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Conserved domains on  [gi|1953806504|gb|KAG0800188|]
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hypothetical protein G6F22_002480 [Rhizopus arrhizus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 5-203 1.18e-162

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: 463.66  E-value: 1.18e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   5 VVPLGAGQDVGRSCVLVTIGGKNIMFDCGMHMGYSDARRFPDFSYISKTGNFTDIIDAVIISHFHLDHCGALPFFTEMLG 84
Cdd:cd16291     1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  85 YDGPIYMTHPTKAICPILLEDYRKITVERKGETNFFTSAMIKNCMKKVHAVSLHQTIKVDDELEIKAYYAGHVLGAAMFY 164
Cdd:cd16291    81 YDGPIYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1953806504 165 VRVGQESVVYTGDYNMTPDRHLGSAWIDKVRPDVLITES 203
Cdd:cd16291   161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 4-416 2.79e-119

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


:

Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 360.66  E-value: 2.79e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   4 EVVPLGAGQDVGRSCVLVTIGGKNIMFDCGMHMGYsDARRFPDFSYISKTgnftdiIDAVIISHFHLDHCGALPFFTEMl 83
Cdd:COG1236     2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGG-KERNWPPFPFRPSD------VDAVVLTHAHLDHSGALPLLVKE- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  84 GYDGPIYMTHPTKAICPILLEDYRKITVERKGETNFFTSAMIKNCMKKVHAVSLHQTIKVDDeLEIKAYYAGHVLGAAMF 163
Cdd:COG1236    74 GFRGPIYATPATADLARILLGDSAKIQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 164 YVRVGQESVVYTGDYNMTPDRHLGSAwiDKVRP-DVLITESTYATTIRDSKRSRERDFLTKVHECVLNGGNVIIPVFALG 242
Cdd:COG1236   153 ELEVGGKRIVFSGDYGREDDPLLAPP--EPVPPaDVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALG 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 243 RAQE-LCILIESYWDRMGLDVPIYFStGLTERATEFYKLFINWTNQkikstfSQRNMFDFKH---IKTWN-RNYIDQPGP 317
Cdd:COG1236   231 RAQElLYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHGEYLRD------EAQDPFALPNlrfVTSVEeSKALNRKGP 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 318 KVLFATPGMLNAGTSLEVFKKWAPDPKNMVIMPGFCVAGTVGSKVLLGQKVIEIDKfTRFEVNLQVRNL-SFSAHADAKG 396
Cdd:COG1236   304 AIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIFG-EEVPVRARVERLfGLSAHADWDE 382

                         410       420
                  ....*....|....*....|.
gi 1953806504 397 IMQLIRQCE-PRNVVLVHGER 416
Cdd:COG1236   383 LLEWIKATGkPERVFLVHGEP 403
 
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 1.18e-162

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: 463.66  E-value: 1.18e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   5 VVPLGAGQDVGRSCVLVTIGGKNIMFDCGMHMGYSDARRFPDFSYISKTGNFTDIIDAVIISHFHLDHCGALPFFTEMLG 84
Cdd:cd16291     1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  85 YDGPIYMTHPTKAICPILLEDYRKITVERKGETNFFTSAMIKNCMKKVHAVSLHQTIKVDDELEIKAYYAGHVLGAAMFY 164
Cdd:cd16291    81 YDGPIYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1953806504 165 VRVGQESVVYTGDYNMTPDRHLGSAWIDKVRPDVLITES 203
Cdd:cd16291   161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 4-416 2.79e-119

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 360.66  E-value: 2.79e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   4 EVVPLGAGQDVGRSCVLVTIGGKNIMFDCGMHMGYsDARRFPDFSYISKTgnftdiIDAVIISHFHLDHCGALPFFTEMl 83
Cdd:COG1236     2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGG-KERNWPPFPFRPSD------VDAVVLTHAHLDHSGALPLLVKE- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  84 GYDGPIYMTHPTKAICPILLEDYRKITVERKGETNFFTSAMIKNCMKKVHAVSLHQTIKVDDeLEIKAYYAGHVLGAAMF 163
Cdd:COG1236    74 GFRGPIYATPATADLARILLGDSAKIQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 164 YVRVGQESVVYTGDYNMTPDRHLGSAwiDKVRP-DVLITESTYATTIRDSKRSRERDFLTKVHECVLNGGNVIIPVFALG 242
Cdd:COG1236   153 ELEVGGKRIVFSGDYGREDDPLLAPP--EPVPPaDVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALG 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 243 RAQE-LCILIESYWDRMGLDVPIYFStGLTERATEFYKLFINWTNQkikstfSQRNMFDFKH---IKTWN-RNYIDQPGP 317
Cdd:COG1236   231 RAQElLYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHGEYLRD------EAQDPFALPNlrfVTSVEeSKALNRKGP 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 318 KVLFATPGMLNAGTSLEVFKKWAPDPKNMVIMPGFCVAGTVGSKVLLGQKVIEIDKfTRFEVNLQVRNL-SFSAHADAKG 396
Cdd:COG1236   304 AIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIFG-EEVPVRARVERLfGLSAHADWDE 382

                         410       420
                  ....*....|....*....|.
gi 1953806504 397 IMQLIRQCE-PRNVVLVHGER 416
Cdd:COG1236   383 LLEWIKATGkPERVFLVHGEP 403
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 244-362 4.14e-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: 145.38  E-value: 4.14e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  244 AQELCILIESYWDRMGL-DVPIYFSTGLTERATEFYKLFINWTNQKIKSTFSQ-RNMFDFKHIK---TWN--RNYIDQPG 316
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKfvkSLEesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1953806504  317 PKVLFATPGMLNAGTSLEVFKKWAPDPKNMVIMPGFCVAGTVGSKV 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 3.97e-30

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: 114.15  E-value: 3.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 244 AQELCILIESYWDR-MGLDVPIYFSTGLTERATEFYKLFINWTNQKIKSTF-----SQRNMFDfkhiktwnrnyidqPGP 317
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFViskseSKAINEG--------------KGP 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1953806504 318 KVLFATPGMLNAGTSLEVFKKWAPDPKNMVIMPGFCVAGTVG 359
Cdd:pfam10996  67 KVIIASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLG 108
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 17-183 2.08e-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: 83.37  E-value: 2.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   17 SCVLVTIGGKNIMFDCGMHMGYSDARRFPDFSYISktgnftdiIDAVIISHFHLDHCGALPFFTEMlgYDGPIYMTHPTK 96
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKK--------IDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   97 AicpiLLEDYRKITVERKGetnfftsamIKNCMKKVHAVSLHQTIKVDDElEIKAYYA-GHVLGAAMFYVRvgQESVVYT 175
Cdd:smart00849  71 E----LLKDLLALLGELGA---------EAEPAPPDRTLKDGDELDLGGG-ELEVIHTpGHTPGSIVLYLP--EGKILFT 134


                   ....*...
gi 1953806504  176 GDYNMTPD 183
Cdd:smart00849 135 GDLLFAGG 142
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 20-200 2.19e-17

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 80.72  E-value: 2.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  20 LVTIGGKNIMFDCGMH--MGYSDARRFPDfSYISKtgnftdiIDAVIISHFHLDHCGALPF----FTEMLGYDGPIYMTH 93
Cdd:pfam16661   1 LLEFDNVRILLDPGWDgsFSYESDLKYLE-KILPE-------VDLILLSHPTLEHLGAYPLlyykFGSHLGSNIPVYATL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  94 PTKAICPI-LLEDYRKITVERKGETNFFTSAMIKNCMKKVHAVSLHQTIKV---DDELEIKAYYAGHVLGAAMFYVRVGQ 169
Cdd:pfam16661  73 PVANLGRVsTYDLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkFDGLTITPYNSGHTLGGTIWKISKNS 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1953806504 170 ESVVYTGDYNMTPDRHL-GSAWIDK--------VRPDVLI 200
Cdd:pfam16661 153 EKIVYAVDWNHTKDSHLnGASLLDStgkpleslVRPTALI 192
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 16-205 6.72e-17

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 81.09  E-value: 6.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  16 RSCVLVTIGGKNIMFDCGmhmgysdarrfPDFSYISKTGNFTDI-IDAVIISHFHLDHCGALPFFTEMLGYDG-PIYMTH 93
Cdd:COG1235    35 RSSILVEADGTRLLIDAG-----------PDLREQLLRLGLDPSkIDAILLTHEHADHIAGLDDLRPRYGPNPiPVYATP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  94 PTKAICpilledyrkitverkgETNFFTSAMIKNCMKKVHAVSLHQTIKVDDeLEIKAYYAGHVLGAAMFY-VRVGQESV 172
Cdd:COG1235   104 GTLEAL----------------ERRFPYLFAPYPGKLEFHEIEPGEPFEIGG-LTVTPFPVPHDAGDPVGYrIEDGGKKL 166

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1953806504 173 VYTGDYNMTPDRHLgsAWIDKVrpDVLITESTY 205
Cdd:COG1235   167 AYATDTGYIPEEVL--ELLRGA--DLLILDATY 195
PRK00055 PRK00055
ribonuclease Z; Reviewed
 3-218 5.47e-10

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 60.58  E-value: 5.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   3 IEVVPLGAGQ---DVGR--SCVLVTIGGKNIMFDCG-------MHMGYSdarrfpdfsyisktgnFTDIiDAVIISHFHL 70
Cdd:PRK00055    2 MELTFLGTGSgvpTPTRnvSSILLRLGGELFLFDCGegtqrqlLKTGIK----------------PRKI-DKIFITHLHG 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  71 DHCGALPFFTEMLGYDGpiyMTHPTKAICPILLEDY----RKIT------VERKGETNFFTSAMIKNcmKKVHAVSLHQT 140
Cdd:PRK00055   65 DHIFGLPGLLSTRSLSG---RTEPLTIYGPKGIKEFvetlLRASgslgyrIAEKDKPGKLDAEKLKA--LGVPPGPLFGK 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 141 IKVDDELEikaYYAGHVLGAAMFY--VRVGQeSVVYTGDYNMTPDRHlgsAWIDKVrpDVLITESTYATTirDSKRSRER 218
Cdd:PRK00055  140 LKRGEDVT---LEDGRIINPADVLgpPRKGR-KVAYCGDTRPCEALV---ELAKGA--DLLVHEATFGDE--DEELAKEY 208
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 17-156 4.32e-04

ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN. [Transcription, RNA processing]


Pssm-ID: 274246 [Multi-domain]  Cd Length: 299  Bit Score: 42.59  E-value: 4.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  17 SCVLVTIGGKNIMFDCG----MHMGYSDARrfpdfsyisktgnFTDIiDAVIISHFHLDHCGALPFFTEMLGYDGpiyMT 92
Cdd:TIGR02651  19 PSIALKLNGELWLFDCGegtqRQMLRSGIS-------------PMKI-DRIFITHLHGDHILGLPGLLSTMSFQG---RK 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953806504  93 HPTKAICPILLEDYRKiTVERKGETNFftsamikNCMKKVHAVSLHQTIKVDDELEIKAYYAGH 156
Cdd:TIGR02651  82 EPLTIYGPPGIKEFIE-TSLRVSYTYL-------NYPIKIHEIEEGGLVFEDDGFKVEAFPLDH 137
 
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 1.18e-162

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: 463.66  E-value: 1.18e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   5 VVPLGAGQDVGRSCVLVTIGGKNIMFDCGMHMGYSDARRFPDFSYISKTGNFTDIIDAVIISHFHLDHCGALPFFTEMLG 84
Cdd:cd16291     1 VTPLGAGQDVGRSCILVTIGGKNIMFDCGMHMGYNDERRFPDFSYISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  85 YDGPIYMTHPTKAICPILLEDYRKITVERKGETNFFTSAMIKNCMKKVHAVSLHQTIKVDDELEIKAYYAGHVLGAAMFY 164
Cdd:cd16291    81 YDGPIYMTHPTKAICPILLEDYRKIAVERKGETNFFTSQMIKDCMKKVIAVNLHETVQVDDELEIKAYYAGHVLGAAMFY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1953806504 165 VRVGQESVVYTGDYNMTPDRHLGSAWIDKVRPDVLITES 203
Cdd:cd16291   161 VRVGDESVVYTGDYNMTPDRHLGAAWIDRLRPDLLITES 199
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 4-416 2.79e-119

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 360.66  E-value: 2.79e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   4 EVVPLGAGQDVGRSCVLVTIGGKNIMFDCGMHMGYsDARRFPDFSYISKTgnftdiIDAVIISHFHLDHCGALPFFTEMl 83
Cdd:COG1236     2 KLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGG-KERNWPPFPFRPSD------VDAVVLTHAHLDHSGALPLLVKE- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  84 GYDGPIYMTHPTKAICPILLEDYRKITVERKGETNFFTSAMIKNCMKKVHAVSLHQTIKVDDeLEIKAYYAGHVLGAAMF 163
Cdd:COG1236    74 GFRGPIYATPATADLARILLGDSAKIQEEEAEAEPLYTEEDAERALELFQTVDYGEPFEIGG-VRVTFHPAGHILGSAQV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 164 YVRVGQESVVYTGDYNMTPDRHLGSAwiDKVRP-DVLITESTYATTIRDSKRSRERDFLTKVHECVLNGGNVIIPVFALG 242
Cdd:COG1236   153 ELEVGGKRIVFSGDYGREDDPLLAPP--EPVPPaDVLITESTYGDRLHPPREEVEAELAEWVRETLARGGTVLIPAFALG 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 243 RAQE-LCILIESYWDRMGLDVPIYFStGLTERATEFYKLFINWTNQkikstfSQRNMFDFKH---IKTWN-RNYIDQPGP 317
Cdd:COG1236   231 RAQElLYLLRELKKEGRLPDIPIYVS-GMAIRATEIYRRHGEYLRD------EAQDPFALPNlrfVTSVEeSKALNRKGP 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 318 KVLFATPGMLNAGTSLEVFKKWAPDPKNMVIMPGFCVAGTVGSKVLLGQKVIEIDKfTRFEVNLQVRNL-SFSAHADAKG 396
Cdd:COG1236   304 AIIIAPSGMLTGGRILHHLKRFLWDPRNTILFVGYQAEGTLGRRLLRGAKEVKIFG-EEVPVRARVERLfGLSAHADWDE 382

                         410       420
                  ....*....|....*....|.
gi 1953806504 397 IMQLIRQCE-PRNVVLVHGER 416
Cdd:COG1236   383 LLEWIKATGkPERVFLVHGEP 403
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 8-445 2.25e-105

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: 326.70  E-value: 2.25e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   8 LGAGQDVGRSCVLVTIGGKNIMFDCGMHMGYSDARRFP--DFSYISKTgnftdiIDAVIISHFHLDHCGALPFFTEMlGY 85
Cdd:COG1782     6 LGAAREVTGSCHLLETGESRILLDCGLFQGGREERERNndAFPFDPEE------LDAVVLTHAHLDHSGLLPLLVKY-GY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  86 DGPIYMTHPTKAICPILLEDYRKITVE------RKGETN------FFTSAMIKNCMKKVHAVSLHQTIKVDDELEIKAYY 153
Cdd:COG1782    79 RGPIYCTPPTRDLMALLLLDSAKIQEEeaeyanKKRYSGhppvepLYTEKDVEKALKHFITLDYGEVTDIAPDIKLTFYN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 154 AGHVLGAAMFYVRVGQE--SVVYTGDYNMTPDRHLGSAWIDKvRPDVLITESTYATTIRDSKRSRERDFLTKVHECVLNG 231
Cdd:COG1782   159 AGHILGSAIVHLHIGDGlhNIVFSGDLGRGKTPLLRPPTPFP-RADTLIMESTYGGRLHPSREEAEEELAKVINETIERG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 232 GNVIIPVFALGRAQELCILIESYWDRMGL-DVPIYFSTGLTERATEFYKLFINWTNQKIKST-FSQRNMFDFKHIKTWNR 309
Cdd:COG1782   238 GKVLIPAFAVGRTQEILYVLNELMREGKIpEVPVYLDSPMAIEATAIHTAYPEYLDEELRDLiFKGENPFLFENLHYVES 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 310 NY-----IDQPGPKVLFATPGMLNAGTSLEVFKKWAPDPKNMVIMPGFCVAGTVGSKVLLGQKVIEIDKfTRFEVNLQVR 384
Cdd:COG1782   318 VEeskeiNDSDEPAIIIATSGMLTGGRILHHLKHLAPDPKNTILFVGYQAEGTLGRRLLDGAKEVKIFG-ETIPVRAEVE 396

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953806504 385 NL-SFSAHADAKGIMQLIRQCE--PRNVVLVHGERGKMNFLSSKIMKEFAIPCYMPANGCSIKM 445
Cdd:COG1782   397 TIdGFSGHADRNELLNWLRRLKpkPKKVFLVHGEPEAAEALASSIRKKLGIEVVIPENLETIRL 460
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 6-203 4.96e-83

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: 259.19  E-value: 4.96e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   6 VPLGAGQDVGRSCVLVTIGGKNIMFDCGMHMGYSDarrfpDFSYISKTGNFTDIIDAVIISHFHLDHCGALPFFTEMLGY 85
Cdd:cd07734     1 TPLGGGQEVGRSCFLVEFKGRTVLLDCGMNPGKED-----PEACLPQFELLPPEIDAILISHFHLDHCGALPYLFRGFIF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  86 DGPIYMTHPTKAICPILLEDYRKITVERKGETNFFTSAMIKNCMKKVHAVSLHQTIKVDDELEIKAYYAGHVLGAAMFYV 165
Cdd:cd07734    76 RGPIYATHPTVALGRLLLEDYVKSAERIGQDQSLYTPEDIEEALKHIVPLGYGQSIDLFPALSLTAYNAGHVLGAAMWEI 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1953806504 166 RVGQESVVYTGDYNMTPDRHLGSAWIDKVRPDVLITES 203
Cdd:cd07734   156 QIYGEKLVYTGDFSNTEDRLLPAASILPPRPDLLITES 193
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 3-203 2.65e-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: 2.65e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   3 IEVVPLGAGQDVGRSCVLVTIGGKNIMFDCGMHMGYS--DARRFPDFSYISKtgnftdiIDAVIISHFHLDHCGALPFFT 80
Cdd:cd16292     1 LEITPLGAGQEVGRSCVILEFKGKTIMLDCGIHPGYSglASLPFFDEIDLSE-------IDLLLITHFHLDHCGALPYFL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  81 EMLGYDGPIYMTHPTKAICPILLEDYRKITVErKGETNFFTSAMIKNCMKKVHAVSLHQTIKVDDeLEIKAYYAGHVLGA 160
Cdd:cd16292    74 QKTNFKGRVFMTHPTKAIYKWLLSDYVRVSNI-SSDEMLYTETDLEASMDKIETIDFHQEVEVNG-IKFTAYNAGHVLGA 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1953806504 161 AMFYVRVGQESVVYTGDYNMTPDRHLGSAWIDKVRPDVLITES 203
Cdd:cd16292   152 AMFMVEIAGVRVLYTGDYSREEDRHLPAAEIPPIKPDVLIVES 194
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 5-203 2.25e-64

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: 210.39  E-value: 2.25e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   5 VVPLGAGQDVGRSCVLVTIGGKNIMFDCGMHMGYSDARR--FPDFSYISKTgnftdiIDAVIISHFHLDHCGALPFFTEM 82
Cdd:cd16295     1 LTFLGAAREVTGSCYLLETGGKRILLDCGLFQGGKELEElnNEPFPFDPKE------IDAVILTHAHLDHSGRLPLLVKE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  83 lGYDGPIYMTHPTKAICPILLEDYRKI---TVERKGETNFFTSAMIKNCMKKVHAVSLHQTIKVDDELEIKAYYAGHVLG 159
Cdd:cd16295    75 -GFRGPIYATPATKDLAELLLLDSAKIqeeEAEHPPAEPLYTEEDVEKALKHFRPVEYGEPFEIGPGVKVTFYDAGHILG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1953806504 160 AAMFYVRVGQE-SVVYTGDYNMTPDRHLGS-AWIDKVrpDVLITES 203
Cdd:cd16295   154 SASVELEIGGGkRILFSGDLGRKNTPLLRDpAPPPEA--DYLIMES 197
Beta-Casp smart01027
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ...
 244-362 4.14e-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: 145.38  E-value: 4.14e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  244 AQELCILIESYWDRMGL-DVPIYFSTGLTERATEFYKLFINWTNQKIKSTFSQ-RNMFDFKHIK---TWN--RNYIDQPG 316
Cdd:smart01027   1 TQELLLILEELWREGELpNVPIYLDSPMAARATEIYKSYPEWMSDEIRKRFEQgRNPFDFKNLKfvkSLEesKRLNDYKG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1953806504  317 PKVLFATPGMLNAGTSLEVFKKWAPDPKNMVIMPGFCVAGTVGSKV 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 3.97e-30

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: 114.15  E-value: 3.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 244 AQELCILIESYWDR-MGLDVPIYFSTGLTERATEFYKLFINWTNQKIKSTF-----SQRNMFDfkhiktwnrnyidqPGP 317
Cdd:pfam10996   1 AQELLYLLDELWREgRLPKIPIYLDSPLAIKATEVYRRYPEYLDDEARHFViskseSKAINEG--------------KGP 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1953806504 318 KVLFATPGMLNAGTSLEVFKKWAPDPKNMVIMPGFCVAGTVG 359
Cdd:pfam10996  67 KVIIASSGMLEGGRSRHHLKHWAPDPKNTVIFTGYQAEGTLG 108
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 7-203 1.37e-27

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: 110.30  E-value: 1.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   7 PLGAGQDVGRSCVLVTIGGKNIMFDCGmhmgYSDARRFPDFSYISKtgnFTDIIDAVIISHFHLDHCGALPFFTEMLGYD 86
Cdd:cd16293     3 PLSGAGDESPLCYLLEIDDVTILLDCG----WDESFDMEYLESLKR---IAPTIDAVLLSHPDLEHLGALPYLVGKLGLT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  87 GPIYMTHPTKAICPI-LLEDYRKITVErkGETNFFTSAMIKNCMKKVHAVSLHQTIKV---DDELEIKAYYAGHVLGAAM 162
Cdd:cd16293    76 CPVYATLPVHKMGRMfMYDLYQSRGLE--EDFNLFTLDDVDEAFDRITQLKYSQPVNLrgkGDGLTITAYNAGHTLGGTI 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1953806504 163 FYVRVGQESVVYTGDYNMTPDRHL-GSAW--IDKVRPDVLITES 203
Cdd:cd16293   154 WKITKDSEDIVYAVDWNHKKERHLnGAVLdsFGGLRPSLLITDA 197
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 9-202 8.54e-19

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: 84.97  E-value: 8.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   9 GAGQdVGRSCVLVTIGGKNIMFDCGMHMGYSDaRRFPDFSYISKTGNFTDI--------------------IDAVIISHF 68
Cdd:cd07732     7 GTNE-IGGNCIEVETGGTRILLDFGLPLDPES-KYFDEVLDFLELGLLPDIvglyrdplllgglrseedpsVDAVLLSHA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  69 HLDHCGALPFftemLGYDGPIYMTHPTKAIcpilLEDYRKITVERKGETNFFtsamikncmkkvHAVSLHQTIKVDDeLE 148
Cdd:cd07732    85 HLDHYGLLNY----LRPDIPVYMGEATKRI----LKALLPFFGEGDPVPRNI------------RVFESGKSFTIGD-FT 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953806504 149 IKAYYAGH-VLGAAMFYVRVGQESVVYTGDYNM-TPDRHLGSAWIDKVR--PDVLITE 202
Cdd:cd07732   144 VTPYLVDHsAPGAYAFLIEAPGKRIFYTGDFRFhGRKPELTEAFVEKAPknIDVLLME 201
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 17-183 2.08e-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: 83.37  E-value: 2.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   17 SCVLVTIGGKNIMFDCGMHMGYSDARRFPDFSYISktgnftdiIDAVIISHFHLDHCGALPFFTEMlgYDGPIYMTHPTK 96
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKK--------IDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   97 AicpiLLEDYRKITVERKGetnfftsamIKNCMKKVHAVSLHQTIKVDDElEIKAYYA-GHVLGAAMFYVRvgQESVVYT 175
Cdd:smart00849  71 E----LLKDLLALLGELGA---------EAEPAPPDRTLKDGDELDLGGG-ELEVIHTpGHTPGSIVLYLP--EGKILFT 134


                   ....*...
gi 1953806504  176 GDYNMTPD 183
Cdd:smart00849 135 GDLLFAGG 142
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 20-200 2.19e-17

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


Pssm-ID: 406948  Cd Length: 192  Bit Score: 80.72  E-value: 2.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  20 LVTIGGKNIMFDCGMH--MGYSDARRFPDfSYISKtgnftdiIDAVIISHFHLDHCGALPF----FTEMLGYDGPIYMTH 93
Cdd:pfam16661   1 LLEFDNVRILLDPGWDgsFSYESDLKYLE-KILPE-------VDLILLSHPTLEHLGAYPLlyykFGSHLGSNIPVYATL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  94 PTKAICPI-LLEDYRKITVERKGETNFFTSAMIKNCMKKVHAVSLHQTIKV---DDELEIKAYYAGHVLGAAMFYVRVGQ 169
Cdd:pfam16661  73 PVANLGRVsTYDLYASRGILGPYDSSELDLDDIDAAFDKIKTLKYSQTVDLkgkFDGLTITPYNSGHTLGGTIWKISKNS 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1953806504 170 ESVVYTGDYNMTPDRHL-GSAWIDK--------VRPDVLI 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 4.65e-17

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: 81.30  E-value: 4.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   6 VPLGaGQD-VGRSCVLVTIGGKNIMFDCGMHMGYSDARR----FPDFSYISKtgnFTDIIDAVIISHFHLDHCGALPFFT 80
Cdd:cd07714     1 IPLG-GLGeIGKNMYVVEYDDDIIIIDCGLKFPDEDMPGvdyiIPDFSYLEE---NKDKIKGIFITHGHEDHIGALPYLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  81 EMLGYdgPIYMTHPTKAICPILLEDYRKItverkGETNFftsamikncmkkvHAVSLHQTIKVDDeLEIKAYYAGH-VLG 159
Cdd:cd07714    77 PELNV--PIYATPLTLALIKKKLEEFKLI-----KKVKL-------------NEIKPGERIKLGD-FEVEFFRVTHsIPD 135

                         170
                  ....*....|....*....
gi 1953806504 160 AAMFYVRVGQESVVYTGDY 178
Cdd:cd07714   136 SVGLAIKTPEGTIVHTGDF 154
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 16-205 6.72e-17

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 81.09  E-value: 6.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  16 RSCVLVTIGGKNIMFDCGmhmgysdarrfPDFSYISKTGNFTDI-IDAVIISHFHLDHCGALPFFTEMLGYDG-PIYMTH 93
Cdd:COG1235    35 RSSILVEADGTRLLIDAG-----------PDLREQLLRLGLDPSkIDAILLTHEHADHIAGLDDLRPRYGPNPiPVYATP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  94 PTKAICpilledyrkitverkgETNFFTSAMIKNCMKKVHAVSLHQTIKVDDeLEIKAYYAGHVLGAAMFY-VRVGQESV 172
Cdd:COG1235   104 GTLEAL----------------ERRFPYLFAPYPGKLEFHEIEPGEPFEIGG-LTVTPFPVPHDAGDPVGYrIEDGGKKL 166

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1953806504 173 VYTGDYNMTPDRHLgsAWIDKVrpDVLITESTY 205
Cdd:COG1235   167 AYATDTGYIPEEVL--ELLRGA--DLLILDATY 195
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
17-206 1.43e-16

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 79.85  E-value: 1.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  17 SCVLVTIGGKNIMFDCG-------MHMGYSDARrfpdfsyisktgnftdiIDAVIISHFHLDHCGALPFFTEMLGYDG-- 87
Cdd:COG1234    20 SSYLLEAGGERLLIDCGegtqrqlLRAGLDPRD-----------------IDAIFITHLHGDHIAGLPGLLSTRSLAGre 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  88 ---PIYMTHPTKAIcpilLEDYRKITVERkgeTNFFTsamikncmkKVHAVSLHQTIKVDDeLEIKAYYAGHVLGAAMFY 164
Cdd:COG1234    83 kplTIYGPPGTKEF----LEALLKASGTD---LDFPL---------EFHEIEPGEVFEIGG-FTVTAFPLDHPVPAYGYR 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1953806504 165 VRVGQESVVYTGDYNMTPdrhlgsAWIDKVR-PDVLITESTYA 206
Cdd:COG1234   146 FEEPGRSLVYSGDTRPCE------ALVELAKgADLLIHEATFL 182
RMMBL pfam07521
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ...
 378-437 1.50e-14

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: 68.42  E-value: 1.50e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953806504 378 EVNLQVRNLS-FSAHADAKGIMQLIRQCEPRNVVLVHGERGKMNFLSSKIMKEFAIPCYMP 437
Cdd:pfam07521   3 PVRARIETIDgFSGHADRRELLELIKGLKPKPIVLVHGEPRALLALAELLKEELGIEVFVP 63
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 5-203 1.79e-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: 71.91  E-value: 1.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   5 VVPLGAG-----QDVGRSCVLVTIGGKNIMFDCGmhmgYSDARRfpdfsyISKTGNFTDIIDAVIISHFHLDHCGALPFF 79
Cdd:cd16272     1 LTFLGTGgavpsLTRNTSSYLLETGGTRILLDCG----EGTVYR------LLKAGVDPDKLDAIFLSHFHLDHIGGLPTL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  80 TEMLGYDG-----PIYMTHPTKAicpiLLEDYRKITVERKGETNFFtsamikncmkKVHAVSLHQTIKVDDELEIKAYYA 154
Cdd:cd16272    71 LFARRYGGrkkplTIYGPKGIKE----FLEKLLNFPVEILPLGFPL----------EIEELEEGGEVLELGDLKVEAFPV 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1953806504 155 GHVLGAAMFYVRVGQESVVYTGDynMTPDRHLgSAWIDKVrpDVLITES 203
Cdd:cd16272   137 KHSVESLGYRIEAEGKSIVYSGD--TGPCENL-VELAKGA--DLLIHEC 180
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
17-177 5.15e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 71.25  E-value: 5.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  17 SCVLVTIGGKNIMFDCGMHMGYSDARRFPDFSYISKTgnftdiIDAVIISHFHLDHCGALPFFTEmlgydgpiymTHPTK 96
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLGPKD------IDAVILTHGHFDHIGGLGELAE----------ATDVP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  97 AICPIllEDYRKITVERKGETNFFTSAMIKNCMKKVHAVSLHQTIKVDDELEIKAYYAGHVLGAAMFYVRVGQESVVYTG 176
Cdd:pfam00753  71 VIVVA--EEARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTG 148


                  .
gi 1953806504 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 ...
 17-216 2.57e-11

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: 64.01  E-value: 2.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  17 SCVLVTIGGKNIMFDCG-------MHMGYSdarrfpdfsyISKtgnftdiIDAVIISHFHLDHCGALPFF---TEMLGYD 86
Cdd:cd07717    18 SSIALRLEGELWLFDCGegtqrqlLRAGLS----------PSK-------IDRIFITHLHGDHILGLPGLlstMSLLGRT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  87 GP--IYMTHPTKAIcpilLEDYRKITVERKGETnfftsamIkncmkKVHAVSLHQTIKVDDE-LEIKAYYAGHVLGAAMF 163
Cdd:cd07717    81 EPltIYGPKGLKEF----LETLLRLSASRLPYP-------I-----EVHELEPDPGLVFEDDgFTVTAFPLDHRVPCFGY 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953806504 164 YVRVGQeSVVYTGDyNMTPDRHlgsawIDKVR-PDVLITESTYATTIRDSKRSR 216
Cdd:cd07717   145 RFEEGR-KIAYLGD-TRPCEGL-----VELAKgADLLIHEATFLDDDAEKAKET 191
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 19-177 5.77e-11

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: 61.92  E-value: 5.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  19 VLVTIGGKNIMFDCGMhmgysdarrfPDFSYISKTGNFTDI-IDAVIISHFHLDHCGALPFFTEMlgYDGPIYMTHPTKA 97
Cdd:cd06262    14 LVSDEEGEAILIDPGA----------GALEKILEAIEELGLkIKAILLTHGHFDHIGGLAELKEA--PGAPVYIHEADAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  98 icpiLLEDyrkitverKGETNFFTSAMIKNCMKKVHAVSLHQTIKVDDeLEIKAYYA-GHVLGAAMFYvrVGQESVVYTG 176
Cdd:cd06262    82 ----LLED--------PELNLAFFGGGPLPPPEPDILLEDGDTIELGG-LELEVIHTpGHTPGSVCFY--IEEEGVLFTG 146


                  .
gi 1953806504 177 D 177
Cdd:cd06262   147 D 147
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
5-182 2.60e-10

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 63.16  E-value: 2.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   5 VVPLGaGQD-VGRSCVLVTIGGKNIMFDCGMhmGYSDARRF------PDFSYISKTGnftDIIDAVIISHFHLDHCGALP 77
Cdd:COG0595     8 IIPLG-GLGeIGKNMYVYEYDDDIIIVDCGL--KFPEDEMPgvdlviPDISYLEENK---DKIKGIVLTHGHEDHIGALP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  78 FFTEMLgyDGPIYMTHptkaicpilledyrkitverkgetnfFTSAMIKNCMK--------KVHAVSLHQTIKVDDeLEI 149
Cdd:COG0595    82 YLLKEL--NVPVYGTP--------------------------LTLALLEAKLKehgllkkvKLHVVKPGDRIKFGP-FKV 132

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1953806504 150 KAYYAGH-VLGAAMFYVRVGQESVVYTGDYNM--TP 182
Cdd:COG0595   133 EFFRVTHsIPDSLGLAIRTPAGTIVHTGDFKFdqTP 168
PRK00055 PRK00055
ribonuclease Z; Reviewed
 3-218 5.47e-10

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 60.58  E-value: 5.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   3 IEVVPLGAGQ---DVGR--SCVLVTIGGKNIMFDCG-------MHMGYSdarrfpdfsyisktgnFTDIiDAVIISHFHL 70
Cdd:PRK00055    2 MELTFLGTGSgvpTPTRnvSSILLRLGGELFLFDCGegtqrqlLKTGIK----------------PRKI-DKIFITHLHG 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  71 DHCGALPFFTEMLGYDGpiyMTHPTKAICPILLEDY----RKIT------VERKGETNFFTSAMIKNcmKKVHAVSLHQT 140
Cdd:PRK00055   65 DHIFGLPGLLSTRSLSG---RTEPLTIYGPKGIKEFvetlLRASgslgyrIAEKDKPGKLDAEKLKA--LGVPPGPLFGK 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 141 IKVDDELEikaYYAGHVLGAAMFY--VRVGQeSVVYTGDYNMTPDRHlgsAWIDKVrpDVLITESTYATTirDSKRSRER 218
Cdd:PRK00055  140 LKRGEDVT---LEDGRIINPADVLgpPRKGR-KVAYCGDTRPCEALV---ELAKGA--DLLVHEATFGDE--DEELAKEY 208
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 17-203 6.19e-10

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: 58.61  E-value: 6.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  17 SCVLVTIGGKNIMFDCGmhmgySDArrfpdfsyISKTGNFTDI--IDAVIISHFHLDHC---GALPFFTEMLGYDGPiym 91
Cdd:cd07716    19 SGYLLEADGFRILLDCG-----SGV--------LSRLQRYIDPedLDAVVLSHLHPDHCadlGVLQYARRYHPRGAR--- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  92 THPTKAICPilledyrKITVERKGETNFFTSAMikncmkKVHAVSLHQTIKVDDeLEIKAYYAGHVLGAAMFYVRVGQES 171
Cdd:cd07716    83 KPPLPLYGP-------AGPAERLAALYGLEDVF------DFHPIEPGEPLEIGP-FTITFFRTVHPVPCYAMRIEDGGKV 148

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1953806504 172 VVYTGDYNMTPdrhlgsAWIDKVR-PDVLITES 203
Cdd:cd07716   149 LVYTGDTGYCD------ELVEFARgADLLLCEA 175
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 18-177 1.25e-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: 58.55  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  18 CVLVTIGGKNIMFDCGMhmGYSDARRFPDfsYISKTGnftDIIDAVIISHFHLDHCGALPFFTEmlGYDGPIYMTHPTKa 97
Cdd:COG0491    17 SYLIVGGDGAVLIDTGL--GPADAEALLA--ALAALG---LDIKAVLLTHLHPDHVGGLAALAE--AFGAPVYAHAAEA- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  98 icPILLEDYRKITVERKGetnfftsamikncMKKVHAVSLHQTIKVDDeLEIKAYYA-GHVLGAAMFYVRvgQESVVYTG 176
Cdd:COG0491    87 --EALEAPAAGALFGREP-------------VPPDRTLEDGDTLELGG-PGLEVIHTpGHTPGHVSFYVP--DEKVLFTG 148


                  .
gi 1953806504 177 D 177
Cdd:COG0491   149 D 149
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 17-80 1.81e-09

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: 58.38  E-value: 1.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  17 SCVLVTIGGKNIMFDCGMHmgySDARRFPDFSYISKTGNFTDI----------------IDAVIISHFHLDHCGALPFFT 80
Cdd:cd07729    33 YAYLIEHPEGTILVDTGFH---PDAADDPGGLELAFPPGVTEEqtleeqlarlgldpedIDYVILSHLHFDHAGGLDLFP 109
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 4-177 2.76e-09

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: 57.14  E-value: 2.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   4 EVVPLGAG---QDVGR--SCVLVTIGGKNIMFDCGmhmgYSDARRFpdfsyiSKTG-NFTDIiDAVIISHFHLDHCGALP 77
Cdd:cd07719     1 RVTLLGTGgpiPDPDRagPSTLVVVGGRVYLVDAG----SGVVRRL------AQAGlPLGDL-DAVFLTHLHSDHVADLP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  78 -FFteMLGYDG------PIYMTHPTKAICPILLEDYRKITVER---KGETNFFTSAMIkncmkKVHAVSLHQTIKVDDEL 147
Cdd:cd07719    70 aLL--LTAWLAgrktplPVYGPPGTRALVDGLLAAYALDIDYRariGDEGRPDPGALV-----EVHEIAAGGVVYEDDGV 142

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1953806504 148 EIKAYYAGH--VLGAAMFYVRVGQESVVYTGD 177
Cdd:cd07719   143 KVTAFLVDHgpVPPALAYRFDTPGRSVVFSGD 174
Int9-like_MBL-fold cd16294
integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ...
 11-174 3.84e-09

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: 55.96  E-value: 3.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  11 GQDVGRSCVLVTIGGKNIMFDCGMHMGYSDarRFPDFSyisktgnftdIIDAVIISHFHldHCGALPFFTEMLGYDGPIY 90
Cdd:cd16294     7 SGHPTLPCNVLKFKSTTIMLDCGLDCPPET--ELIDLS----------TVDVILISNYH--CMLALPFITEYTGFTGVVY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  91 MTHPTKAICPILLEDyrkitverkgetnfftsamIKNCMKKVHAVSLHQTIKVDDELEIKAYYAGHVLGAAMFYVRVGQE 170
Cdd:cd16294    73 ATEPTVQIGRLLMEE-------------------LVQALSKIQLVGYSQKLDLFGAVQVTALSSGYCLGSSNWVIQSHYE 133


                  ....
gi 1953806504 171 SVVY 174
Cdd:cd16294   134 KISY 137
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 13-77 2.56e-08

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: 55.25  E-value: 2.56e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953806504  13 DVGR--SCVLVTIGGKNIMFDCGMHMGYSDARRFPDfSYISKTGnfTDIIDAVIISHFHLDHCGALP 77
Cdd:COG2333     7 DVGQgdAILIRTPDGKTILIDTGPRPSFDAGERVVL-PYLRALG--IRRLDLLVLTHPDADHIGGLA 70
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 8-203 2.86e-08

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: 54.19  E-value: 2.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   8 LGAGQDVG-----RSCVLVTIGGKNIMFDCGMHmgysdarrfpdfSYIS--KTGNFTDIIDAVIISHFHLDHCGALPFFT 80
Cdd:cd07740     3 LGSGDAFGsggrlNTCFHVASEAGRFLIDCGAS------------SLIAlkRAGIDPNAIDAIFITHLHGDHFGGLPFFL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  81 E----MLGYDGPIYMTHPtkaicPILLEDYRKITverkgETNFFTSAmikncmkKVHAVSLHQTIKVD-------DELEI 149
Cdd:cd07740    71 LdaqfVAKRTRPLTIAGP-----PGLRERLRRAM-----EALFPGSS-------KVPRRFDLEVIELEpgepttlGGVTV 133

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953806504 150 KAYYAGHVLGAAMFYVRVGQE--SVVYTGDynmtpdrhlgSAWIDKVRP-----DVLITES 203
Cdd:cd07740   134 TAFPVVHPSGALPLALRLEAAgrVLAYSGD----------TEWTDALVPlargaDLFICEC 184
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 4-194 4.40e-08

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: 54.52  E-value: 4.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504   4 EVVPLGA--GQDVGR-SCVLVTIGGKN--IMFDCGMHMGYSDARRFPDFSYISKTGNFTDI---IDAVIISHFHLDHCGA 75
Cdd:cd07735     2 ELVVLGCsgGPDEGNtSSFLLDPAGSDgdILLDAGTGVGALSLEEMFNDILFPSQKAAYELyqrIRHYLITHAHLDHIAG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  76 LPFFTEMLGYDGpiymtHPTKAICPIlledyrKITVERKGET--------NFFTSAMIKNCMKKVHAVSLHQTIKVDDeL 147
Cdd:cd07735    82 LPLLSPNDGGQR-----GSPKTIYGL------PETIDALKKHifnwviwpDFTSIPSGKYPYLRLEPIEPEYPIALTG-L 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1953806504 148 EIKAYYAGH-VLGAAMFYVRVGQESVVYTGDynMTPDRHLGSAWIDKV 194
Cdd:cd07735   150 SVTAFPVSHgVPVSTAFLIRDGGDSFLFFGD--TGPDSVSKSPRLDAL 195
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 17-205 5.36e-08

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: 53.65  E-value: 5.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  17 SCVLVTIGGKNIMFDCGmhmgySDARRFPDfsYISKTGNFTDIidAVIISHFHLDH-CGaLPFFTemlgydgPIYMthPT 95
Cdd:cd07715    24 SCVEVRAGGELLILDAG-----TGIRELGN--ELMKEGPPGEA--HLLLSHTHWDHiQG-FPFFA-------PAYD--PG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  96 KAI---CPILLEDYRKITVERKGETNFF---TSAMikNCMKKVHAVSLHQTIKVDDeLEIKAYYAGHVLGAAMFYVRVGQ 169
Cdd:cd07715    85 NRIhiyGPHKDGGSLEEVLRRQMSPPYFpvpLEEL--LAAIEFHDLEPGEPFSIGG-VTVTTIPLNHPGGALGYRIEEDG 161

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1953806504 170 ESVVYTGDYNMTP-DRHLGSAWIDKVR-PDVLITESTY 205
Cdd:cd07715   162 KSVVYATDTEHYPdDGESDEALLEFARgADLLIHDAQY 199
SNM1A-1C-like_MBL-fold cd16273
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ...
 35-205 5.46e-08

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: 52.54  E-value: 5.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  35 HMGYSDARRFPDFSYISKTgNFT---------DIIDAVIISHFHLDHCGAL-PFFTEmlgydGPIYMTHPTKaicpILLE 104
Cdd:cd16273     4 KKKPKRKKPCPFYKIIPGT-SFVvdafkygkiPGISAYFLSHFHSDHYGGLtKSWSH-----GPIYCSEITA----NLVK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 105 DyrKITVERKgetnfftsamikncmkKVHAVSLHQTIKVDDELEIKAYYAGHVLGAAMFYVRVGQ-ESVVYTGDYNMTPD 183
Cdd:cd16273    74 L--KLKVDEE----------------YIVVLPMNTPVEIDGDVSVTLLDANHCPGAVMFLFELPDgRRILHTGDFRANPE 135

                         170       180
                  ....*....|....*....|..
gi 1953806504 184 RHLGSAWIDKVRPDVLITESTY 205
Cdd:cd16273   136 MLEHPLLLGKRRIDTVYLDTTY 157
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 16-95 1.26e-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: 52.09  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  16 RSCVLVTIGGKNIMFDCGmhmgysdarrfPDFSY------ISKtgnftdiIDAVIISHFHLDHCGALP---FFTEMLGYD 86
Cdd:cd16279    35 RSSILIETGGKNILIDTG-----------PDFRQqalragIRK-------LDAVLLTHAHADHIHGLDdlrPFNRLQQRP 96


                  ....*....
gi 1953806504  87 GPIYMTHPT 95
Cdd:cd16279    97 IPVYASEET 105
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 14-200 1.67e-07

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 52.61  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  14 VGRSCVLVTIGGKNIMFDcgmhMGYSDARRFPDFSYISktgnFTDI--IDAVIISHFHLDHCGaLPFFTEMLGYDGPIYM 91
Cdd:COG2220     9 LGHATFLIETGGKRILID----PVFSGRASPVNPLPLD----PEDLpkIDAVLVTHDHYDHLD-DATLRALKRTGATVVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  92 THPTKAIcpilledyrkitVERKGETNfftsamikncmkkVHAVSLHQTIKVDDeLEIKAYYAGH--------VLGAAMF 163
Cdd:COG2220    80 PLGVAAW------------LRAWGFPR-------------VTELDWGESVELGG-LTVTAVPARHssgrpdrnGGLWVGF 133

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1953806504 164 YVRVGQESVVYTGDYNMTPD-RHLGsawiDKVRPDVLI 200
Cdd:COG2220   134 VIETDGKTIYHAGDTGYFPEmKEIG----ERFPIDVAL 167
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 18-94 4.57e-07

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: 51.85  E-value: 4.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  18 CVLVTIGGKNIMFDCGmhmgYSD-----ARRFpdfsyisktgnftDI----IDAVIISHFHLDHCGALPFFTEMLGyDGP 88
Cdd:cd07713    22 SLLIETEGKKILFDTG----QSGvllhnAKKL-------------GIdlsdIDAVVLSHGHYDHTGGLKALLELNP-KAP 83


                  ....*.
gi 1953806504  89 IYMtHP 94
Cdd:cd07713    84 VYA-HP 88
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
18-94 2.44e-06

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 49.50  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  18 CVLVTIGGKNIMFDCGmhmgYSD-----ARRFpdfsyisktgnftDI----IDAVIISHFHLDHCGALPFFTEMLGyDGP 88
Cdd:COG1237    24 SALIETEGKRILFDTG----QSDvllknAEKL-------------GIdlsdIDAVVLSHGHYDHTGGLPALLELNP-KAP 85


                  ....*.
gi 1953806504  89 IYMtHP 94
Cdd:COG1237    86 VYA-HP 90
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 25-80 3.29e-06

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: 48.80  E-value: 3.29e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953806504  25 GKNIMFDCGMHMGYSDA-RRFPDfsYISKTGNFTDI-----------------IDAVIISHFHLDHCGALPFFT 80
Cdd:cd07730    33 GGKILFDLGYRKDFEEYtPRVPE--RLYRTPVPLEVeedvaeqlaaggidpedIDAVILSHLHWDHIGGLSDFP 104
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 13-77 5.96e-06

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 47.13  E-value: 5.96e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953806504  13 DVGRS-CVLVTIGGKNIMFDCGMHMGYSDARRFPdfsYISKTGNFTdiIDAVIISHFHLDHCGALP 77
Cdd:cd07731     6 DVGQGdAILIQTPGKTILIDTGPRDSFGEDVVVP---YLKARGIKK--LDYLILTHPDADHIGGLD 66
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 17-93 9.84e-06

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: 46.81  E-value: 9.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  17 SCVLVTIGGKNIMFDCGMhmgysdarrFPDFSYI----SKTGNFTDIIDAVIISHFHLDHCGALPFFTEMLGYDGPIYMT 92
Cdd:cd07711    23 TVTLIKDGGKNILVDTGT---------PWDRDLLlkalAEHGLSPEDIDYVVLTHGHPDHIGNLNLFPNATVIVGWDICG 93


                  .
gi 1953806504  93 H 93
Cdd:cd07711    94 D 94
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 60-207 4.11e-05

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 44.99  E-value: 4.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  60 IDAVIISHFHLDHCGALPFFTEmlGYDGPIYMTHPTKAicpILledyrkitverkgETNFFTSAMIKNCMKKVHAVSLHQ 139
Cdd:pfam12706  29 IDAVLLTHDHYDHLAGLLDLRE--GRPRPLYAPLGVLA---HL-------------RRNFPYLFLLEHYGVRVHEIDWGE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 140 TIKVDDE-LEIKA------------YYAGHVLGaamFYVRVGQESVVYTGDYNMTPDrHLGsAWIDKVrpDVLITESTYA 206
Cdd:pfam12706  91 SFTVGDGgLTVTAtparhgsprgldPNPGDTLG---FRIEGPGKRVYYAGDTGYFPD-EIG-ERLGGA--DLLLLDGGAW 163


                  .
gi 1953806504 207 T 207
Cdd:pfam12706 164 R 164
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-74 1.31e-04

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


Pssm-ID: 293839  Cd Length: 252  Bit Score: 44.02  E-value: 1.31e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953806504  18 CVLVTIGGKNIMFDCGMHMGYSDarRFPDFSY----------ISKTGNFTDIIDAVIISHFHLDHCG 74
Cdd:cd16281    45 CLLIETGGRNILIDTGIGDKQDP--KFRSIYVqhsehsllksLARLGLSPEDITDVILTHLHFDHCG 109
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 20-84 3.30e-04

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


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 41.90  E-value: 3.30e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953806504  20 LVTIGGKNIMFDCGMHMgYSDARRFpdFSYISKTGNFTDIIDAVIISHFHLDHCGALPFFTEMLG 84
Cdd:cd07725    19 LLRDGDETTLIDTGLAT-EEDAEAL--WEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSG 80
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 17-76 3.38e-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: 42.92  E-value: 3.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953806504  17 SCVLVTIGGKNIMFDCGM--HMGYSdarrfpdfsyiskTGNFTDI----------IDAVIISHFHLDHCGAL 76
Cdd:cd07720    50 NAFLVRTGGRLILVDTGAggLFGPT-------------AGKLLANlaaagidpedIDDVLLTHLHPDHIGGL 108
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 17-156 4.32e-04

ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN. [Transcription, RNA processing]


Pssm-ID: 274246 [Multi-domain]  Cd Length: 299  Bit Score: 42.59  E-value: 4.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  17 SCVLVTIGGKNIMFDCG----MHMGYSDARrfpdfsyisktgnFTDIiDAVIISHFHLDHCGALPFFTEMLGYDGpiyMT 92
Cdd:TIGR02651  19 PSIALKLNGELWLFDCGegtqRQMLRSGIS-------------PMKI-DRIFITHLHGDHILGLPGLLSTMSFQG---RK 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953806504  93 HPTKAICPILLEDYRKiTVERKGETNFftsamikNCMKKVHAVSLHQTIKVDDELEIKAYYAGH 156
Cdd:TIGR02651  82 EPLTIYGPPGIKEFIE-TSLRVSYTYL-------NYPIKIHEIEEGGLVFEDDGFKVEAFPLDH 137
PRK02113 PRK02113
MBL fold metallo-hydrolase;
16-76 6.75e-04

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 41.69  E-value: 6.75e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953806504  16 RSCVLVTIGGKNIMFDCGmhmgysdarrfPDFSYISKTGNFtDIIDAVIISHFHLDHCGAL 76
Cdd:PRK02113   35 RTSALVETEGARILIDCG-----------PDFREQMLRLPF-GKIDAVLITHEHYDHVGGL 83
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 14-72 4.04e-03

Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. 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: 293841  Cd Length: 181  Bit Score: 38.80  E-value: 4.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953806504  14 VGRSCVLVTIGGKNIMFDCGMHMGYSdARRFPDFSYISKTGNFTDI---IDAVIISHFHLDH 72
Cdd:cd16283     2 IGHATFLIQIEGLNILTDPVFSERAS-PVSFGGPKRLTPPGLPLEElppIDAVLISHNHYDH 62
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 60-200 4.24e-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.


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 39.09  E-value: 4.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  60 IDAVIISHFHLDHCGALPFFTEMlgyDGPIYMTHPT----KAICPILLEDYRKITVERKGETNF------FTSAMikncm 129
Cdd:cd16282    53 VRYVVNTHYHGDHTLGNAAFADA---GAPIIAHENTreelAARGEAYLELMRRLGGDAMAGTELvlpdrtFDDGL----- 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504 130 kkvhavslhqTIKVDD-ELEIKAYYAGHVLGAAMFYVRvgQESVVYTGD--YNMTPDRHLGS---AWI---DKVR---PD 197
Cdd:cd16282   125 ----------TLDLGGrTVELIHLGPAHTPGDLVVWLP--EEGVLFAGDlvFNGRIPFLPDGslaGWIaalDRLLaldAT 192


                  ...
gi 1953806504 198 VLI 200
Cdd:cd16282   193 VVV 195
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 18-76 6.51e-03

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: 37.99  E-value: 6.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953806504  18 CVLVTIGGKNIMFDCG-MHMgysdARRFPDFSyisktgnftdiIDAVIISHFHLDHCGAL 76
Cdd:cd07736    39 SALIEVDGERILLDAGlTDL----AERFPPGS-----------IDAILLTHFHMDHVQGL 83
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 18-94 7.00e-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: 38.36  E-value: 7.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953806504  18 CVLVTIGGKNIMFDCGMHMGYSDARRfpdfsYISKTGNFTDIIDAVIISHFHLDHCGALPFFTEMlgYDGPIYMtHP 94
Cdd:cd07721    13 AYLIEDDDGLTLIDTGLPGSAKRILK-----ALRELGLSPKDIRRILLTHGHIDHIGSLAALKEA--PGAPVYA-HE 81
 
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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