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Conserved domains on  [gi|2118900534|ref|XP_044482255|]
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uncharacterized protein LOC123208782 isoform X3 [Mangifera indica]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NB-ARC super family cl26397
NB-ARC domain;
209-455 7.39e-32

NB-ARC domain;


The actual alignment was detected with superfamily member pfam00931:

Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 125.57  E-value: 7.39e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  209 RNYTFKNVWDAL-NGENVFMIGVYGMGGLGKTTLVQEVGRKAKE-EKLFDDIVFVEVSESPDIKNIQTVIANNLGLKfen 286
Cdd:pfam00931    1 REDMVEKVIGKLsEKDEPGIVGIHGMGGVGKTTLAAQIFNDFDEvEGHFDSVAWVVVSKTFTISTLQQTILQNLGLS--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  287 NLGVKLENESERAKWLYSRMEGQKILLILDNIWEPLEFEKIGIPYRADRGRNKLLFTTRNLNVLD-MMDSTNNFKMGILN 365
Cdd:pfam00931   78 EDDWDNKEEGELARKIRRALLTKRFLLVLDDVWDEEDWDKIGIPLPDRENGCRVLLTTRSEEVAGrVGGPSDPHEVELLE 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  366 ETEAWTLFTKMtdLFAENIIQTHELHSLAKDVCKECKGLPIVICTIAKALKNKSHPSYWDCALRELrEPSPRKYARYLEE 445
Cdd:pfam00931  158 PDEAWELFENK--VFPKTLGECELLEDVAKEIVEKCRGLPLALKVLGGLLSCKKTVEEWKHVYDVL-QSELKSNSYSLNS 234

                          250
                   ....*....|
gi 2118900534  446 DYAKIALSYK 455
Cdd:pfam00931  235 VRSILQLSYE 244
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 1812-1859 5.00e-22

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


:

Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 90.43  E-value: 5.00e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2118900534 1812 YYCDYCDKDITGRIRMRCAICPDFDLCVECFSVGAEVETHKSNHPYKV 1859
Cdd:cd02335      1 YHCDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDHNYRV 48
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
615-743 1.28e-14

Leucine-rich repeat (LRR) protein [Transcription];


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 78.44  E-value: 1.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  615 MSKLRVLNLGGLWQSSLPSSIDSLTNLQTLCLDNSRVKDF-AIIGKLQTLKVLSLQRSNIEVFSTELGQLTQLRLLDLSY 693
Cdd:COG4886    112 LTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSN 191

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2118900534  694 CwGLKVIaPNVISQLSQLEEFYIKGCSINwehKVLKELKLLSNLTSLELD 743
Cdd:COG4886    192 N-QITDL-PEPLGNLTNLEELDLSGNQLT---DLPEPLANLTNLETLDLS 236
GvpP super family cl44178
Gas vesicle protein YhaH [General function prediction only];
37-95 2.54e-03

Gas vesicle protein YhaH [General function prediction only];


The actual alignment was detected with superfamily member COG4980:

Pssm-ID: 444004 [Multi-domain]  Cd Length: 106  Bit Score: 39.18  E-value: 2.54e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118900534   37 KTNFDNLREEVKNLK-NARDEVQRKVTDAKRNVGE----IKQNVEDWQESVNKTITEAEQLIKE 95
Cdd:COG4980     37 KDKADDLKDKAEDLKdELKEKASELSEEAKEKLDElieeIKEKIEELKEEVEPKIEELKEEAEK 100
 
Name Accession Description Interval E-value
NB-ARC pfam00931
NB-ARC domain;
209-455 7.39e-32

NB-ARC domain;


Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 125.57  E-value: 7.39e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  209 RNYTFKNVWDAL-NGENVFMIGVYGMGGLGKTTLVQEVGRKAKE-EKLFDDIVFVEVSESPDIKNIQTVIANNLGLKfen 286
Cdd:pfam00931    1 REDMVEKVIGKLsEKDEPGIVGIHGMGGVGKTTLAAQIFNDFDEvEGHFDSVAWVVVSKTFTISTLQQTILQNLGLS--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  287 NLGVKLENESERAKWLYSRMEGQKILLILDNIWEPLEFEKIGIPYRADRGRNKLLFTTRNLNVLD-MMDSTNNFKMGILN 365
Cdd:pfam00931   78 EDDWDNKEEGELARKIRRALLTKRFLLVLDDVWDEEDWDKIGIPLPDRENGCRVLLTTRSEEVAGrVGGPSDPHEVELLE 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  366 ETEAWTLFTKMtdLFAENIIQTHELHSLAKDVCKECKGLPIVICTIAKALKNKSHPSYWDCALRELrEPSPRKYARYLEE 445
Cdd:pfam00931  158 PDEAWELFENK--VFPKTLGECELLEDVAKEIVEKCRGLPLALKVLGGLLSCKKTVEEWKHVYDVL-QSELKSNSYSLNS 234

                          250
                   ....*....|
gi 2118900534  446 DYAKIALSYK 455
Cdd:pfam00931  235 VRSILQLSYE 244
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 1812-1859 5.00e-22

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 90.43  E-value: 5.00e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2118900534 1812 YYCDYCDKDITGRIRMRCAICPDFDLCVECFSVGAEVETHKSNHPYKV 1859
Cdd:cd02335      1 YHCDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDHNYRV 48
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
615-743 1.28e-14

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 78.44  E-value: 1.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  615 MSKLRVLNLGGLWQSSLPSSIDSLTNLQTLCLDNSRVKDF-AIIGKLQTLKVLSLQRSNIEVFSTELGQLTQLRLLDLSY 693
Cdd:COG4886    112 LTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSN 191

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2118900534  694 CwGLKVIaPNVISQLSQLEEFYIKGCSINwehKVLKELKLLSNLTSLELD 743
Cdd:COG4886    192 N-QITDL-PEPLGNLTNLEELDLSGNQLT---DLPEPLANLTNLETLDLS 236
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
1811-1864 1.42e-14

Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 78.19  E-value: 1.42e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2118900534 1811 SYYCDYCDKDITGRIRMRCAICPDFDLCVECFSVGAEVETHKSNHPYKVHELKS 1864
Cdd:COG5114      5 KIHCDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIETNS 58
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 1811-1852 3.27e-09

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 53.98  E-value: 3.27e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 2118900534  1811 SYYCDYCDKDITGrIRMRCAICPDFDLCVECFSVGAEVETHK 1852
Cdd:smart00291    4 SYSCDTCGKPIVG-VRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 1812-1843 5.97e-06

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 44.78  E-value: 5.97e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2118900534 1812 YYCDYCDKDITGRIRMRCAICPDFDLCVECFS 1843
Cdd:pfam00569    5 YTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQ 36
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 590-693 4.90e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 45.22  E-value: 4.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  590 PNLEYFCMTDKYGSSfKIPEDLfTVMSKLRVLNLGG-LWQSSLPSSIDSLTNLQTLCL-DNSRVKDF-AIIGKLQTLKVL 666
Cdd:PLN00113   140 PNLETLDLSNNMLSG-EIPNDI-GSFSSLKVLDLGGnVLVGKIPNSLTNLTSLEFLTLaSNQLVGQIpRELGQMKSLKWI 217

                           90       100
                   ....*....|....*....|....*...
gi 2118900534  667 SLQRSNIE-VFSTELGQLTQLRLLDLSY 693
Cdd:PLN00113   218 YLGYNNLSgEIPYEIGGLTSLNHLDLVY 245
COG3903 COG3903
Predicted ATPase [General function prediction only];
230-317 1.63e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 43.47  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  230 VYGMGGLGKTTLVQEVGRKAKEEklFDD-IVFVEVSESPDIKNIQTVIAnnlglkfeNNLGVKLENESERAKWLYSRMEG 308
Cdd:COG3903    181 LTGPGGVGKTRLALEVAHRLADR--FPDgVWFVDLAGVTDPALVLAAVA--------RALGVRDAPGRDPAARLRAALAD 250


                   ....*....
gi 2118900534  309 QKILLILDN 317
Cdd:COG3903    251 RRLLLVLDN 259
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 227-327 1.67e-03

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 41.15  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  227 MIGVYGMGGLGKTTLVQEVGRKAKEEKLFDDIVFVEVSESPDIKNIQTVIANNLG-LKFENNLGVKLENESER---AKWL 302
Cdd:cd03238     23 LVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNKLIFIDQLQFLIDVGLGyLTLGQKLSTLSGGELQRvklASEL 102

                           90       100
                   ....*....|....*....|....*
gi 2118900534  303 YSRMEGqkILLILDNIWEPLEFEKI 327
Cdd:cd03238    103 FSEPPG--TLFILDEPSTGLHQQDI 125
GvpP COG4980
Gas vesicle protein YhaH [General function prediction only];
37-95 2.54e-03

Gas vesicle protein YhaH [General function prediction only];


Pssm-ID: 444004 [Multi-domain]  Cd Length: 106  Bit Score: 39.18  E-value: 2.54e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118900534   37 KTNFDNLREEVKNLK-NARDEVQRKVTDAKRNVGE----IKQNVEDWQESVNKTITEAEQLIKE 95
Cdd:COG4980     37 KDKADDLKDKAEDLKdELKEKASELSEEAKEKLDElieeIKEKIEELKEEVEPKIEELKEEAEK 100
 
Name Accession Description Interval E-value
NB-ARC pfam00931
NB-ARC domain;
209-455 7.39e-32

NB-ARC domain;


Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 125.57  E-value: 7.39e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  209 RNYTFKNVWDAL-NGENVFMIGVYGMGGLGKTTLVQEVGRKAKE-EKLFDDIVFVEVSESPDIKNIQTVIANNLGLKfen 286
Cdd:pfam00931    1 REDMVEKVIGKLsEKDEPGIVGIHGMGGVGKTTLAAQIFNDFDEvEGHFDSVAWVVVSKTFTISTLQQTILQNLGLS--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  287 NLGVKLENESERAKWLYSRMEGQKILLILDNIWEPLEFEKIGIPYRADRGRNKLLFTTRNLNVLD-MMDSTNNFKMGILN 365
Cdd:pfam00931   78 EDDWDNKEEGELARKIRRALLTKRFLLVLDDVWDEEDWDKIGIPLPDRENGCRVLLTTRSEEVAGrVGGPSDPHEVELLE 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  366 ETEAWTLFTKMtdLFAENIIQTHELHSLAKDVCKECKGLPIVICTIAKALKNKSHPSYWDCALRELrEPSPRKYARYLEE 445
Cdd:pfam00931  158 PDEAWELFENK--VFPKTLGECELLEDVAKEIVEKCRGLPLALKVLGGLLSCKKTVEEWKHVYDVL-QSELKSNSYSLNS 234

                          250
                   ....*....|
gi 2118900534  446 DYAKIALSYK 455
Cdd:pfam00931  235 VRSILQLSYE 244
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 1812-1859 5.00e-22

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 90.43  E-value: 5.00e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2118900534 1812 YYCDYCDKDITGRIRMRCAICPDFDLCVECFSVGAEVETHKSNHPYKV 1859
Cdd:cd02335      1 YHCDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDHNYRV 48
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
615-743 1.28e-14

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 78.44  E-value: 1.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  615 MSKLRVLNLGGLWQSSLPSSIDSLTNLQTLCLDNSRVKDF-AIIGKLQTLKVLSLQRSNIEVFSTELGQLTQLRLLDLSY 693
Cdd:COG4886    112 LTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSN 191

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2118900534  694 CwGLKVIaPNVISQLSQLEEFYIKGCSINwehKVLKELKLLSNLTSLELD 743
Cdd:COG4886    192 N-QITDL-PEPLGNLTNLEELDLSGNQLT---DLPEPLANLTNLETLDLS 236
COG5114 COG5114
Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];
1811-1864 1.42e-14

Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];


Pssm-ID: 227445 [Multi-domain]  Cd Length: 432  Bit Score: 78.19  E-value: 1.42e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2118900534 1811 SYYCDYCDKDITGRIRMRCAICPDFDLCVECFSVGAEVETHKSNHPYKVHELKS 1864
Cdd:COG5114      5 KIHCDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYHGYRIIETNS 58
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 1812-1860 5.54e-11

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 58.99  E-value: 5.54e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2118900534 1812 YYCDYCDKDITGRiRMRCAICPDFDLCVECFSVGAevETHKSNHPYKVH 1860
Cdd:cd02249      1 YSCDGCLKPIVGV-RYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 1811-1852 3.27e-09

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 53.98  E-value: 3.27e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 2118900534  1811 SYYCDYCDKDITGrIRMRCAICPDFDLCVECFSVGAEVETHK 1852
Cdd:smart00291    4 SYSCDTCGKPIVG-VRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 1814-1859 5.49e-09

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 53.50  E-value: 5.49e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2118900534 1814 CDYCDK-DITGRiRMRCAICPDFDLCVECFSVGAEVETHKSNHPYKV 1859
Cdd:cd02338      3 CDGCGKsNFTGR-RYKCLICYDYDLCADCYDSGVTTERHLFDHPMQC 48
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
607-822 8.29e-09

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 59.95  E-value: 8.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  607 IPEDLFTvMSKLRVLNLGGLWQSSLPSSIDSLTNLQTLCLDNSRVKDFAIIGKLQTLKVLSLQRSNIEVFStELGQLTQL 686
Cdd:COG4886    197 LPEPLGN-LTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLP-PLANLTNL 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  687 RLLDLSYCwGLKVIAPNVISQLSQLEEFYIKGCSINWEHKVLKELKLLSNLTSLELDIVDNDVLPRDFISKELRRYKITI 766
Cdd:COG4886    275 KTLDLSNN-QLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLL 353

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2118900534  767 GCKYYRDLITKSLRILKFACNSTISQETLRGINNVEVLLIVKPSDDEEDLDEKPTS 822
Cdd:COG4886    354 LLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLD 409
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
611-743 1.66e-08

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 59.18  E-value: 1.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  611 LFTVMSKLRVLNLGGLWQSSLPSSIDSLTNLQTLCLDNSRvkdfaIIGKLQTLKVLSLQRSNIEVFSTELGQLTQLRLLD 690
Cdd:COG4886     68 LLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE-----ELSNLTNLESLDLSGNQLTDLPEELANLTNLKELD 142

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2118900534  691 LSYCwGLKVIaPNVISQLSQLEEFYIKGCSINwehKVLKELKLLSNLTSLELD 743
Cdd:COG4886    143 LSNN-QLTDL-PEPLGNLTNLKSLDLSNNQLT---DLPEELGNLTNLKELDLS 190
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 1814-1857 1.58e-07

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 49.18  E-value: 1.58e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2118900534 1814 CDYCDKDITGrIRMRCAICPDFDLCVECFSVGaeveTHKsNHPY 1857
Cdd:cd02340      3 CDGCQGPIVG-VRYKCLVCPDYDLCESCEAKG----VHP-EHAM 40
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 1814-1855 1.76e-07

Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.


Pssm-ID: 239085  Cd Length: 49  Bit Score: 49.51  E-value: 1.76e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2118900534 1814 CDYCDKDITGRIRMRCAICPDFDLCVECFSVGAEVETHKSNH 1855
Cdd:cd02345      3 CSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLH 44
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 1814-1860 3.51e-06

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 45.81  E-value: 3.51e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2118900534 1814 CDYCDKD-ITGrIRMRCAICPDFDLCVECFSVGAEVETHKSNHPYKVH 1860
Cdd:cd02334      3 CNICKEFpITG-FRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 1812-1843 5.97e-06

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 44.78  E-value: 5.97e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2118900534 1812 YYCDYCDKDITGRIRMRCAICPDFDLCVECFS 1843
Cdd:pfam00569    5 YTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQ 36
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 1812-1858 8.28e-05

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.


Pssm-ID: 239077  Cd Length: 41  Bit Score: 41.39  E-value: 8.28e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2118900534 1812 YYCDYCDKDITgrIRMRCAICPDFDLCVECFSvgaevethKSNHPYK 1858
Cdd:cd02337      1 YTCNECKHHVE--TRWHCTVCEDYDLCITCYN--------TKNHPHK 37
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 1814-1842 2.70e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 40.13  E-value: 2.70e-04
                           10        20
                   ....*....|....*....|....*....
gi 2118900534 1814 CDYCDKDITGRIRMRCAICPDFDLCVECF 1842
Cdd:cd02339      3 CDTCRKQGIIGIRWKCAECPNYDLCTTCY 31
ZZ_EF cd02343
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ...
 1814-1855 3.98e-04

Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239083  Cd Length: 48  Bit Score: 39.99  E-value: 3.98e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2118900534 1814 CDYCDKdITGRIRMRCAICPDFDLCVECFSVGAEVETHKSNH 1855
Cdd:cd02343      3 CDGCDE-IAPWHRYRCLQCTDMDLCKTCFLGGVKPEGHEDDH 43
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 590-693 4.90e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 45.22  E-value: 4.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  590 PNLEYFCMTDKYGSSfKIPEDLfTVMSKLRVLNLGG-LWQSSLPSSIDSLTNLQTLCL-DNSRVKDF-AIIGKLQTLKVL 666
Cdd:PLN00113   140 PNLETLDLSNNMLSG-EIPNDI-GSFSSLKVLDLGGnVLVGKIPNSLTNLTSLEFLTLaSNQLVGQIpRELGQMKSLKWI 217

                           90       100
                   ....*....|....*....|....*...
gi 2118900534  667 SLQRSNIE-VFSTELGQLTQLRLLDLSY 693
Cdd:PLN00113   218 YLGYNNLSgEIPYEIGGLTSLNHLDLVY 245
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 568-711 5.76e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 44.84  E-value: 5.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  568 TKIFLPGKsNIISQLRLKDLDCPNLEYFCMTDKyGSSFKIPEDLFTVMSKLRVLNLG-GLWQSSLPSSidSLTNLQTLCL 646
Cdd:PLN00113    72 VSIDLSGK-NISGKISSAIFRLPYIQTINLSNN-QLSGPIPDDIFTTSSSLRYLNLSnNNFTGSIPRG--SIPNLETLDL 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  647 DNSRV--KDFAIIGKLQTLKVLSL--------------QRSNIEVFS-----------TELGQLTQLRLLDLSYCwGLKV 699
Cdd:PLN00113   148 SNNMLsgEIPNDIGSFSSLKVLDLggnvlvgkipnsltNLTSLEFLTlasnqlvgqipRELGQMKSLKWIYLGYN-NLSG 226

                          170
                   ....*....|..
gi 2118900534  700 IAPNVISQLSQL 711
Cdd:PLN00113   227 EIPYEIGGLTSL 238
COG3903 COG3903
Predicted ATPase [General function prediction only];
230-317 1.63e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 43.47  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  230 VYGMGGLGKTTLVQEVGRKAKEEklFDD-IVFVEVSESPDIKNIQTVIAnnlglkfeNNLGVKLENESERAKWLYSRMEG 308
Cdd:COG3903    181 LTGPGGVGKTRLALEVAHRLADR--FPDgVWFVDLAGVTDPALVLAAVA--------RALGVRDAPGRDPAARLRAALAD 250


                   ....*....
gi 2118900534  309 QKILLILDN 317
Cdd:COG3903    251 RRLLLVLDN 259
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 227-327 1.67e-03

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 41.15  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  227 MIGVYGMGGLGKTTLVQEVGRKAKEEKLFDDIVFVEVSESPDIKNIQTVIANNLG-LKFENNLGVKLENESER---AKWL 302
Cdd:cd03238     23 LVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNKLIFIDQLQFLIDVGLGyLTLGQKLSTLSGGELQRvklASEL 102

                           90       100
                   ....*....|....*....|....*
gi 2118900534  303 YSRMEGqkILLILDNIWEPLEFEKI 327
Cdd:cd03238    103 FSEPPG--TLFILDEPSTGLHQQDI 125
GvpP COG4980
Gas vesicle protein YhaH [General function prediction only];
37-95 2.54e-03

Gas vesicle protein YhaH [General function prediction only];


Pssm-ID: 444004 [Multi-domain]  Cd Length: 106  Bit Score: 39.18  E-value: 2.54e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118900534   37 KTNFDNLREEVKNLK-NARDEVQRKVTDAKRNVGE----IKQNVEDWQESVNKTITEAEQLIKE 95
Cdd:COG4980     37 KDKADDLKDKAEDLKdELKEKASELSEEAKEKLDElieeIKEKIEELKEEVEPKIEELKEEAEK 100
AAA_22 pfam13401
AAA domain;
230-318 6.87e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.48  E-value: 6.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118900534  230 VYGMGGLGKTTLVQEVGRKAKEEKlfDDIVFVEVSESPDIKNIQTVIANNLGLKfennlGVKLENESE--RAKWLYSRME 307
Cdd:pfam13401   10 LTGESGTGKTTLLRRLLEQLPEVR--DSVVFVDLPSGTSPKDLLRALLRALGLP-----LSGRLSKEEllAALQQLLLAL 82

                           90
                   ....*....|.
gi 2118900534  308 GQKILLILDNI 318
Cdd:pfam13401   83 AVAVVLIIDEA 93
 
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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