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Conserved domains on  [gi|1386806178|ref|NP_001349911|]
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zinc phosphodiesterase ELAC protein 2 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 52-307 3.79e-114

Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. This eukaryotic subgroup includes the N-terminus of human ELAC2 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: 293854 [Multi-domain]  Cd Length: 175  Bit Score: 344.25  E-value: 3.79e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178  52 LQVVAAGGRDAGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPKCVLS 131
Cdd:cd16296     1 LQVVAAGSRDMGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 132 GPpqlekyleaikifsgplkgielavrphsapeykdetmtvyqvpihserrcgkqqpsqsprtspnrlspkqssdsgsae 211
Cdd:cd16296    81 GP------------------------------------------------------------------------------ 82

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 212 ngqCPPEDSSAGANRKAWGRDPSLVVAFVCKLHLRKGNFLVLKAKELGLPVGTAAIAPIIAAVKDGKSITYEGREIAAEE 291
Cdd:cd16296    83 ---NKQSPDKIGVRRQILERDPSLVVAFICKLHLKKGNFLVLKAKELGLPVGTAAIAPIIAAVKDGKSITFEGREILAEE 159

                         250
                  ....*....|....*.
gi 1386806178 292 LCTPPDPGLVFIVVEC 307
Cdd:cd16296   160 LCTPPDPGIVFIVVEC 175
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 479-689 4.69e-102

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


:

Pssm-ID: 293804 [Multi-domain]  Cd Length: 204  Bit Score: 314.10  E-value: 4.69e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 479 IVFLGTGSAIPMKIRNVSSTLVNLSPDKSVLLDCGEGTFGQLCRHYGQQ-IDRVLCSLTAVFVSHLHADHHTGLLNILLQ 557
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 558 REHALRsffqaslgKPFQPLLVVAPTQLRAWLQQYHNHCQEILHHVSMIPAKCLQKGAEVSNTTLERLISLLLETCDLEE 637
Cdd:cd07718    81 RKKLFK--------PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKS 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1386806178 638 FQTCLVRHCKHAFGCALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEAT 689
Cdd:cd07718   153 IETVPVIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
 
Name Accession Description Interval E-value
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 52-307 3.79e-114

Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. This eukaryotic subgroup includes the N-terminus of human ELAC2 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: 293854 [Multi-domain]  Cd Length: 175  Bit Score: 344.25  E-value: 3.79e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178  52 LQVVAAGGRDAGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPKCVLS 131
Cdd:cd16296     1 LQVVAAGSRDMGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 132 GPpqlekyleaikifsgplkgielavrphsapeykdetmtvyqvpihserrcgkqqpsqsprtspnrlspkqssdsgsae 211
Cdd:cd16296    81 GP------------------------------------------------------------------------------ 82

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 212 ngqCPPEDSSAGANRKAWGRDPSLVVAFVCKLHLRKGNFLVLKAKELGLPVGTAAIAPIIAAVKDGKSITYEGREIAAEE 291
Cdd:cd16296    83 ---NKQSPDKIGVRRQILERDPSLVVAFICKLHLKKGNFLVLKAKELGLPVGTAAIAPIIAAVKDGKSITFEGREILAEE 159

                         250
                  ....*....|....*.
gi 1386806178 292 LCTPPDPGLVFIVVEC 307
Cdd:cd16296   160 LCTPPDPGIVFIVVEC 175
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 479-689 4.69e-102

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


Pssm-ID: 293804 [Multi-domain]  Cd Length: 204  Bit Score: 314.10  E-value: 4.69e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 479 IVFLGTGSAIPMKIRNVSSTLVNLSPDKSVLLDCGEGTFGQLCRHYGQQ-IDRVLCSLTAVFVSHLHADHHTGLLNILLQ 557
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 558 REHALRsffqaslgKPFQPLLVVAPTQLRAWLQQYHNHCQEILHHVSMIPAKCLQKGAEVSNTTLERLISLLLETCDLEE 637
Cdd:cd07718    81 RKKLFK--------PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKS 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1386806178 638 FQTCLVRHCKHAFGCALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEAT 689
Cdd:cd07718   153 IETVPVIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
478-753 7.30e-49

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 173.07  E-value: 7.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 478 EIVFLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHygqQIDrvLCSLTAVFVSHLHADHHTGLLNILLQ 557
Cdd:COG1234     2 KLTFLGTGGAVPTPGRATSSYLLE-AGGERLLIDCGEGTQRQLLRA---GLD--PRDIDAIFITHLHGDHIAGLPGLLST 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 558 REHALRSffqaslgkpfQPLLVVAPTQLRAWLQQYHNHCQEILH-HVSMIPakcLQKGaevsnttlerlislllETCDLE 636
Cdd:COG1234    76 RSLAGRE----------KPLTIYGPPGTKEFLEALLKASGTDLDfPLEFHE---IEPG----------------EVFEIG 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 637 EFQ--TCLVRHCKHAFGcALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGM 714
Cdd:COG1234   127 GFTvtAFPLDHPVPAYG-YRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAA 205

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1386806178 715 RMNAEFIMLNHFSQRYAKIPLF----SPDFNEKVGIAFDHMKV 753
Cdd:COG1234   206 EAGVKRLVLTHFSPRYDDPEELlaeaRAVFPGPVELAEDGMVI 248
PRK00055 PRK00055
ribonuclease Z; Reviewed
 478-730 3.40e-40

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 149.18  E-value: 3.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 478 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRvlcsltaVFVSHLHADHHTGLLNI 554
Cdd:PRK00055    3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQL-LKTGikpRKIDK-------IFITHLHGDHIFGLPGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 555 LLQ-----REHALRSFFQASLGKPFQPLLVVAPTqlRAWLqqyhnhcqeILHH------------VSMIPAKC----LQK 613
Cdd:PRK00055   74 LSTrslsgRTEPLTIYGPKGIKEFVETLLRASGS--LGYR---------IAEKdkpgkldaeklkALGVPPGPlfgkLKR 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 614 GAEVsntTLE--RLISLlletcdleefqTCLVRhckhafgcalVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLE 691
Cdd:PRK00055  143 GEDV---TLEdgRIINP-----------ADVLG----------PPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFG 198

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1386806178 692 DGLEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHFSQRY 730
Cdd:PRK00055  199 DEDEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRY 237
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 478-730 2.83e-34

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: 133.11  E-value: 2.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 478 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRVlcsltavFVSHLHADHHTGLLNI 554
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-NGELWLFDCGEGTQRQM-LRSGispMKIDRI-------FITHLHGDHILGLPGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 555 L-----LQREHAL--------RSFFQASLG-----KPFQPLLV-VAPTQLRAWLQQYHNHCQEILHHV-SM--------- 605
Cdd:TIGR02651  72 LstmsfQGRKEPLtiygppgiKEFIETSLRvsytyLNYPIKIHeIEEGGLVFEDDGFKVEAFPLDHSIpSLgyrfeekdr 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 606 -------------IPA----KCLQKGAEVsnTTLERlislllETCDLEEFqTCLVRHckhafgcalvhssGWKVVYSGDT 668
Cdd:TIGR02651 152 pgkfdrekakelgIPPgplyGKLKRGETV--TLIDG------RIIDPEDV-LGPPRK-------------GRKIAYTGDT 209

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386806178 669 MPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHFSQRY 730
Cdd:TIGR02651 210 RPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY 271
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 66-112 9.84e-15

tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related structurally to the Lactamase_B family members. tRNase Z is the endonuclease that is involved in tRNA 3'-end maturation through removal of the 3'-trailer sequences from tRNA precursors. The fission yeast Schizosaccharomyces pombe contains two candidate tRNase Zs encoded by two essential genes. The first, Swiss:Q10155, is targeted to the nucleus and has an SV40 nuclear localization signal at its N-terminus, consisting of four consecutive arginine and lysine residues between residues 208 and 211 (KKRK) that is critical for the NLS function. The second, Swiss:P87168, is targeted to the mitochondria, with an N-terminal mitochondrial targeting signal within the first 38 residues.


Pssm-ID: 404562 [Multi-domain]  Cd Length: 63  Bit Score: 69.15  E-value: 9.84e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1386806178  66 LYVFSEYNRYLF-NCGEGVQRLMQEHKLKVARLDNIFLTRMH-WSNVGG 112
Cdd:pfam13691  15 LLLHFDSKRYLFgNVGEGTQRALNEQKVRLSKLEDIFLTGKVsWSNIGG 63
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
74-172 6.37e-13

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 69.45  E-value: 6.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178  74 RYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPK-CVLSGPPQLEKYLEAIKIFSGPLKG 152
Cdd:COG1234    30 RLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGREKpLTIYGPPGTKEFLEALLKASGTDLD 109

                          90       100
                  ....*....|....*....|.
gi 1386806178 153 IELAVRPHSAPE-YKDETMTV 172
Cdd:COG1234   110 FPLEFHEIEPGEvFEIGGFTV 130
PRK00055 PRK00055
ribonuclease Z; Reviewed
 75-150 2.76e-07

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 52.88  E-value: 2.76e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1386806178  75 YLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPKCV-LSGPPQLEKYLEAIKIFSGPL 150
Cdd:PRK00055   32 FLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSGRTEPLtIYGPKGIKEFVETLLRASGSL 108
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 496-692 2.85e-05

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: 45.62  E-value: 2.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178  496 SSTLVNlSPDKSVLLDCGEGTFGQLCRHYGQQIDRvlcSLTAVFVSHLHADhHTGLLNILLQREHAlrsffqaslgkpfq 575
Cdd:smart00849   1 NSYLVR-DDGGAILIDTGPGEAEDLLAELKKLGPK---KIDAIILTHGHPD-HIGGLPELLEAPGA-------------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178  576 plLVVAPTQLRAWLQQYHNHCQEILHHV-SMIPAKCLQKGAEVsnttlerlisllletcDLEEFQTCLVRHCKHAFGCAL 654
Cdd:smart00849  62 --PVYAPEGTAELLKDLLALLGELGAEAePAPPDRTLKDGDEL----------------DLGGGELEVIHTPGHTPGSIV 123

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1386806178  655 VHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLED 692
Cdd:smart00849 124 LYLPEGKILFTGDLLFAGGDGRTLVDGGDAAASDALES 161
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 508-726 3.04e-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: 45.76  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 508 VLLDCGEGTFGQLCR--HYGQQIDRvlcSLTAVFVSHLHADHHTGLLNIllqREHALRSFFqASLG--------KPFQPL 577
Cdd:pfam12706   3 ILIDPGPDLRQQALPalQPGRLRDD---PIDAVLLTHDHYDHLAGLLDL---REGRPRPLY-APLGvlahlrrnFPYLFL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 578 LVVAPTQLR--AWLQQYHNHCQEIlhHVSMIPAKclQKGAEVSNTTLERLISLLLETcdleefqtclvrhckhafgcalv 655
Cdd:pfam12706  76 LEHYGVRVHeiDWGESFTVGDGGL--TVTATPAR--HGSPRGLDPNPGDTLGFRIEG----------------------- 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386806178 656 hsSGWKVVYSGDTMPCEALV-QMGKDATLLIHEATLEDglEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHF 726
Cdd:pfam12706 129 --PGKRVYYAGDTGYFPDEIgERLGGADLLLLDGGAWR--DDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
 
Name Accession Description Interval E-value
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 52-307 3.79e-114

Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. This eukaryotic subgroup includes the N-terminus of human ELAC2 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: 293854 [Multi-domain]  Cd Length: 175  Bit Score: 344.25  E-value: 3.79e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178  52 LQVVAAGGRDAGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPKCVLS 131
Cdd:cd16296     1 LQVVAAGSRDMGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 132 GPpqlekyleaikifsgplkgielavrphsapeykdetmtvyqvpihserrcgkqqpsqsprtspnrlspkqssdsgsae 211
Cdd:cd16296    81 GP------------------------------------------------------------------------------ 82

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 212 ngqCPPEDSSAGANRKAWGRDPSLVVAFVCKLHLRKGNFLVLKAKELGLPVGTAAIAPIIAAVKDGKSITYEGREIAAEE 291
Cdd:cd16296    83 ---NKQSPDKIGVRRQILERDPSLVVAFICKLHLKKGNFLVLKAKELGLPVGTAAIAPIIAAVKDGKSITFEGREILAEE 159

                         250
                  ....*....|....*.
gi 1386806178 292 LCTPPDPGLVFIVVEC 307
Cdd:cd16296   160 LCTPPDPGIVFIVVEC 175
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 479-689 4.69e-102

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


Pssm-ID: 293804 [Multi-domain]  Cd Length: 204  Bit Score: 314.10  E-value: 4.69e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 479 IVFLGTGSAIPMKIRNVSSTLVNLSPDKSVLLDCGEGTFGQLCRHYGQQ-IDRVLCSLTAVFVSHLHADHHTGLLNILLQ 557
Cdd:cd07718     1 VVFLGTGSAIPSKYRNVSGILLRIPGDGSILLDCGEGTLGQLRRHYGPEeADEVLRNLKCIFISHLHADHHLGLIRLLAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 558 REHALRsffqaslgKPFQPLLVVAPTQLRAWLQQYHNHCQEILHHVSMIPAKCLQKGAEVSNTTLERLISLLLETCDLEE 637
Cdd:cd07718    81 RKKLFK--------PPSPPLYVVAPRQLRRWLREYSSLEDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLLEELGLKS 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1386806178 638 FQTCLVRHCKHAFGCALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEAT 689
Cdd:cd07718   153 IETVPVIHCPDAYGIVLTHEDGWKIVYSGDTRPCEALVEAGKGADLLIHEAT 204
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
478-753 7.30e-49

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 173.07  E-value: 7.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 478 EIVFLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHygqQIDrvLCSLTAVFVSHLHADHHTGLLNILLQ 557
Cdd:COG1234     2 KLTFLGTGGAVPTPGRATSSYLLE-AGGERLLIDCGEGTQRQLLRA---GLD--PRDIDAIFITHLHGDHIAGLPGLLST 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 558 REHALRSffqaslgkpfQPLLVVAPTQLRAWLQQYHNHCQEILH-HVSMIPakcLQKGaevsnttlerlislllETCDLE 636
Cdd:COG1234    76 RSLAGRE----------KPLTIYGPPGTKEFLEALLKASGTDLDfPLEFHE---IEPG----------------EVFEIG 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 637 EFQ--TCLVRHCKHAFGcALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGM 714
Cdd:COG1234   127 GFTvtAFPLDHPVPAYG-YRFEEPGRSLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAELAKETGHSTAKEAAELAA 205

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1386806178 715 RMNAEFIMLNHFSQRYAKIPLF----SPDFNEKVGIAFDHMKV 753
Cdd:COG1234   206 EAGVKRLVLTHFSPRYDDPEELlaeaRAVFPGPVELAEDGMVI 248
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 479-730 9.87e-47

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: 166.86  E-value: 9.87e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 479 IVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYGqqidRVLCSLTAVFVSHLHADHHTGLLNiLLQR 558
Cdd:cd07717     1 LTFLGTGSAVPTPERNLSSIALRL-EGELWLFDCGEGTQRQL-LRAG----LSPSKIDRIFITHLHGDHILGLPG-LLST 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 559 ehalrsffqASLGKPFQPLLVVAPTQLRAWLQQYHNHCQEILhhvsmipakclqkGAEVsntTLERLISLLLETCDLEEF 638
Cdd:cd07717    74 ---------MSLLGRTEPLTIYGPKGLKEFLETLLRLSASRL-------------PYPI---EVHELEPDPGLVFEDDGF 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 639 Q--TCLVRHCKHAFGCALVhsSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGMRM 716
Cdd:cd07717   129 TvtAFPLDHRVPCFGYRFE--EGRKIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKAKETGHSTAKQAAEIAKKA 206

                         250
                  ....*....|....
gi 1386806178 717 NAEFIMLNHFSQRY 730
Cdd:cd07717   207 GVKKLVLTHFSARY 220
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 479-688 1.91e-40

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: 147.02  E-value: 1.91e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 479 IVFLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHyGQQIDRvlcsLTAVFVSHLHADHHTGLLNILLQR 558
Cdd:cd16272     1 LTFLGTGGAVPSLTRNTSSYLLE-TGGTRILLDCGEGTVYRLLKA-GVDPDK----LDAIFLSHFHLDHIGGLPTLLFAR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 559 EHALRSffqaslgkpfQPLLVVAPTQLRAWLQQYHNHCQEILHHVSmipakclqkgaevsnTTLERLISLLLETCDLEEF 638
Cdd:cd16272    75 RYGGRK----------KPLTIYGPKGIKEFLEKLLNFPVEILPLGF---------------PLEIEELEEGGEVLELGDL 129

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1386806178 639 --QTCLVRHCKHAFGCALvHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEA 688
Cdd:cd16272   130 kvEAFPVKHSVESLGYRI-EAEGKSIVYSGDTGPCENLVELAKGADLLIHEC 180
PRK00055 PRK00055
ribonuclease Z; Reviewed
 478-730 3.40e-40

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 149.18  E-value: 3.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 478 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRvlcsltaVFVSHLHADHHTGLLNI 554
Cdd:PRK00055    3 ELTFLGTGSGVPTPTRNVSSILLRL-GGELFLFDCGEGTQRQL-LKTGikpRKIDK-------IFITHLHGDHIFGLPGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 555 LLQ-----REHALRSFFQASLGKPFQPLLVVAPTqlRAWLqqyhnhcqeILHH------------VSMIPAKC----LQK 613
Cdd:PRK00055   74 LSTrslsgRTEPLTIYGPKGIKEFVETLLRASGS--LGYR---------IAEKdkpgkldaeklkALGVPPGPlfgkLKR 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 614 GAEVsntTLE--RLISLlletcdleefqTCLVRhckhafgcalVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLE 691
Cdd:PRK00055  143 GEDV---TLEdgRIINP-----------ADVLG----------PPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFG 198

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1386806178 692 DGLEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHFSQRY 730
Cdd:PRK00055  199 DEDEELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRY 237
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 478-730 2.83e-34

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: 133.11  E-value: 2.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 478 EIVFLGTGSAIPMKIRNVSSTLVNLsPDKSVLLDCGEGTFGQLcRHYG---QQIDRVlcsltavFVSHLHADHHTGLLNI 554
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKL-NGELWLFDCGEGTQRQM-LRSGispMKIDRI-------FITHLHGDHILGLPGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 555 L-----LQREHAL--------RSFFQASLG-----KPFQPLLV-VAPTQLRAWLQQYHNHCQEILHHV-SM--------- 605
Cdd:TIGR02651  72 LstmsfQGRKEPLtiygppgiKEFIETSLRvsytyLNYPIKIHeIEEGGLVFEDDGFKVEAFPLDHSIpSLgyrfeekdr 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 606 -------------IPA----KCLQKGAEVsnTTLERlislllETCDLEEFqTCLVRHckhafgcalvhssGWKVVYSGDT 668
Cdd:TIGR02651 152 pgkfdrekakelgIPPgplyGKLKRGETV--TLIDG------RIIDPEDV-LGPPRK-------------GRKIAYTGDT 209

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386806178 669 MPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHFSQRY 730
Cdd:TIGR02651 210 RPCEEVIEFAKNADLLIHEATFLDEDKKLAKEYGHSTAAQAAEIAKEANVKRLILTHISPRY 271
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 478-686 4.93e-23

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: 97.20  E-value: 4.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 478 EIVFLGTGSAIPMKIRNVSSTLVnLSPDKSVLLDCGEGTFGQLCRHyGQQIDRvlcsLTAVFVSHLHADHHTGLLNILLQ 557
Cdd:cd07719     1 RVTLLGTGGPIPDPDRAGPSTLV-VVGGRVYLVDAGSGVVRRLAQA-GLPLGD----LDAVFLTHLHSDHVADLPALLLT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 558 REHALRSffqaslgkpfQPLLVVAPTQLRAWLQQY-HNHCQEILHHVSMIPAKCLQKGAEVSNTTlerlISLLLETCDLE 636
Cdd:cd07719    75 AWLAGRK----------TPLPVYGPPGTRALVDGLlAAYALDIDYRARIGDEGRPDPGALVEVHE----IAAGGVVYEDD 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1386806178 637 EFQ--TCLVRH--CKHAFgcAL-VHSSGWKVVYSGDTMPCEALVQMGKDATLLIH 686
Cdd:cd07719   141 GVKvtAFLVDHgpVPPAL--AYrFDTPGRSVVFSGDTGPSENLIELAKGADLLVH 193
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 481-688 7.28e-18

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: 82.69  E-value: 7.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 481 FLGTGSAIPMKIRNVSSTLVNlSPDKSVLLDCGEGTFGQLCRhygQQIDRVlcSLTAVFVSHLHADHHTGLLNILLQREH 560
Cdd:cd07740     2 FLGSGDAFGSGGRLNTCFHVA-SEAGRFLIDCGASSLIALKR---AGIDPN--AIDAIFITHLHGDHFGGLPFFLLDAQF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 561 -ALRSffqaslgkpfQPLLVVAPTQLRAWLQQyhnhCQEilhhvSMIPAkclqkgaevSNTTLERL-ISLLL----ETCD 634
Cdd:cd07740    76 vAKRT----------RPLTIAGPPGLRERLRR----AME-----ALFPG---------SSKVPRRFdLEVIElepgEPTT 127

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1386806178 635 LEEF--QTCLVRHCKHAFGCALVHSSGWKVV-YSGDTMPCEALVQMGKDATLLIHEA 688
Cdd:cd07740   128 LGGVtvTAFPVVHPSGALPLALRLEAAGRVLaYSGDTEWTDALVPLARGADLFICEC 184
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 496-688 1.55e-17

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: 80.95  E-value: 1.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 496 SSTLVNlSPDKSVLLDCGEGTFGQLCRHygqqIDrvLCSLTAVFVSHLHADH---HTGLLnillqreHALRSffqASLGK 572
Cdd:cd07716    19 SGYLLE-ADGFRILLDCGSGVLSRLQRY----ID--PEDLDAVVLSHLHPDHcadLGVLQ-------YARRY---HPRGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 573 PFQPLLVVAPTQlrawlqqyhnhcqeilhhvsmiPAKCLQKGAEVSNTTLERLISlllETCDLE----EFQTCLVRHCKH 648
Cdd:cd07716    82 RKPPLPLYGPAG----------------------PAERLAALYGLEDVFDFHPIE---PGEPLEigpfTITFFRTVHPVP 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1386806178 649 AFGCALVHSSGwKVVYSGDTMPCEALVQMGKDATLLIHEA 688
Cdd:cd07716   137 CYAMRIEDGGK-VLVYTGDTGYCDELVEFARGADLLLCEA 175
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 73-160 1.71e-16

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: 78.07  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178  73 NRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPK-CVLSGPPQLEKYLEAIKIFSGPLK 151
Cdd:cd16272    27 TRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRKKpLTIYGPKGIKEFLEKLLNFPVEIL 106


                  ....*....
gi 1386806178 152 GIELAVRPH 160
Cdd:cd16272   107 PLGFPLEIE 115
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 478-753 5.78e-16

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 78.78  E-value: 5.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 478 EIVFLGTGSAIPM----------------KIRNVSSTLVNlSPDKSVLLDCGEGtFGQLCRHYGQQIDRvlcsLTAVFVS 541
Cdd:COG1235     2 KVTFLGSGSSGGVpqigcdcpvcastdprYGRTRSSILVE-ADGTRLLIDAGPD-LREQLLRLGLDPSK----IDAILLT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 542 HLHADHHTGLLNillqrehaLRSFFQAslgkpfQPLLVVAP----TQLRAWLQQYHNHCQEILHHVSMIPAKClqkgaev 617
Cdd:COG1235    76 HEHADHIAGLDD--------LRPRYGP------NPIPVYATpgtlEALERRFPYLFAPYPGKLEFHEIEPGEP------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 618 snttlerlisllLETCDLeEFQTCLVRH-CKHAFGCaLVHSSGWKVVYSGDT-MPCEALVQMGKDATLLIHEATLEDGle 695
Cdd:COG1235   135 ------------FEIGGL-TVTPFPVPHdAGDPVGY-RIEDGGKKLAYATDTgYIPEEVLELLRGADLLILDATYDDP-- 198

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386806178 696 eeavEKTHSTTSQAINVGMRMNAEFIMLNHFSQRYAKIPLF-----SPDFNEKVGIAFDHMKV 753
Cdd:COG1235   199 ----EPGHLSNEEALELLARLGPKRLVLTHLSPDNNDHELDydeleAALLPAGVEVAYDGMEI 257
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 66-112 9.84e-15

tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related structurally to the Lactamase_B family members. tRNase Z is the endonuclease that is involved in tRNA 3'-end maturation through removal of the 3'-trailer sequences from tRNA precursors. The fission yeast Schizosaccharomyces pombe contains two candidate tRNase Zs encoded by two essential genes. The first, Swiss:Q10155, is targeted to the nucleus and has an SV40 nuclear localization signal at its N-terminus, consisting of four consecutive arginine and lysine residues between residues 208 and 211 (KKRK) that is critical for the NLS function. The second, Swiss:P87168, is targeted to the mitochondria, with an N-terminal mitochondrial targeting signal within the first 38 residues.


Pssm-ID: 404562 [Multi-domain]  Cd Length: 63  Bit Score: 69.15  E-value: 9.84e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1386806178  66 LYVFSEYNRYLF-NCGEGVQRLMQEHKLKVARLDNIFLTRMH-WSNVGG 112
Cdd:pfam13691  15 LLLHFDSKRYLFgNVGEGTQRALNEQKVRLSKLEDIFLTGKVsWSNIGG 63
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 73-179 3.21e-13

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: 70.17  E-value: 3.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178  73 NRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHwsnvG----GLCGMILTLKETGLPKCV-LSGPPQLEKYLEAIKIFS 147
Cdd:cd07717    27 ELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLH----GdhilGLPGLLSTMSLLGRTEPLtIYGPKGLKEFLETLLRLS 102

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1386806178 148 GPLKGIELAVRPHSAPE---YKDETMTVYQVPI-HS 179
Cdd:cd07717   103 ASRLPYPIEVHELEPDPglvFEDDGFTVTAFPLdHR 138
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
74-172 6.37e-13

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 69.45  E-value: 6.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178  74 RYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPK-CVLSGPPQLEKYLEAIKIFSGPLKG 152
Cdd:COG1234    30 RLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGREKpLTIYGPPGTKEFLEALLKASGTDLD 109

                          90       100
                  ....*....|....*....|.
gi 1386806178 153 IELAVRPHSAPE-YKDETMTV 172
Cdd:COG1234   110 FPLEFHEIEPGEvFEIGGFTV 130
PRK00055 PRK00055
ribonuclease Z; Reviewed
 75-150 2.76e-07

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 52.88  E-value: 2.76e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1386806178  75 YLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPKCV-LSGPPQLEKYLEAIKIFSGPL 150
Cdd:PRK00055   32 FLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSGRTEPLtIYGPKGIKEFVETLLRASGSL 108
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 496-692 2.85e-05

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: 45.62  E-value: 2.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178  496 SSTLVNlSPDKSVLLDCGEGTFGQLCRHYGQQIDRvlcSLTAVFVSHLHADhHTGLLNILLQREHAlrsffqaslgkpfq 575
Cdd:smart00849   1 NSYLVR-DDGGAILIDTGPGEAEDLLAELKKLGPK---KIDAIILTHGHPD-HIGGLPELLEAPGA-------------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178  576 plLVVAPTQLRAWLQQYHNHCQEILHHV-SMIPAKCLQKGAEVsnttlerlisllletcDLEEFQTCLVRHCKHAFGCAL 654
Cdd:smart00849  62 --PVYAPEGTAELLKDLLALLGELGAEAePAPPDRTLKDGDEL----------------DLGGGELEVIHTPGHTPGSIV 123

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1386806178  655 VHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLED 692
Cdd:smart00849 124 LYLPEGKILFTGDLLFAGGDGRTLVDGGDAAASDALES 161
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 508-726 3.04e-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: 45.76  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 508 VLLDCGEGTFGQLCR--HYGQQIDRvlcSLTAVFVSHLHADHHTGLLNIllqREHALRSFFqASLG--------KPFQPL 577
Cdd:pfam12706   3 ILIDPGPDLRQQALPalQPGRLRDD---PIDAVLLTHDHYDHLAGLLDL---REGRPRPLY-APLGvlahlrrnFPYLFL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 578 LVVAPTQLR--AWLQQYHNHCQEIlhHVSMIPAKclQKGAEVSNTTLERLISLLLETcdleefqtclvrhckhafgcalv 655
Cdd:pfam12706  76 LEHYGVRVHeiDWGESFTVGDGGL--TVTATPAR--HGSPRGLDPNPGDTLGFRIEG----------------------- 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386806178 656 hsSGWKVVYSGDTMPCEALV-QMGKDATLLIHEATLEDglEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHF 726
Cdd:pfam12706 129 --PGKRVYYAGDTGYFPDEIgERLGGADLLLLDGGAWR--DDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK02126 PRK02126
ribonuclease Z; Provisional
 506-731 1.07e-04

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 45.29  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 506 KSVLLDCGegtfgqlcrhygqQID----RVLCSLTAVFVSHLHADHHTG---LLNILLQREHALRSF------------F 566
Cdd:PRK02126   28 RALLFDLG-------------DLHhlppRELLRISHIFVSHTHMDHFIGfdrLLRHCLGRPRRLRLFgppgfadqvehkL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 567 QA---SLGKPFQPLLVVAPTQLRAW-LQQYHNHCQE----------------------------ILHHvsMIP--AKCLQ 612
Cdd:PRK02126   95 AGytwNLVENYPTTFRVHEVELHDGrIRRALFSCRRafareaeeelslpdgvlldepwfrvraaFLDH--GIPclAFALE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 613 KGAEVsNTTLERLISLLLETCD-LEEFQTCL---------VRHCKHAFGC-------------ALVHSS-GWKVVYSGDT 668
Cdd:PRK02126  173 EKAHI-NIDKNRLAELGLPPGPwLRELKHAVlrgepddtpIRVLWRDGGGehervrplgelkeRVLRIEpGQKIGYVTDI 251

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1386806178 669 MP----CEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHFSQRYA 731
Cdd:PRK02126  252 GYteenLARIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQ 318
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
493-558 5.35e-04

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 41.97  E-value: 5.35e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1386806178 493 RNVSSTLVNlSPDKSVLLDCGEGTFGQLCRHY---GQQIDRVlcslTAVFVSHLHADhHTGLLNILLQR 558
Cdd:pfam00753   4 GQVNSYLIE-GGGGAVLIDTGGSAEAALLLLLaalGLGPKDI----DAVILTHGHFD-HIGGLGELAEA 66
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 73-143 2.19e-03

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: 40.19  E-value: 2.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386806178  73 NRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPKCV-LSGPPQLEKYLEAI 143
Cdd:cd07719    28 RVYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLLTAWLAGRKTPLpVYGPPGTRALVDGL 99
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 478-547 2.25e-03

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


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 40.15  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 478 EIVFLGTGSA--IPM-----------KIRNV---SSTLVNlSPDKSVLLDCGEgTF-GQLCRHYGQQIDrvlcsltAVFV 540
Cdd:cd16279     2 KLTFLGTGTSsgVPVigcdcgvcdssDPKNRrlrSSILIE-TGGKNILIDTGP-DFrQQALRAGIRKLD-------AVLL 72


                  ....*..
gi 1386806178 541 SHLHADH 547
Cdd:cd16279    73 THAHADH 79
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 479-547 3.48e-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) 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: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 39.87  E-value: 3.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386806178 479 IVFLGTGSA--IPMK-IRNVSSTLVNLsPDKSVLLDCGEGTFGQLCRHygqQIDRVlcSLTAVFVSHLHADH 547
Cdd:cd07741     1 IIFLGTGGGrfVVITqLRASGGIWIEL-NGKNIHIDPGPGALVRMCRP---KLDPT--KLDAIILSHRHLDH 66
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 479-552 4.55e-03

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: 38.98  E-value: 4.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806178 479 IVFLG-----TGSAIpmkirnvsstLVNLsPDKSVLLDCG-----EGTFGQLCRHYGQQIDrvlcSLTAVFVSHLHADhH 548
Cdd:cd16295     1 LTFLGaarevTGSCY----------LLET-GGKRILLDCGlfqggKELEELNNEPFPFDPK----EIDAVILTHAHLD-H 64


                  ....
gi 1386806178 549 TGLL 552
Cdd:cd16295    65 SGRL 68
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 503-555 4.63e-03

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


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 39.05  E-value: 4.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1386806178 503 SPDKSVLLDCGEGtfgqlCRHYGQQIDRVL-----CSLTAVFVSHLHADHHTGLLNIL 555
Cdd:cd07722    25 TGKRRILIDTGEG-----RPSYIPLLKSVLdsegnATISDILLTHWHHDHVGGLPDVL 77
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 489-558 5.31e-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) 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: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 39.02  E-value: 5.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386806178 489 PMKIRNVSSTLVnLSPDKSVLLDCgegtfgQLCRHYGQQ----IDRVLCSLTAVFVSHLHADHHTGlLNILLQR 558
Cdd:cd07739    10 EISSFPVTSTLI-YGETEAVLVDA------QFTRADAERladwIKASGKTLTTIYITHGHPDHYFG-LEVLLEA 75
 
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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