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Conserved domains on  [gi|909711114|ref|WP_049954312|]
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aryl-sulfate sulfotransferase [Halostagnicola larsenii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Arylsulfotrans super family cl26042
Arylsulfotransferase (ASST); This family consists of several bacterial Arylsulfotransferase ...
 175-340 6.84e-09

Arylsulfotransferase (ASST); This family consists of several bacterial Arylsulfotransferase proteins. Arylsulfotransferase (ASST) transfers a sulfate group from phenolic sulfate esters to a phenolic acceptor substrate.


The actual alignment was detected with superfamily member pfam14269:

Pssm-ID: 421257  Cd Length: 301  Bit Score: 56.65  E-value: 6.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114  175 GEITWEWYAEDHLTPGTpfYEEYGGHQRDGEHDDWT-----HMNDIDQLENGNFQMSIRNFDSIIEVDPETDEIV-DVIG 248
Cdd:pfam14269 107 NEVLFRWSALEHVDQIP--LELSVQPLGDFGGSEKFpwdyfHLNSVPKFGDGDYLISLRYYCSLFLIRPSNGKVMwQLNG 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114  249 EPGNKTVLDE------QHNPhRIEDEG----TMVVADSRN----------NRIVELDLESNE-EIWRYTGTANDPL--QW 305
Cdd:pfam14269 185 PTGGDFELGPnstfsyQHDA-RFVNQTedkiVISLFNNANtpfngrapttGLILDVDLQNKTvTLLRKLWDAEDPIhsVS 263

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 909711114  306 PRDADRLPNGNTLITDSRNNRVLEVAPDGEIVWEF 340
Cdd:pfam14269 264 QGSYQLLPNGHVLVGHGSIGRIEEYDANGKIVMTA 298
 
Name Accession Description Interval E-value
Arylsulfotran_2 pfam14269
Arylsulfotransferase (ASST);
175-340 6.84e-09

Arylsulfotransferase (ASST);


Pssm-ID: 372989  Cd Length: 301  Bit Score: 56.65  E-value: 6.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114  175 GEITWEWYAEDHLTPGTpfYEEYGGHQRDGEHDDWT-----HMNDIDQLENGNFQMSIRNFDSIIEVDPETDEIV-DVIG 248
Cdd:pfam14269 107 NEVLFRWSALEHVDQIP--LELSVQPLGDFGGSEKFpwdyfHLNSVPKFGDGDYLISLRYYCSLFLIRPSNGKVMwQLNG 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114  249 EPGNKTVLDE------QHNPhRIEDEG----TMVVADSRN----------NRIVELDLESNE-EIWRYTGTANDPL--QW 305
Cdd:pfam14269 185 PTGGDFELGPnstfsyQHDA-RFVNQTedkiVISLFNNANtpfngrapttGLILDVDLQNKTvTLLRKLWDAEDPIhsVS 263

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 909711114  306 PRDADRLPNGNTLITDSRNNRVLEVAPDGEIVWEF 340
Cdd:pfam14269 264 QGSYQLLPNGHVLVGHGSIGRIEEYDANGKIVMTA 298
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
 233-340 1.77e-08

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 55.40  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114 233 IIEVDPETdEIVDVIGEPGNKtvLDEQHNPHRIE--DEGTMVVADSRNNRIVELDLESNEEI-WRYTGTANDPLQWPRDA 309
Cdd:cd05819   31 IQVFDPDG-NFITSFGSFGSG--DGQFNEPAGVAvdSDGNLYVADTGNHRIQKFDPDGNFLAsFGGSGDGDGEFNGPRGI 107

                         90       100       110
                 ....*....|....*....|....*....|.
gi 909711114 310 DRLPNGNTLITDSRNNRVLEVAPDGEIVWEF 340
Cdd:cd05819  108 AVDSSGNIYVADTGNHRIQKFDPDGEFLTTF 138
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
231-363 1.12e-06

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 49.69  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114 231 DSIIEVDPETDEIVDVIGEPGNktvldeqhnPHRI---EDEGTMVVADSRNNRIVELDLESNEEIWRYTGTAndplqWPR 307
Cdd:COG3391   90 GRVSVIDLATGKVVATIPVGGG---------PRGLavdPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGA-----GPH 155

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 909711114 308 DADRLPNGNTL-ITDSRNNRVLevapdgEIVWEFDDADGTVIplayeaDRIGVGEQP 363
Cdd:COG3391  156 GIAVDPDGKRLyVANSGSNTVS------VIVSVIDTATGKVV------ATIPVGGGP 200
 
Name Accession Description Interval E-value
Arylsulfotran_2 pfam14269
Arylsulfotransferase (ASST);
175-340 6.84e-09

Arylsulfotransferase (ASST);


Pssm-ID: 372989  Cd Length: 301  Bit Score: 56.65  E-value: 6.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114  175 GEITWEWYAEDHLTPGTpfYEEYGGHQRDGEHDDWT-----HMNDIDQLENGNFQMSIRNFDSIIEVDPETDEIV-DVIG 248
Cdd:pfam14269 107 NEVLFRWSALEHVDQIP--LELSVQPLGDFGGSEKFpwdyfHLNSVPKFGDGDYLISLRYYCSLFLIRPSNGKVMwQLNG 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114  249 EPGNKTVLDE------QHNPhRIEDEG----TMVVADSRN----------NRIVELDLESNE-EIWRYTGTANDPL--QW 305
Cdd:pfam14269 185 PTGGDFELGPnstfsyQHDA-RFVNQTedkiVISLFNNANtpfngrapttGLILDVDLQNKTvTLLRKLWDAEDPIhsVS 263

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 909711114  306 PRDADRLPNGNTLITDSRNNRVLEVAPDGEIVWEF 340
Cdd:pfam14269 264 QGSYQLLPNGHVLVGHGSIGRIEEYDANGKIVMTA 298
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
 233-340 1.77e-08

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 55.40  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114 233 IIEVDPETdEIVDVIGEPGNKtvLDEQHNPHRIE--DEGTMVVADSRNNRIVELDLESNEEI-WRYTGTANDPLQWPRDA 309
Cdd:cd05819   31 IQVFDPDG-NFITSFGSFGSG--DGQFNEPAGVAvdSDGNLYVADTGNHRIQKFDPDGNFLAsFGGSGDGDGEFNGPRGI 107

                         90       100       110
                 ....*....|....*....|....*....|.
gi 909711114 310 DRLPNGNTLITDSRNNRVLEVAPDGEIVWEF 340
Cdd:cd05819  108 AVDSSGNIYVADTGNHRIQKFDPDGEFLTTF 138
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
 265-337 2.94e-07

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 51.55  E-value: 2.94e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 909711114 265 IEDEGTMVVADSRNNRIVELDLESNEEI-WRYTGTANDPLQWPRDADRLPNGNTLITDSRNNRVLEVAPDGEIV 337
Cdd:cd05819   15 VDSSGNIYVADTGNNRIQVFDPDGNFITsFGSFGSGDGQFNEPAGVAVDSDGNLYVADTGNHRIQKFDPDGNFL 88
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
231-363 1.12e-06

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 49.69  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114 231 DSIIEVDPETDEIVDVIGEPGNktvldeqhnPHRI---EDEGTMVVADSRNNRIVELDLESNEEIWRYTGTAndplqWPR 307
Cdd:COG3391   90 GRVSVIDLATGKVVATIPVGGG---------PRGLavdPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGA-----GPH 155

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 909711114 308 DADRLPNGNTL-ITDSRNNRVLevapdgEIVWEFDDADGTVIplayeaDRIGVGEQP 363
Cdd:COG3391  156 GIAVDPDGKRLyVANSGSNTVS------VIVSVIDTATGKVV------ATIPVGGGP 200
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
 233-343 2.93e-06

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 48.47  E-value: 2.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114 233 IIEVDPETDEIVdVIGEPGNKTvlDEQHNPHRI--EDEGTMVVADSRNNRIVELDLESN-EEIWRYTGTANDPLQWPRD- 308
Cdd:cd05819   78 IQKFDPDGNFLA-SFGGSGDGD--GEFNGPRGIavDSSGNIYVADTGNHRIQKFDPDGEfLTTFGSGGSGPGQFNGPTGv 154

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 909711114 309 -ADrlPNGNTLITDSRNNRVLEVAPDGEIVWEFDDA 343
Cdd:cd05819  155 aVD--SDGNIYVADTGNHRIQVFDPDGNFLTTFGST 188
Arylsulfotrans pfam05935
Arylsulfotransferase (ASST); This family consists of several bacterial Arylsulfotransferase ...
 173-272 6.17e-06

Arylsulfotransferase (ASST); This family consists of several bacterial Arylsulfotransferase proteins. Arylsulfotransferase (ASST) transfers a sulfate group from phenolic sulfate esters to a phenolic acceptor substrate.


Pssm-ID: 399139  Cd Length: 368  Bit Score: 48.13  E-value: 6.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114  173 RDGEITWEWYAEDHLTP---GTPFYEEYGGHQRDGE--HDDWTHMNDIDQLENGN-FQMSIRNFDSIIEVDPETDEIVDV 246
Cdd:pfam05935 131 KTGEVVDVWDLFKILDPyrdALLKALDAPFGDIPGVggGRDWAHINSIQYDEKDDsIIVSSRHQSAVVKIDYRTGKVKWI 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 909711114  247 IGEPG--NKTVLD----------------EQHNPHRIEDEGTMV 272
Cdd:pfam05935 211 LGDPEgwSKELQKklltpvdsegdfdwtwGQHTAVLIPNGSLMV 254
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
 260-340 1.01e-05

NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271324 [Multi-domain]  Cd Length: 285  Bit Score: 47.16  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114 260 HNPHRI--EDEGTMVVADSRNNRIVELDlESNEEIWRY--TGTANDPLQWPRDADRLPNGNTLITDSRNNRVLEVAPDGE 335
Cdd:cd14954  165 DSPRGVavNPDGNIVVSDFNNHRLQVFD-PDGQFLRFFgsEGSGNGQFKRPRGVAVDDEGNIIVADSGNHRVQVFSPDGE 243


                 ....*
gi 909711114 336 IVWEF 340
Cdd:cd14954  244 FLCSF 248
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
 231-334 1.30e-05

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 46.54  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114 231 DSIIEVDPETdEIVDVIGEPGNKtvlDEQ-HNPH--RIEDEGTMVVADSRNNRIVELDLESN-EEIWRYTGTANDPLQWP 306
Cdd:cd05819  123 HRIQKFDPDG-EFLTTFGSGGSG---PGQfNGPTgvAVDSDGNIYVADTGNHRIQVFDPDGNfLTTFGSTGTGPGQFNYP 198

                         90       100
                 ....*....|....*....|....*...
gi 909711114 307 RDADRLPNGNTLITDSRNNRVLEVAPDG 334
Cdd:cd05819  199 TGIAVDSDGNIYVADSGNNRVQVFDPDG 226
NHL_like_3 cd14956
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ...
 265-359 1.94e-05

Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271326 [Multi-domain]  Cd Length: 274  Bit Score: 46.12  E-value: 1.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114 265 IEDEGTMVVADSRNNRIVELDLESNEEI-WRYTGTANDPLQWPRDADRLPNGNTLITDSRNNRVLEVAPDGEIVWEFD-- 341
Cdd:cd14956  161 VDPDGTLYVADTYNDRIQVFDNDGAFLRkWGGRGTGPGQFNYPYGIAIDPDGNVFVADFGNNRIQKFTADGTFLTSWGsp 240

                         90       100       110
                 ....*....|....*....|....*....|...
gi 909711114 342 ---------------DADGTVIPLAYEADRIGV 359
Cdd:cd14956  241 gtgpgqfknpwgvvvDADGTVYVADSNNNRVQR 273
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
 268-330 8.47e-05

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 44.23  E-value: 8.47e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 909711114 268 EGTMVVADSRNNRIVELDLESNEEIWR-YTGTANDPLQWPRDADRLPNGNTLITDSRNNRVLEV 330
Cdd:cd05819  206 DGNIYVADSGNNRVQVFDPDGAGFGGNgNFLGSDGQFNRPSGLAVDSDGNLYVADTGNNRIQVF 269
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
231-364 1.72e-04

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 42.76  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114 231 DSIIEVDPETDEIVDVIGEPGNKTVLDEQHNPHRIEDEGTMVVADSRNNRIVELDLESNEEIWRYTGTANdplqwPRDAD 310
Cdd:COG3391   42 GGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVANSGSGRVSVIDLATGKVVATIPVGGG-----PRGLA 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 909711114 311 RLPNGNTL-ITDSRNNRvlevapdgeiVWEFDDADGTVIplayeaDRIGVGEQPD 364
Cdd:COG3391  117 VDPDGGRLyVADSGNGR----------VSVIDTATGKVV------ATIPVGAGPH 155
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
 260-356 2.75e-04

NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein with a cytosolic kinase domain and an extracellular sensor domain that contains NHL repeats. It plays a key role in the development of central nervous system tuberculosis, by mediating the invasion of host brain endothelia. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271322 [Multi-domain]  Cd Length: 247  Bit Score: 42.19  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114 260 HNPHRI--EDEGTMVVADSRNNRIVELDLESNE-EIWRYTGTANdplqwPRDADRLPNGNTLITDSRNNRVLEVAPDGEI 336
Cdd:cd14952   10 DGPGGVavDAAGNVYVADSGNNRVLKLAAGSTTqTVLPFTGLYQ-----PQGVAVDAAGTVYVTDFGNNRVLKLAAGSTT 84

                         90       100       110
                 ....*....|....*....|....*....|..
gi 909711114 337 VWE--FD----------DADGTViplaYEADR 356
Cdd:cd14952   85 QTVlpFTglndptgvavDAAGNV----YVADT 112
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
170-356 3.32e-04

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 42.31  E-value: 3.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114 170 TVDRDGEItweWYAED------HLTPGTPFYEEYGGHqrdgehDDWTHMNDIDQLENGNFQMSIRNFDSIIEVDPETDEI 243
Cdd:COG4257   65 AVDPDGNL---WFTDNgnnrigRIDPKTGEITTFALP------GGGSNPHGIAFDPDGNLWFTDQGGNRIGRLDPATGEV 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114 244 VDVIGEPGNKtvldeqhNPHRIE--DEGTMVVADSRNNRIVELDLESNEeIWRYTGTAndPLQWPRDADRLPNGNTLITD 321
Cdd:COG4257  136 TEFPLPTGGA-------GPYGIAvdPDGNLWVTDFGANAIGRIDPDTGT-LTEYALPT--PGAGPRGLAVDPDGNLWVAD 205

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 909711114 322 SRNNRVLEVAPDGEIVWEFDDADGTVIPLAYEADR 356
Cdd:COG4257  206 TGSGRIGRFDPKTGTVTEYPLPGGGARPYGVAVDG 240
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
 260-331 5.28e-04

NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein with a cytosolic kinase domain and an extracellular sensor domain that contains NHL repeats. It plays a key role in the development of central nervous system tuberculosis, by mediating the invasion of host brain endothelia. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271322 [Multi-domain]  Cd Length: 247  Bit Score: 41.42  E-value: 5.28e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 909711114 260 HNPHRI--EDEGTMVVADSRNNRIVELDLESNE-EIWRYTGTaNDPLQWPRDADrlpnGNTLITDSRNNRVLEVA 331
Cdd:cd14952  178 NSPSGVavDTAGNVYVTDHGNNRVLKLAAGSTTpTVLPFTGL-NGPLGVAVDAA----GNVYVADRGNDRVVKLP 247
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
 265-328 5.37e-04

NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271324 [Multi-domain]  Cd Length: 285  Bit Score: 41.76  E-value: 5.37e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 909711114 265 IEDEGTMVVADSRNNRIVELDlesnEEIWRYT-----GTANDPLQWPRDADRLPNGNTLITDSRNNRVL 328
Cdd:cd14954  219 VDDEGNIIVADSGNHRVQVFS----PDGEFLCsfgteGNGEGQFDRPSGVAVTPDGRIVVVDRGNHRIQ 283
NHL_TRIM71_like cd14954
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ...
 265-340 1.54e-03

NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271324 [Multi-domain]  Cd Length: 285  Bit Score: 40.22  E-value: 1.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 909711114 265 IEDEGTMVVADSRNNRIVELDLESNEeIWRYTGTANDP--LQWPRDADRLPNGNTLITDSRNNRVLEVAPDGEIVWEF 340
Cdd:cd14954  125 VDSEGRIYVSDTRNHRVQVFDSDGQF-IRKFGFEGAGPgqLDSPRGVAVNPDGNIVVSDFNNHRLQVFDPDGQFLRFF 201
NHL_PKND_like cd14952
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ...
 260-356 2.34e-03

NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein with a cytosolic kinase domain and an extracellular sensor domain that contains NHL repeats. It plays a key role in the development of central nervous system tuberculosis, by mediating the invasion of host brain endothelia. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271322 [Multi-domain]  Cd Length: 247  Bit Score: 39.50  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114 260 HNPH--RIEDEGTMVVADSRNNRIVELDlesneeiwrytGTANDPLQWPRDADRLPN-------GNTLITDSRNNRVLEV 330
Cdd:cd14952  136 SNPDgvAVDGAGNVYVTDTGNNRVLKLA-----------AGSTTQTVLPFTGLNSPSgvavdtaGNVYVTDHGNNRVLKL 204

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 909711114 331 AP--DGEIVWEFD----------DADGTViplaYEADR 356
Cdd:cd14952  205 AAgsTTPTVLPFTglngplgvavDAAGNV----YVADR 238
NHL cd05819
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
 297-340 3.10e-03

NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.


Pssm-ID: 271320 [Multi-domain]  Cd Length: 269  Bit Score: 39.22  E-value: 3.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 909711114 297 GTANDPLQWPRDADRLPNGNTLITDSRNNRVLEVAPDGEIVWEF 340
Cdd:cd05819    1 GTGPGELNNPQGIAVDSSGNIYVADTGNNRIQVFDPDGNFITSF 44
NHL_like_1 cd14953
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ...
 269-336 4.44e-03

Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271323 [Multi-domain]  Cd Length: 323  Bit Score: 39.05  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114 269 GTMVVADSRNNRIVELDLE--------SNEEIWRYTGTANDP-LQWPR----DAdrlpNGNTLITDSRNNRVLEVAPDGE 335
Cdd:cd14953  198 GNLYVADRGNHRIRKITPDgvvttvagTGTAGFSGDGGATAAqLNNPTgvavDA----AGNLYVADSGNHRIRKITPAGV 273


                 .
gi 909711114 336 I 336
Cdd:cd14953  274 V 274
NHL_TRIM32_like cd14961
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ...
 260-335 7.05e-03

NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; The E3 ubiquitin-protein ligase TRIM32 (HT2A) is widely expressed and is responsible for ubiquinating a large variety of targets, including dysbindin (DTNBP1), NPHP7/Glis2, TAp73, and others. TRIM32 promotes disassociation of the plakoglobin-PI3K complex and reduces PI3K-Akt-FoxO signaling. Mutations in TRIM32 have been implemented in the two diverse diseases limb-girdle muscular dystrophy type 2H (LGMD2H) or sarcotubular myopathy (STM) and Bardet-Biedl syndrome type 11 (BBS11). The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.


Pssm-ID: 271331 [Multi-domain]  Cd Length: 273  Bit Score: 38.03  E-value: 7.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 909711114 260 HNPHRIE--DEGTMVVADSRNNRIVELDLESNEEIWR-YTGTANDPLQWPRDADRLPNGNTLITDSRNNRVLEVAPDGE 335
Cdd:cd14961   11 NNPTGVAvtPTGRVVVADDGNKRIQVFDSDGNCLQQFgPKGDAGQDIRYPLDVAVTPDGHIVVTDAGDRSVKVFSFDGR 89
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
228-337 9.79e-03

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 37.69  E-value: 9.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 909711114 228 RNFDSIIEVDPETDEIVDVIGEPGNKTvldeqhnPHRIE--DEGTMVVADSRNNRIVELDLESnEEIWRYTgtANDPLQW 305
Cdd:COG4257  163 FGANAIGRIDPDTGTLTEYALPTPGAG-------PRGLAvdPDGNLWVADTGSGRIGRFDPKT-GTVTEYP--LPGGGAR 232

                         90       100       110
                 ....*....|....*....|....*....|..
gi 909711114 306 PRDADRLPNGNTLITDSRNNRVLEVAPDGEIV 337
Cdd:COG4257  233 PYGVAVDGDGRVWFAESGANRIVRFDPDTELT 264
 
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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