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Conserved domains on  [gi|1518538928|ref|WP_123396379|]
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MULTISPECIES: ribonuclease Z [Muribaculum]

Protein Classification

ribonuclease Z( domain architecture ID 10869904)

ribonuclease Z is a tRNA 3-prime endonuclease that is involved in the maturation of tRNA, such as processing of tRNAs that lack an encoded CCA motif at the 3' end, to prepare for the addition of the motif by tRNA nucleotidyltransferase

CATH:  3.60.15.10
EC:  3.1.26.11
Gene Ontology:  GO:0042781|GO:0046872
PubMed:  17597585|11471246|17363966|12032089
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 6-301 1.19e-106

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: 310.54  E-value: 1.19e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928   6 INYLGCGSATPTLRHLPSCQVVDFRDNLFMIDCGEGAQLSMRRQRLKFSRLSHIFISHLHGDHCLGLPGLVSTLALTGRE 85
Cdd:cd07717     1 LTFLGTGSAVPTPERNLSSIALRLEGELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGRT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  86 gGDITIHTFKEGVEIFKTMLDFFCRETPFTIHYNVINPrGNEVLFENDSIVVRSFPLYHRVPCSGFVFAEkpklrhlrgd 165
Cdd:cd07717    81 -EPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEP-DPGLVFEDDGFTVTAFPLDHRVPCFGYRFEE---------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 166 mvrfynvpirqyqaikggadfvtddGRvipnewltlpadaavSYAYCSDTVYDERVAAAVEGVDTIYHEATYTDEYADKA 245
Cdd:cd07717   149 -------------------------GR---------------KIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKA 188

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1518538928 246 RSRGHSTAAEAARIARLAGANRLVLGHFSKRYIDEAKHLDEAKEIFPNTIIAYEGM 301
Cdd:cd07717   189 KETGHSTAKQAAEIAKKAGVKKLVLTHFSARYKDPEELLKEARAVFPNTILAEDFM 244
 
Name Accession Description Interval E-value
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 6-301 1.19e-106

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: 310.54  E-value: 1.19e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928   6 INYLGCGSATPTLRHLPSCQVVDFRDNLFMIDCGEGAQLSMRRQRLKFSRLSHIFISHLHGDHCLGLPGLVSTLALTGRE 85
Cdd:cd07717     1 LTFLGTGSAVPTPERNLSSIALRLEGELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGRT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  86 gGDITIHTFKEGVEIFKTMLDFFCRETPFTIHYNVINPrGNEVLFENDSIVVRSFPLYHRVPCSGFVFAEkpklrhlrgd 165
Cdd:cd07717    81 -EPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEP-DPGLVFEDDGFTVTAFPLDHRVPCFGYRFEE---------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 166 mvrfynvpirqyqaikggadfvtddGRvipnewltlpadaavSYAYCSDTVYDERVAAAVEGVDTIYHEATYTDEYADKA 245
Cdd:cd07717   149 -------------------------GR---------------KIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKA 188

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1518538928 246 RSRGHSTAAEAARIARLAGANRLVLGHFSKRYIDEAKHLDEAKEIFPNTIIAYEGM 301
Cdd:cd07717   189 KETGHSTAKQAAEIAKKAGVKKLVLTHFSARYKDPEELLKEARAVFPNTILAEDFM 244
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 6-301 1.78e-104

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: 306.84  E-value: 1.78e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928   6 INYLGCGSATPTLRHLPSCQVVDFRDNLFMIDCGEGAQLSMRRQRLKFSRLSHIFISHLHGDHCLGLPGLVSTLALTGRE 85
Cdd:TIGR02651   2 ITFLGTGGGVPTKERNLPSIALKLNGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGRK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  86 GgDITIHTFKEGVEIFKTMLDFFCRETPFTIHYNVINPrgNEVLFENDSIVVRSFPLYHRVPCSGFVFAEKPKLRHLRGD 165
Cdd:TIGR02651  82 E-PLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEE--GGLVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDRE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 166 MVRFYNVPI-RQYQAIKGGADFVTDDGRVIPNEWLTLPADAAVSYAYCSDTVYDERVAAAVEGVDTIYHEATYTDEYADK 244
Cdd:TIGR02651 159 KAKELGIPPgPLYGKLKRGETVTLIDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDKKL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1518538928 245 ARSRGHSTAAEAARIARLAGANRLVLGHFSKRYIDEAKHLDEAKEIFPNTIIAYEGM 301
Cdd:TIGR02651 239 AKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDEEELLEEAKKIFPNTYIAEDFM 295
PRK00055 PRK00055
ribonuclease Z; Reviewed
 4-305 7.42e-101

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 296.71  E-value: 7.42e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928   4 FQINYLGCGSATPTLRHLPSCQVVDFRDNLFMIDCGEGAQLSMRRQRLKFSRLSHIFISHLHGDHCLGLPGLVSTLALTG 83
Cdd:PRK00055    2 MELTFLGTGSGVPTPTRNVSSILLRLGGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  84 REGgDITIHTFKEGVEIFKTMLDFFcretpftihynvinprgnevlfendsivvrsfplyhrvPCSGFVFAEKPKLRHLR 163
Cdd:PRK00055   82 RTE-PLTIYGPKGIKEFVETLLRAS--------------------------------------GSLGYRIAEKDKPGKLD 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 164 GDMVRFYNVPIRQ-YQAIKGGADFVTDDGRVIPNEWLTLPADAAVSYAYCSDTVYDERVAAAVEGVDTIYHEATYTDEYA 242
Cdd:PRK00055  123 AEKLKALGVPPGPlFGKLKRGEDVTLEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDE 202

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1518538928 243 DKARSRGHSTAAEAARIARLAGANRLVLGHFSKRY-IDEAKHLDEAKEIFPNTIIAYEGMFLDL 305
Cdd:PRK00055  203 ELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYtGDPEELLKEAREIFPNTELAEDLMRVEV 266
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
4-305 2.29e-83

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 251.27  E-value: 2.29e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928   4 FQINYLGCGSATPTLRHLPSCQVVDFRDNLFMIDCGEGAQLSMRRQRLKFSRLSHIFISHLHGDHCLGLPGLVSTLALTG 83
Cdd:COG1234     1 MKLTFLGTGGAVPTPGRATSSYLLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  84 REgGDITIHTFKEGVEIFKTMLDFFCRETPFTIHYNVINPrgnEVLFENDSIVVRSFPLYHRVPCSGFVFAEKPKlrhlr 163
Cdd:COG1234    81 RE-KPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEP---GEVFEIGGFTVTAFPLDHPVPAYGYRFEEPGR----- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 164 gdmvrfynvpirqyqaikggadfvtddgrvipnewltlpadaavSYAYCSDTVYDERVAAAVEGVDTIYHEATYTDEYAD 243
Cdd:COG1234   152 --------------------------------------------SLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAE 187

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1518538928 244 KARSRGHSTAAEAARIARLAGANRLVLGHFSKRYIDEAKHLDEAKEIFP-NTIIAYEGMFLDL 305
Cdd:COG1234   188 LAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDDPEELLAEARAVFPgPVELAEDGMVIEL 250
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 36-273 5.66e-12

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: 63.48  E-value: 5.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  36 IDCGEG-AQLSMRR---QRLKFSRLSHIFISHLHGDHCLGLPGLvstlaltgREGGDITIHTFKEGVEIFKTMLDFFCRE 111
Cdd:pfam12706   5 IDPGPDlRQQALPAlqpGRLRDDPIDAVLLTHDHYDHLAGLLDL--------REGRPRPLYAPLGVLAHLRRNFPYLFLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 112 TPFTIHYNVINPrGNEVLFENDSIVVRSFPLYHRVPcsgfvfaekPKLRHLRGDMVRFynvpirqyqaikggadFVTDDG 191
Cdd:pfam12706  77 EHYGVRVHEIDW-GESFTVGDGGLTVTATPARHGSP---------RGLDPNPGDTLGF----------------RIEGPG 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 192 RVIpnewltlpadaavsyAYCSDTVY-DERVAAAVEGVDTIYHEATYTDEyaDKARSRGHSTAAEAARIARLAGANRLVL 270
Cdd:pfam12706 131 KRV---------------YYAGDTGYfPDEIGERLGGADLLLLDGGAWRD--DEMIHMGHMTPEEAVEAAADLGARRKVL 193


                  ...
gi 1518538928 271 GHF 273
Cdd:pfam12706 194 IHI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 26-141 1.29e-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: 44.85  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928   26 VVDFRDNLFMIDCGEGAQLSMRR--QRLKFSRLSHIFISHLHGDHCLGLPGLVSTLaltgreggDITIHTFKEGVEIFKT 103
Cdd:smart00849   4 LVRDDGGAILIDTGPGEAEDLLAelKKLGPKKIDAIILTHGHPDHIGGLPELLEAP--------GAPVYAPEGTAELLKD 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1518538928  104 MLDFFCRETPFTIHYNVINP--RGNEVLFENDSIVVRSFP 141
Cdd:smart00849  76 LLALLGELGAEAEPAPPDRTlkDGDELDLGGGELEVIHTP 115
 
Name Accession Description Interval E-value
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 6-301 1.19e-106

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: 310.54  E-value: 1.19e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928   6 INYLGCGSATPTLRHLPSCQVVDFRDNLFMIDCGEGAQLSMRRQRLKFSRLSHIFISHLHGDHCLGLPGLVSTLALTGRE 85
Cdd:cd07717     1 LTFLGTGSAVPTPERNLSSIALRLEGELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLPGLLSTMSLLGRT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  86 gGDITIHTFKEGVEIFKTMLDFFCRETPFTIHYNVINPrGNEVLFENDSIVVRSFPLYHRVPCSGFVFAEkpklrhlrgd 165
Cdd:cd07717    81 -EPLTIYGPKGLKEFLETLLRLSASRLPYPIEVHELEP-DPGLVFEDDGFTVTAFPLDHRVPCFGYRFEE---------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 166 mvrfynvpirqyqaikggadfvtddGRvipnewltlpadaavSYAYCSDTVYDERVAAAVEGVDTIYHEATYTDEYADKA 245
Cdd:cd07717   149 -------------------------GR---------------KIAYLGDTRPCEGLVELAKGADLLIHEATFLDDDAEKA 188

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1518538928 246 RSRGHSTAAEAARIARLAGANRLVLGHFSKRYIDEAKHLDEAKEIFPNTIIAYEGM 301
Cdd:cd07717   189 KETGHSTAKQAAEIAKKAGVKKLVLTHFSARYKDPEELLKEARAVFPNTILAEDFM 244
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 6-301 1.78e-104

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: 306.84  E-value: 1.78e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928   6 INYLGCGSATPTLRHLPSCQVVDFRDNLFMIDCGEGAQLSMRRQRLKFSRLSHIFISHLHGDHCLGLPGLVSTLALTGRE 85
Cdd:TIGR02651   2 ITFLGTGGGVPTKERNLPSIALKLNGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTMSFQGRK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  86 GgDITIHTFKEGVEIFKTMLDFFCRETPFTIHYNVINPrgNEVLFENDSIVVRSFPLYHRVPCSGFVFAEKPKLRHLRGD 165
Cdd:TIGR02651  82 E-PLTIYGPPGIKEFIETSLRVSYTYLNYPIKIHEIEE--GGLVFEDDGFKVEAFPLDHSIPSLGYRFEEKDRPGKFDRE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 166 MVRFYNVPI-RQYQAIKGGADFVTDDGRVIPNEWLTLPADAAVSYAYCSDTVYDERVAAAVEGVDTIYHEATYTDEYADK 244
Cdd:TIGR02651 159 KAKELGIPPgPLYGKLKRGETVTLIDGRIIDPEDVLGPPRKGRKIAYTGDTRPCEEVIEFAKNADLLIHEATFLDEDKKL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1518538928 245 ARSRGHSTAAEAARIARLAGANRLVLGHFSKRYIDEAKHLDEAKEIFPNTIIAYEGM 301
Cdd:TIGR02651 239 AKEYGHSTAAQAAEIAKEANVKRLILTHISPRYSDEEELLEEAKKIFPNTYIAEDFM 295
PRK00055 PRK00055
ribonuclease Z; Reviewed
 4-305 7.42e-101

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 296.71  E-value: 7.42e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928   4 FQINYLGCGSATPTLRHLPSCQVVDFRDNLFMIDCGEGAQLSMRRQRLKFSRLSHIFISHLHGDHCLGLPGLVSTLALTG 83
Cdd:PRK00055    2 MELTFLGTGSGVPTPTRNVSSILLRLGGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLLSTRSLSG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  84 REGgDITIHTFKEGVEIFKTMLDFFcretpftihynvinprgnevlfendsivvrsfplyhrvPCSGFVFAEKPKLRHLR 163
Cdd:PRK00055   82 RTE-PLTIYGPKGIKEFVETLLRAS--------------------------------------GSLGYRIAEKDKPGKLD 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 164 GDMVRFYNVPIRQ-YQAIKGGADFVTDDGRVIPNEWLTLPADAAVSYAYCSDTVYDERVAAAVEGVDTIYHEATYTDEYA 242
Cdd:PRK00055  123 AEKLKALGVPPGPlFGKLKRGEDVTLEDGRIINPADVLGPPRKGRKVAYCGDTRPCEALVELAKGADLLVHEATFGDEDE 202

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1518538928 243 DKARSRGHSTAAEAARIARLAGANRLVLGHFSKRY-IDEAKHLDEAKEIFPNTIIAYEGMFLDL 305
Cdd:PRK00055  203 ELAKEYGHSTARQAAEIAKEAGVKRLILTHFSPRYtGDPEELLKEAREIFPNTELAEDLMRVEV 266
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
4-305 2.29e-83

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 251.27  E-value: 2.29e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928   4 FQINYLGCGSATPTLRHLPSCQVVDFRDNLFMIDCGEGAQLSMRRQRLKFSRLSHIFISHLHGDHCLGLPGLVSTLALTG 83
Cdd:COG1234     1 MKLTFLGTGGAVPTPGRATSSYLLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  84 REgGDITIHTFKEGVEIFKTMLDFFCRETPFTIHYNVINPrgnEVLFENDSIVVRSFPLYHRVPCSGFVFAEKPKlrhlr 163
Cdd:COG1234    81 RE-KPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEP---GEVFEIGGFTVTAFPLDHPVPAYGYRFEEPGR----- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 164 gdmvrfynvpirqyqaikggadfvtddgrvipnewltlpadaavSYAYCSDTVYDERVAAAVEGVDTIYHEATYTDEYAD 243
Cdd:COG1234   152 --------------------------------------------SLVYSGDTRPCEALVELAKGADLLIHEATFLDEEAE 187

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1518538928 244 KARSRGHSTAAEAARIARLAGANRLVLGHFSKRYIDEAKHLDEAKEIFP-NTIIAYEGMFLDL 305
Cdd:COG1234   188 LAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDDPEELLAEARAVFPgPVELAEDGMVIEL 250
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 11-305 1.88e-29

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 112.68  E-value: 1.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  11 CGSATPTLRHLPSCQVVDFRDNLFMIDCGEGAQLSMRRQRLKFSRLSHIFISHLHGDHCLGLPGLVStlaltGREGGDIT 90
Cdd:COG1235    24 CASTDPRYGRTRSSILVEADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRP-----RYGPNPIP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  91 IHTFKEGVEIFKTMLDFFCRETPFTIHYNVINPrGNEVLFENdsIVVRSFPLYH-RVPCSGFVFaekpklrhlrgdmvrf 169
Cdd:COG1235    99 VYATPGTLEALERRFPYLFAPYPGKLEFHEIEP-GEPFEIGG--LTVTPFPVPHdAGDPVGYRI---------------- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 170 ynvpirqyqaikggadfvTDDGRVIpnewltlpadaavsyAYCSDTVY-DERVAAAVEGVDTIYHEATYTDEYAdkarsr 248
Cdd:COG1235   160 ------------------EDGGKKL---------------AYATDTGYiPEEVLELLRGADLLILDATYDDPEP------ 200

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1518538928 249 GHSTAAEAARIARLAGANRLVLGHFSKRYIDE--AKHLDEAKEIFPNTIIAYEGMFLDL 305
Cdd:COG1235   201 GHLSNEEALELLARLGPKRLVLTHLSPDNNDHelDYDELEAALLPAGVEVAYDGMEIEL 259
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 9-235 9.66e-29

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: 108.50  E-value: 9.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928   9 LGCGSATPTLRHLPSCQVVDFRDNLFMIDCGEGAQLSMRRQRLKFSRLSHIFISHLHGDHCLGLPGLVSTLALTGREGGd 88
Cdd:cd16272     4 LGTGGAVPSLTRNTSSYLLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRKKP- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  89 ITIHTFKEGVEIFKTMLDFFCRETPFTIHYNVINPRGNEVLFENDSIVVRSFPLYHRVPCSGFVFaekpklrhlrgdmvr 168
Cdd:cd16272    83 LTIYGPKGIKEFLEKLLNFPVEILPLGFPLEIEELEEGGEVLELGDLKVEAFPVKHSVESLGYRI--------------- 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1518538928 169 fynvpirqyqaikggadfvTDDGRVIpnewltlpadaavsyAYCSDTVYDERVAAAVEGVDTIYHEA 235
Cdd:cd16272   148 -------------------EAEGKSI---------------VYSGDTGPCENLVELAKGADLLIHEC 180
PRK02126 PRK02126
ribonuclease Z; Provisional
 27-292 4.50e-28

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 110.78  E-value: 4.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  27 VDFRDN----LFmiDCGEGAQLSMRrqrlKFSRLSHIFISHLHGDH----------CL---------GLPGLVSTLA--- 80
Cdd:PRK02126   21 VDFLFErralLF--DLGDLHHLPPR----ELLRISHIFVSHTHMDHfigfdrllrhCLgrprrlrlfGPPGFADQVEhkl 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  81 ------LTGREGGDITIHTfkegVEIFKTMLD---FFCRETpFTIHYNVINPRGNEVLFENDSIVVRSFPLYHRVPCSGF 151
Cdd:PRK02126   95 agytwnLVENYPTTFRVHE----VELHDGRIRralFSCRRA-FAREAEEELSLPDGVLLDEPWFRVRAAFLDHGIPCLAF 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 152 VFAEKPKLRHLRGDMVRFYNVP---IRQY-QAIKGGADfvtDDGRV---------IPNEWLTLPADAAV--------SYA 210
Cdd:PRK02126  170 ALEEKAHINIDKNRLAELGLPPgpwLRELkHAVLRGEP---DDTPIrvlwrdgggEHERVRPLGELKERvlriepgqKIG 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 211 YCSDTVYDE----RVAAAVEGVDTIYHEATYTDEYADKARSRGHSTAAEAARIARLAGANRLVLGHFSKRYIDEAKHL-D 285
Cdd:PRK02126  247 YVTDIGYTEenlaRIVELAAGVDLLFIEAVFLDEDAEKARRKNHLTARQAGRLAREAGVKRLLPFHFSPRYQGRGAELyR 326


                  ....*..
gi 1518538928 286 EAKEIFP 292
Cdd:PRK02126  327 EARAAFA 333
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 9-86 5.74e-16

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: 74.47  E-value: 5.74e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1518538928   9 LGCGSATPTLRHLPSCQVVDFRDNLFMIDCGEGAQLSMRRQRLKFSRLSHIFISHLHGDHCLGLPGLVSTLALTGREG 86
Cdd:cd07719     5 LGTGGPIPDPDRAGPSTLVVVGGRVYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLLTAWLAGRKT 82
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 36-273 5.66e-12

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: 63.48  E-value: 5.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  36 IDCGEG-AQLSMRR---QRLKFSRLSHIFISHLHGDHCLGLPGLvstlaltgREGGDITIHTFKEGVEIFKTMLDFFCRE 111
Cdd:pfam12706   5 IDPGPDlRQQALPAlqpGRLRDDPIDAVLLTHDHYDHLAGLLDL--------REGRPRPLYAPLGVLAHLRRNFPYLFLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 112 TPFTIHYNVINPrGNEVLFENDSIVVRSFPLYHRVPcsgfvfaekPKLRHLRGDMVRFynvpirqyqaikggadFVTDDG 191
Cdd:pfam12706  77 EHYGVRVHEIDW-GESFTVGDGGLTVTATPARHGSP---------RGLDPNPGDTLGF----------------RIEGPG 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 192 RVIpnewltlpadaavsyAYCSDTVY-DERVAAAVEGVDTIYHEATYTDEyaDKARSRGHSTAAEAARIARLAGANRLVL 270
Cdd:pfam12706 131 KRV---------------YYAGDTGYfPDEIGERLGGADLLLLDGGAWRD--DEMIHMGHMTPEEAVEAAADLGARRKVL 193


                  ...
gi 1518538928 271 GHF 273
Cdd:pfam12706 194 IHI 196
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 9-75 1.10e-11

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: 62.95  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928   9 LGCGSATP--------TLRHLPScqvvdfrDNLFMIDCGEGAQLSMRRQ------RLKFSRLSHIFISHLHGDHCLGLPG 74
Cdd:cd07718     4 LGTGSAIPskyrnvsgILLRIPG-------DGSILLDCGEGTLGQLRRHygpeeaDEVLRNLKCIFISHLHADHHLGLIR 76


                  .
gi 1518538928  75 L 75
Cdd:cd07718    77 L 77
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 9-153 1.21e-10

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: 59.58  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928   9 LGCGSATPTLRHLPSCQVVDFRDNLFMIDCGEGAQLSMRRQRLKFSRLSHIFISHLHGDHCLGLPGLVSTLALTGREGGD 88
Cdd:cd07740     3 LGSGDAFGSGGRLNTCFHVASEAGRFLIDCGASSLIALKRAGIDPNAIDAIFITHLHGDHFGGLPFFLLDAQFVAKRTRP 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  89 ITIH---TFKEGVE-IFKTMLDFFCRETP-FTIHYNVINPrgnEVLFENDSIVVRSFPLYHRVPCSGFVF 153
Cdd:cd07740    83 LTIAgppGLRERLRrAMEALFPGSSKVPRrFDLEVIELEP---GEPTTLGGVTVTAFPVVHPSGALPLAL 149
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 35-229 1.72e-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: 58.99  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  35 MIDCGEGAqLSMRRQRLKFSRLSHIFISHLHGDHCLGLPGL--VSTLALTGREGGDITIHTFKEGVEIFKTMLDFfcrET 112
Cdd:cd07716    31 LLDCGSGV-LSRLQRYIDPEDLDAVVLSHLHPDHCADLGVLqyARRYHPRGARKPPLPLYGPAGPAERLAALYGL---ED 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 113 PFTIHynVINPRGNevlFENDSIVVRSFPLYHRVPCsgfvFAekpklrhlrgdmVRfynvpirqyqaikggadfVTDDGR 192
Cdd:cd07716   107 VFDFH--PIEPGEP---LEIGPFTITFFRTVHPVPC----YA------------MR------------------IEDGGK 147

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1518538928 193 VIpnewltlpadaavsyAYCSDTVYDERVAAAVEGVD 229
Cdd:cd07716   148 VL---------------VYTGDTGYCDELVEFARGAD 169
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 4-268 8.18e-10

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: 58.38  E-value: 8.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928   4 FQINYLGCGSAtPTLRHLPSCQVVDFRDNLF-MIDCGEG-------------AQLSMRRQRLKFSRLSHIFISHLHGDHC 69
Cdd:cd07735     1 FELVVLGCSGG-PDEGNTSSFLLDPAGSDGDiLLDAGTGvgalsleemfndiLFPSQKAAYELYQRIRHYLITHAHLDHI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  70 LGLPgLVSTlALTGREGGDITIHTFKEGVEIFKTML-------DFFCRETPFtIHYNVINPRGNEVLFENDSIVVRSFPL 142
Cdd:cd07735    80 AGLP-LLSP-NDGGQRGSPKTIYGLPETIDALKKHIfnwviwpDFTSIPSGK-YPYLRLEPIEPEYPIALTGLSVTAFPV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 143 YHRVPCS-GFvfaekpklrhlrgdmvrfynvpirqyqaikggadFVTDDGRVIpnewltlpadaavsyAYCSDTVYD--- 218
Cdd:cd07735   157 SHGVPVStAF----------------------------------LIRDGGDSF---------------LFFGDTGPDsvs 187

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1518538928 219 ---------ERVAAAVEG-VDTIYHEATYTDEYADKARSrGHST----AAEAARIARLAGANRL 268
Cdd:cd07735   188 ksprldalwRALAPLIPKkLKAIIIECSFPNSRPDALLY-GHLTpkllAEELAKLAKEVLKGAL 250
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 23-250 2.37e-07

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: 50.57  E-value: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  23 SCQVVDFRDNLFMIDCGEGAQ-LSMRRQRLKFSRLSHIFISHLHGDHCLGLPgLVSTLALTGREggdITIH-TFKEGVEI 100
Cdd:cd07715    24 SCVEVRAGGELLILDAGTGIReLGNELMKEGPPGEAHLLLSHTHWDHIQGFP-FFAPAYDPGNR---IHIYgPHKDGGSL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 101 FKTMLDFFcrETPF----------TIHYNVINPrGNEVLFenDSIVVRSFPLYHRVPCSGFvfaekpklrhlrgdmvRFy 170
Cdd:cd07715   100 EEVLRRQM--SPPYfpvpleellaAIEFHDLEP-GEPFSI--GGVTVTTIPLNHPGGALGY----------------RI- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928 171 nvpirqyqaikggadfvTDDGRVIpnewltlpadaavsyAYCSDT-------VYDERVAAAVEGVDTIYHEATYTD-EYA 242
Cdd:cd07715   158 -----------------EEDGKSV---------------VYATDTehypddgESDEALLEFARGADLLIHDAQYTDeEYP 205


                  ....*...
gi 1518538928 243 DKaRSRGH 250
Cdd:cd07715   206 SK-RGWGH 212
RNaseZ_ELAC2-N-term-like_MBL-fold cd16296
Ribonuclease Z, N-terminus of human ELAC2 and related proteins; MBL-fold metallo-hydrolase ...
 32-83 2.68e-07

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: 49.57  E-value: 2.68e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1518538928  32 NLFMIDCGEGAQLSMRRQRLKFSRLSHIFISHLHGDHCLGLPGLVSTLALTG 83
Cdd:cd16296    22 NRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETG 73
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 9-153 1.27e-06

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: 47.85  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928   9 LGCGSAT--PTLR-HLPSCQ-------------VVDFRDNLFMIDCGEgaqlSMRRQ--RLKFSRLSHIFISHLHGDHCL 70
Cdd:cd16279     6 LGTGTSSgvPVIGcDCGVCDssdpknrrlrssiLIETGGKNILIDTGP----DFRQQalRAGIRKLDAVLLTHAHADHIH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  71 GLPGLvstLALTGREGGDITIHTFKEGVEIFKTMLDFFCRETPF----TIHYNVINPRGNevlFENDSIVVRSFPLYH-R 145
Cdd:cd16279    82 GLDDL---RPFNRLQQRPIPVYASEETLDDLKRRFPYFFAATGGggvpKLDLHIIEPDEP---FTIGGLEITPLPVLHgK 155


                  ....*...
gi 1518538928 146 VPCSGFVF 153
Cdd:cd16279   156 LPSLGFRF 163
Lactamase_B_4 pfam13691
tRNase Z endonuclease; This is family of tRNase Z enzymes, that are closely related ...
 14-71 9.34e-06

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: 42.58  E-value: 9.34e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1518538928  14 ATPTLRHLPSCQVVDFRDNLFMI-DCGEGAQLSMRRQRLKFSRLSHIFISHLHGDHCLG 71
Cdd:pfam13691   4 TTPTADTPGPLLLLHFDSKRYLFgNVGEGTQRALNEQKVRLSKLEDIFLTGKVSWSNIG 62
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 26-141 1.29e-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: 44.85  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928   26 VVDFRDNLFMIDCGEGAQLSMRR--QRLKFSRLSHIFISHLHGDHCLGLPGLVSTLaltgreggDITIHTFKEGVEIFKT 103
Cdd:smart00849   4 LVRDDGGAILIDTGPGEAEDLLAelKKLGPKKIDAIILTHGHPDHIGGLPELLEAP--------GAPVYAPEGTAELLKD 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1518538928  104 MLDFFCRETPFTIHYNVINP--RGNEVLFENDSIVVRSFP 141
Cdd:smart00849  76 LLALLGELGAEAEPAPPDRTlkDGDELDLGGGELEVIHTP 115
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
26-124 1.92e-05

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 44.67  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  26 VVDFRDNLFMIDCG----EGAQLSMRRQRLKFSRLSHIFISHLHGDHCLGLPGLVSTLALTGREGGDITIHTFKEGVEIF 101
Cdd:pfam00753  10 LIEGGGGAVLIDTGgsaeAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEELGLA 89

                          90       100
                  ....*....|....*....|...
gi 1518538928 102 KTMLDFFCRETPFTIHYNVINPR 124
Cdd:pfam00753  90 ASRLGLPGPPVVPLPPDVVLEEG 112
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 23-105 4.34e-05

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 44.79  E-value: 4.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  23 SCQVVDFRDNLFMIDCGEgAQLSMRRQRLKF----SRLSHIFISHLHGDHCLGLPGLVstlaltgREGGDITIHTFKEGV 98
Cdd:COG1236    15 SCYLLETGGTRILIDCGL-FQGGKERNWPPFpfrpSDVDAVVLTHAHLDHSGALPLLV-------KEGFRGPIYATPATA 86


                  ....*..
gi 1518538928  99 EIFKTML 105
Cdd:COG1236    87 DLARILL 93
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 26-76 2.13e-04

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: 41.50  E-value: 2.13e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1518538928  26 VVDFRDNLFMIDCGEGAQLSMRRQRLKFS-RLSHIFISHLHGDHCLGLPGLV 76
Cdd:cd06262    15 VSDEEGEAILIDPGAGALEKILEAIEELGlKIKAILLTHGHFDHIGGLAELK 66
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 23-105 3.92e-04

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: 40.52  E-value: 3.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  23 SCQVVDFRDNLFMIDCG--EGAQLSMRRQRLKF----SRLSHIFISHLHGDHCLGLPGLVstlaltgREGGDITIHTFKE 96
Cdd:cd16295    13 SCYLLETGGKRILLDCGlfQGGKELEELNNEPFpfdpKEIDAVILTHAHLDHSGRLPLLV-------KEGFRGPIYATPA 85


                  ....*....
gi 1518538928  97 GVEIFKTML 105
Cdd:cd16295    86 TKDLAELLL 94
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 34-153 1.64e-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: 39.10  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  34 FMIDCGEGAQLSMRRQRLKFSRLSHIFISHLHGDHCLGLPGLVStlALTgrEGGditihTFKEGVeifktmldFFC---- 109
Cdd:cd07741    32 IHIDPGPGALVRMCRPKLDPTKLDAIILSHRHLDHSNDANVLIE--AMT--EGG-----FKKRGT--------LLApeda 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1518538928 110 -RETPfTIHYNVINPRGNEVL-------FENDSIVVRSFPLYHRVP-CSGFVF 153
Cdd:cd07741    95 lNGEP-VVLLYYHRRKLEEIEileegdeYELGGIKIEATRHKHSDPtTYGFIF 146
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 35-95 1.91e-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: 38.67  E-value: 1.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1518538928  35 MIDCGEGAQL---SMRR--QRLKFSRLSHIFISHLHGDHCLGLPGLVSTLAltgreGGDITIHTFK 95
Cdd:cd07722    31 LIDTGEGRPSyipLLKSvlDSEGNATISDILLTHWHHDHVGGLPDVLDLLR-----GPSPRVYKFP 91
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 35-138 2.42e-03

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: 38.69  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  35 MIDCGEGAQLSMRR-------QRLKFSRLSHIFISHLHGDHCLGLPGL-----VSTLALTGREGGDITIHTFKEGVEIFK 102
Cdd:COG2333    25 LIDTGPRPSFDAGErvvlpylRALGIRRLDLLVLTHPDADHIGGLAAVleafpVGRVLVSGPPDTSETYERLLEALKEKG 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1518538928 103 TMLDFFCRETPFTI---HYNVINPRGNEVLFE---NDSIVVR 138
Cdd:COG2333   105 IPVRPCRAGDTWQLggvRFEVLWPPEDLLEGSdenNNSLVLR 146
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 11-84 3.15e-03

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: 38.08  E-value: 3.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1518538928  11 CGSATPTLrhlpSCQVVDFRDNLFMIDCG-EGAQLSMRRQRLKFSRLSH----IFISHLHGDHCLGLPGLVSTLALTGR 84
Cdd:cd07734     4 GGGQEVGR----SCFLVEFKGRTVLLDCGmNPGKEDPEACLPQFELLPPeidaILISHFHLDHCGALPYLFRGFIFRGP 78
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 16-158 7.12e-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: 36.83  E-value: 7.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  16 PTLRHLPSCQVVDFRDNLFMIDCGEgAQLSMRRQRLKFSRlshIFISHLHGDHCLGLPGLvstlaltgREGGDITIHTF- 94
Cdd:cd07736    31 PSYRRRPCSALIEVDGERILLDAGL-TDLAERFPPGSIDA---ILLTHFHMDHVQGLFHL--------RWGVGDPIPVYg 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1518538928  95 ---KEGV-EIFKT--MLDFFCRETPFtihynvinprgneVLFENDSIVVRSFPLYHRVPCSGFVFAEKPK 158
Cdd:cd07736    99 ppdPQGCaDLFKHpgILDFQPLVAPF-------------QSFELGGLKITPLPLNHSKPTFGYLLESGGK 155
 
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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