVHP 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 440801023 158 LGAAMFYVRVGDQ--SVVYTGDynmtpdrhlgAAWIEKLRP-----DVLITES 203
Cdd:cd07740  142 SGALPLALRLEAAgrVLAYSGD----------TEWTDALVPlargaDLFICEC 184
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 18-177 8.79e-09

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: 56.24  E-value: 8.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  18 CILVSLGGKNIMFDCGMhmGYDDARRFPDFnfISKSGNftnAIDCIIITHFHLDHCGALPYFTEmcGYDGPIYMTHPTKA 97
Cdd:COG0491   17 SYLIVGGDGAVLIDTGL--GPADAEALLAA--LAALGL---DIKAVLLTHLHPDHVGGLAALAE--AFGAPVYAHAAEAE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  98 IcpilledyrkitVERKGETNFFTSQMIKDcmkkVVGLNVHQTVQVDeELEIRAYYA-GHVLGAAMFYVRvgDQSVVYTG 176
Cdd:COG0491   88 A------------LEAPAAGALFGREPVPP----DRTLEDGDTLELG-GPGLEVIHTpGHTPGHVSFYVP--DEKVLFTG 148


                 .
gi 440801023 177 D 177
Cdd:COG0491  149 D 149
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
2-92 1.04e-08

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 58.15  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   2 DIKVTPLGaGQD-VGRSCILVSLGGKNIMFDCGM------HMGYDDArrFPDFNFISKsgnftNA--IDCIIITHFHLDH 72
Cdd:COG0595    5 KLRIIPLG-GLGeIGKNMYVYEYDDDIIIVDCGLkfpedeMPGVDLV--IPDISYLEE-----NKdkIKGIVLTHGHEDH 76

                         90       100
                 ....*....|....*....|
gi 440801023  73 CGALPYFTEMcgYDGPIYMT 92
Cdd:COG0595   77 IGALPYLLKE--LNVPVYGT 94
PRK00055 PRK00055
ribonuclease Z; Reviewed
 3-206 1.34e-08

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 56.34  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   3 IKVTPLGAGQ---DVGR--SCILVSLGGKNIMFDCG-------MHMGYddarrfpdfnfisksgNFTNaIDCIIITHFHL 70
Cdd:PRK00055   2 MELTFLGTGSgvpTPTRnvSSILLRLGGELFLFDCGegtqrqlLKTGI----------------KPRK-IDKIFITHLHG 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  71 DHCGALPYFTEMCGYDGpiyMTHPTKAICPILLEDY----RKIT------VERKGETNFFTSQMIKDcmKKVVGLNVHQT 140
Cdd:PRK00055  65 DHIFGLPGLLSTRSLSG---RTEPLTIYGPKGIKEFvetlLRASgslgyrIAEKDKPGKLDAEKLKA--LGVPPGPLFGK 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023 141 VQVDEELEiraYYAGHVLGAAMFY--VRVGdQSVVYTGDYNMTPDrhlgaawIEKL--RPDVLITESTYA 206
Cdd:PRK00055 140 LKRGEDVT---LEDGRIINPADVLgpPRKG-RKVAYCGDTRPCEA-------LVELakGADLLVHEATFG 198
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 4-177 1.84e-08

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: 54.83  E-value: 1.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   4 KVTPLGAG---QDVGR--SCILVSLGGKNIMFDCGMhmGYddARRFpdfnfiSKSGNFTNAIDCIIITHFHLDHCGALP- 77
Cdd:cd07719    1 RVTLLGTGgpiPDPDRagPSTLVVVGGRVYLVDAGS--GV--VRRL------AQAGLPLGDLDAVFLTHLHSDHVADLPa 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  78 -----YFTemcGYDGP--IYMTHPTKAICPILLEDYRKITVERKGETNFFTSQMIKDCmkKVVGLNVHQTVQVDEELEIR 150
Cdd:cd07719   71 llltaWLA---GRKTPlpVYGPPGTRALVDGLLAAYALDIDYRARIGDEGRPDPGALV--EVHEIAAGGVVYEDDGVKVT 145

                        170       180
                 ....*....|....*....|....*....
gi 440801023 151 AYYAGH--VLGAAMFYVRVGDQSVVYTGD 177
Cdd:cd07719  146 AFLVDHgpVPPALAYRFDTPGRSVVFSGD 174
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 4-205 1.18e-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: 53.37  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   4 KVTPLGA--GQDVGR-SCILVSLGGKN--IMFDCGMHMG---YDDARRFPDFNFISKSGNFTNAIDCIIITHFHLDHCGA 75
Cdd:cd07735    2 ELVVLGCsgGPDEGNtSSFLLDPAGSDgdILLDAGTGVGalsLEEMFNDILFPSQKAAYELYQRIRHYLITHAHLDHIAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  76 LPYFTEMCGYDG----PIYMTHPTKAicpILLEDYrkitverkgetnF-------FTSQMIKDCM-KKVVGLNVHQTVQV 143
Cdd:cd07735   82 LPLLSPNDGGQRgspkTIYGLPETID---ALKKHI------------FnwviwpdFTSIPSGKYPyLRLEPIEPEYPIAL 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 440801023 144 DeELEIRAYYAGH-VLGAAMFYVRVGDQSVVYTGDynMTPD------------RHLGAAWIEKLRpdVLITESTY 205
Cdd:cd07735  147 T-GLSVTAFPVSHgVPVSTAFLIRDGGDSFLFFGD--TGPDsvsksprldalwRALAPLIPKKLK--AIIIECSF 216
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 17-195 1.32e-07

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: 52.99  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  17 SCILVSLGGKNIMFDCGMHmgyDDARRFPDFNFISKSGNFTNA----------------IDCIIITHFHLDHCGALPYFT 80
Cdd:cd07729   33 YAYLIEHPEGTILVDTGFH---PDAADDPGGLELAFPPGVTEEqtleeqlarlgldpedIDYVILSHLHFDHAGGLDLFP 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  81 emcgyDGPIYMThptkaicpilLEDYRKITverkgETNFFTSQMIKDCMKKVVGLNVHQTVQVDEELE----IRAYYA-G 155
Cdd:cd07729  110 -----NATIIVQ----------RAELEYAT-----GPDPLAAGYYEDVLALDDDLPGGRVRLVDGDYDlfpgVTLIPTpG 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 440801023 156 HVLGAAMFYVRVGDQSVVYTGD-----YNMTPDRHLGAAW--------IEKLR 195
Cdd:cd07729  170 HTPGHQSVLVRLPEGTVLLAGDaaytyENLEEGRPPGINYdpeaalasLERLK 222
Int9-like_MBL-fold cd16294
integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ...
 11-161 1.87e-07

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: 51.34  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  11 GQDVGRSCILVSLGGKNIMFDCGMHMgyddarrFPDFNFISKSgnftnAIDCIIITHFHldHCGALPYFTEMCGYDGPIY 90
Cdd:cd16294    7 SGHPTLPCNVLKFKSTTIMLDCGLDC-------PPETELIDLS-----TVDVILISNYH--CMLALPFITEYTGFTGVVY 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 440801023  91 MTHPTKAICPILLEDyrkitverkgetnfftsqmIKDCMKKVVGLNVHQTVQVDEELEIRAYYAGHVLGAA 161
Cdd:cd16294   73 ATEPTVQIGRLLMEE-------------------LVQALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSS 124
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 16-95 2.63e-07

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: 51.32  E-value: 2.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  16 RSCILVSLGGKNIMFDCGmhmgyddarrfPDF------NFISKsgnftnaIDCIIITHFHLDHCGALP---YFTEMCGYD 86
Cdd:cd16279   35 RSSILIETGGKNILIDTG-----------PDFrqqalrAGIRK-------LDAVLLTHAHADHIHGLDdlrPFNRLQQRP 96


                 ....*....
gi 440801023  87 GPIYMTHPT 95
Cdd:cd16279   97 IPVYASEET 105
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 4-203 3.82e-07

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: 50.52  E-value: 3.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   4 KVTPLG-----AGQDVGRSCILVSLGGKNIMFDCGmhmgyddarrfpdfnfiskSGNFTN--------AIDCIIITHFHL 70
Cdd:cd07716    1 KLTVLGcsgsyPGPGGACSGYLLEADGFRILLDCG-------------------SGVLSRlqryidpeDLDAVVLSHLHP 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  71 DHC---GALPYFTEMCGYDGPiymTHPTKAICPilledyrKITVERKGETNFFTSQMikdcmkKVVGLNVHQTVQVDeEL 147
Cdd:cd07716   62 DHCadlGVLQYARRYHPRGAR---KPPLPLYGP-------AGPAERLAALYGLEDVF------DFHPIEPGEPLEIG-PF 124

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 440801023 148 EIRAYYAGHVLGAAMFYVRVGDQSVVYTGDYNMTPdrhlgaAWIEKLR-PDVLITES 203
Cdd:cd07716  125 TITFFRTVHPVPCYAMRIEDGGKVLVYTGDTGYCD------ELVEFARgADLLLCEA 175
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 13-78 5.68e-07

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: 51.40  E-value: 5.68e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 440801023  13 DVGR-SCILVSLG-GKNIMFDCGMHMGYDDARRFPDfNFISKSGnfTNAIDCIIITHFHLDHCGALPY 78
Cdd:COG2333    7 DVGQgDAILIRTPdGKTILIDTGPRPSFDAGERVVL-PYLRALG--IRRLDLLVLTHPDADHIGGLAA 71
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 18-94 1.36e-06

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: 50.31  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  18 CILVSLGGKNIMFDCGmhmgYDDArrfpdfnFISksgnftNA---------IDCIIITHFHLDHCGALPYFTEMCGyDGP 88
Cdd:cd07713   22 SLLIETEGKKILFDTG----QSGV-------LLH------NAkklgidlsdIDAVVLSHGHYDHTGGLKALLELNP-KAP 83


                 ....*.
gi 440801023  89 IYMtHP 94
Cdd:cd07713   84 VYA-HP 88
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 17-205 1.86e-06

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: 49.03  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  17 SCILVSLGGKNIMFDCGMhmGyddARRFPdfNFISKSGNFTNAIdcIIITHFHLDH-CGaLPYFTemcgydgPIYMTHpt 95
Cdd:cd07715   24 SCVEVRAGGELLILDAGT--G---IRELG--NELMKEGPPGEAH--LLLSHTHWDHiQG-FPFFA-------PAYDPG-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  96 kaicpilledyRKITV-----ERKGETNFFTSQM--------IKDCMKKV--VGLNVHQTVQVDeELEIRAYYAGHVLGA 160
Cdd:cd07715   85 -----------NRIHIygphkDGGSLEEVLRRQMsppyfpvpLEELLAAIefHDLEPGEPFSIG-GVTVTTIPLNHPGGA 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 440801023 161 AMFYVRVGDQSVVYTGDYNMTP-DRHLGAAWIEKLR-PDVLITESTY 205
Cdd:cd07715  153 LGYRIEEDGKSVVYATDTEHYPdDGESDEALLEFARgADLLIHDAQY 199
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 13-78 2.37e-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: 48.28  E-value: 2.37e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 440801023  13 DVGRS-CILVSLGGKNIMFDCGMHMGYDDARRFPdfnFISKSGNftNAIDCIIITHFHLDHCGALPY 78
Cdd:cd07731    6 DVGQGdAILIQTPGKTILIDTGPRDSFGEDVVVP---YLKARGI--KKLDYLILTHPDADHIGGLDA 67
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 2-200 6.25e-06

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 47.60  E-value: 6.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   2 DIKVTPLGAgqdvgrSCILVSLGGKNIMFDcgmhmgyddarrfPdfnFISKSGNFTN----------AIDCIIITHFHLD 71
Cdd:COG2220    3 GMKITWLGH------ATFLIETGGKRILID-------------P---VFSGRASPVNplpldpedlpKIDAVLVTHDHYD 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  72 HCG-----ALPyftemcgydgpiymTHPTKAICPILLEDYrkitVERKGETNfftsqmikdcmkkVVGLNVHQTVQVDeE 146
Cdd:COG2220   61 HLDdatlrALK--------------RTGATVVAPLGVAAW----LRAWGFPR-------------VTELDWGESVELG-G 108

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 440801023 147 LEIRAYYAGH--------VLGAAMFYVRVGDQSVVYTGDYNMTPD-RHLGaawiEKLRPDVLI 200
Cdd:COG2220  109 LTVTAVPARHssgrpdrnGGLWVGFVIETDGKTIYHAGDTGYFPEmKEIG----ERFPIDVAL 167
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
18-94 9.61e-06

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 47.57  E-value: 9.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  18 CILVSLGGKNIMFDCG-----MH----MGYDdarrfpdfnfisksgnfTNAIDCIIITHFHLDHCGALPYFTEMCGyDGP 88
Cdd:COG1237   24 SALIETEGKRILFDTGqsdvlLKnaekLGID-----------------LSDIDAVVLSHGHYDHTGGLPALLELNP-KAP 85


                 ....*.
gi 440801023  89 IYMtHP 94
Cdd:COG1237   86 VYA-HP 90
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 47-205 1.54e-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: 45.61  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  47 FNFISKSGnftnaIDCIIITHFHLDHCGAL-PYFTEmcgydGPIYMTHPTKaicpILLEDyrKITVERKgetnfftsqmi 125
Cdd:cd16273   29 FKYGKIPG-----ISAYFLSHFHSDHYGGLtKSWSH-----GPIYCSEITA----NLVKL--KLKVDEE----------- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023 126 kdcmkKVVGLNVHQTVQVDEELEIRAYYAGHVLGAAMFYVRVGD-QSVVYTGDYNMTPDRHLGAAWIEKLRPDVLITEST 204
Cdd:cd16273   82 -----YIVVLPMNTPVEIDGDVSVTLLDANHCPGAVMFLFELPDgRRILHTGDFRANPEMLEHPLLLGKRRIDTVYLDTT 156


                 .
gi 440801023 205 Y 205
Cdd:cd16273  157 Y 157
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 20-81 7.71e-05

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 43.83  E-value: 7.71e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 440801023  20 LVSLGGKNIMFDCGMHMgYDDARRFpdFNFISKSGNFTNAIDCIIITHFHLDHCGALPYFTE 81
Cdd:cd07725   19 LLRDGDETTLIDTGLAT-EEDAEAL--WEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQE 77
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 17-93 3.24e-04

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 42.19  E-value: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  17 SCILVSLGGKNIMFDCGMhmgyddarrFPDFNFI----SKSGNFTNAIDCIIITHFHLDHCGALPYFTEMCGYDGPIYMT 92
Cdd:cd07711   23 TVTLIKDGGKNILVDTGT---------PWDRDLLlkalAEHGLSPEDIDYVVLTHGHPDHIGNLNLFPNATVIVGWDICG 93


                 .
gi 440801023  93 H 93
Cdd:cd07711   94 D 94
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 17-177 3.68e-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: 42.15  E-value: 3.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  17 SCILVSL-GGKNIMFDCG------MHmgyddaRRFP---DFNFISKsgnftnaIDCIIITHFHLDHCGALPYFTEM---- 82
Cdd:cd07718   18 SGILLRIpGDGSILLDCGegtlgqLR------RHYGpeeADEVLRN-------LKCIFISHLHADHHLGLIRLLAErkkl 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  83 -CGYDGPIYMTHPTK---------AICPILLEDYRKITVERKGET---NFFTSQMIKDCMKKVVGLNVHQTVQVDeelei 149
Cdd:cd07718   85 fKPPSPPLYVVAPRQlrrwlreysSLEDLGLHDISFISNRVSQSLpesDDPLSRDLLSNLLEELGLKSIETVPVI----- 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 440801023 150 rayyagHVLGAamFYVRVGDQ---SVVYTGD 177
Cdd:cd07718  160 ------HCPDA--YGIVLTHEdgwKIVYSGD 182
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 18-76 5.38e-04

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. 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: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 41.45  E-value: 5.38e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 440801023  18 CILVSLGGKNIMFDCGMHmgyDDARRFPdfnfisksgnfTNAIDCIIITHFHLDHCGAL 76
Cdd:cd07736   39 SALIEVDGERILLDAGLT---DLAERFP-----------PGSIDAILLTHFHMDHVQGL 83
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 20-156 5.43e-04

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 41.36  E-value: 5.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  20 LVSLGGKNIMFDCGMHM-GYDDARRfpdfNFISKSGNFTnaIDCIIITHFHLDHCGALPYFTEMCGYDGPIYMTHPTKAI 98
Cdd:cd07722   22 LVGTGKRRILIDTGEGRpSYIPLLK----SVLDSEGNAT--ISDILLTHWHHDHVGGLPDVLDLLRGPSPRVYKFPRPEE 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 440801023  99 CPILLEDYRKItverkgetnfftsqmikdcmkkvVGLNVHQTVQVdEELEIRAYYA-GH 156
Cdd:cd07722   96 DEDPDEDGGDI-----------------------HDLQDGQVFKV-EGATLRVIHTpGH 130
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 17-76 8.45e-04

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: 41.38  E-value: 8.45e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 440801023  17 SCILVSLGGKNIMFDCGM--HMGyDDARRFPDfNfISKSGNFTNAIDCIIITHFHLDHCGAL 76
Cdd:cd07720   50 NAFLVRTGGRLILVDTGAggLFG-PTAGKLLA-N-LAAAGIDPEDIDDVLLTHLHPDHIGGL 108
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 60-177 9.26e-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) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 40.98  E-value: 9.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  60 IDCIIITHFHLDHCGALPYFTEMCG---YDGPI---YMTHPTkaICPILLEDYRKItverKGETNFFtsQMIKDCMkkvv 133
Cdd:cd07743   46 LKAIINTHSHADHIGGNAYLQKKTGckvYAPKIekaFIENPL--LEPSYLGGAYPP----KELRNKF--LMAKPSK---- 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 440801023 134 glnVHQTVQ------VDEELEIRAyYAGHVLGaaMFYVRVGDqSVVYTGD 177
Cdd:cd07743  114 ---VDDIIEegelelGGVGLEIIP-LPGHSFG--QIGILTPD-GVLFAGD 156
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-74 1.10e-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: 293839  Cd Length: 252  Bit Score: 41.33  E-value: 1.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 440801023  18 CILVSLGGKNIMFDCGMHMGYDDA-----RRFPDFNF---ISKSGNFTNAIDCIIITHFHLDHCG 74
Cdd:cd16281   45 CLLIETGGRNILIDTGIGDKQDPKfrsiyVQHSEHSLlksLARLGLSPEDITDVILTHLHFDHCG 109
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 63-200 1.75e-03

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 40.24  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  63 IIITHFHLDHCGALPYFTEMcgyDGPIYMTHPT----KAICPILLEDYRKITVERKGETNF------FTSQMIKDcmkkv 132
Cdd:cd16282   56 VVNTHYHGDHTLGNAAFADA---GAPIIAHENTreelAARGEAYLELMRRLGGDAMAGTELvlpdrtFDDGLTLD----- 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 440801023 133 VGlnvhqtvqvDEELEIRAYYAGHVLGAAMFYVRvgDQSVVYTGD--YNMTPDRHLGA---AWIE------KLRPDVLI 200
Cdd:cd16282  128 LG---------GRTVELIHLGPAHTPGDLVVWLP--EEGVLFAGDlvFNGRIPFLPDGslaGWIAaldrllALDATVVV 195
PRK02113 PRK02113
MBL fold metallo-hydrolase;
16-90 2.01e-03

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 40.54  E-value: 2.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 440801023  16 RSCILVSLGGKNIMFDCGmhmgyddarrfPDFNFISKSGNFtNAIDCIIITHFHLDHCGALPYFTEMCGY-DGPIY 90
Cdd:PRK02113  35 RTSALVETEGARILIDCG-----------PDFREQMLRLPF-GKIDAVLITHEHYDHVGGLDDLRPFCRFgEVPIY 98
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 18-94 2.75e-03

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 39.51  E-value: 2.75e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 440801023  18 CILVSLGGKNIMFDCGMHMGYDDARRFpdfnfISKSGNFTNAIDCIIITHFHLDHCGALPYFTEMcgYDGPIYMtHP 94
Cdd:cd07721   13 AYLIEDDDGLTLIDTGLPGSAKRILKA-----LRELGLSPKDIRRILLTHGHIDHIGSLAALKEA--PGAPVYA-HE 81
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 60-238 3.58e-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: 39.22  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023   60 IDCIIITHFHLDHCGALPYFTEMCGydGPIYMTHPTKAicpILledyrkitverkgETNFFTSQMIKDCMKKVVGLNVHQ 139
Cdd:pfam12706  29 IDAVLLTHDHYDHLAGLLDLREGRP--RPLYAPLGVLA---HL-------------RRNFPYLFLLEHYGVRVHEIDWGE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440801023  140 TVQV-DEELEIRA------------YYAGHVLGaamFYVRVGDQSVVYTGDYNMTPDrHLGaawiEKLRP-DVLITESTY 205
Cdd:pfam12706  91 SFTVgDGGLTVTAtparhgsprgldPNPGDTLG---FRIEGPGKRVYYAGDTGYFPD-EIG----ERLGGaDLLLLDGGA 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 440801023  206 attirdskrWRERDFLKRVHSCVEK--------GGKVLIPV 238
Cdd:pfam12706 163 ---------WRDDEMIHMGHMTPEEaveaaadlGARRKVLI 194
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 25-80 7.24e-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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 38.79  E-value: 7.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 440801023  25 GKNIMFDCGMHMGYDDA-RRFPdfNFISKSGNFTNA-----------------IDCIIITHFHLDHCGALPYFT 80
Cdd:cd07730   33 GGKILFDLGYRKDFEEYtPRVP--ERLYRTPVPLEVeedvaeqlaaggidpedIDAVILSHLHWDHIGGLSDFP 104
 
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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