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Conserved domains on  [gi|2192205457|gb|KAH9653459|]
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protein PHOX1 [Citrus sinensis]

Protein Classification

PB1 domain-containing protein( domain architecture ID 13518705)

PB1 domain-containing protein may mediate specific protein-protein interactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PB1 pfam00564
PB1 domain;
263-340 1.73e-16

PB1 domain;


:

Pssm-ID: 395447  Cd Length: 84  Bit Score: 74.64  E-value: 1.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457 263 TVKLVFGEDI-RVAQLPLNSSLLQLREVISDRFPSCRA-VLIKYRDEEGDLVTITTDEELR--WAEASAEMQGSVRLFVV 338
Cdd:pfam00564   3 RLKLRYGGGIrRFLSVSRGISFEELRALVEQRFGLDDVdFKLKYPDEDGDLVSLTSDEDLEeaLEEARSLGSKSLRLHVF 82


                  ..
gi 2192205457 339 EV 340
Cdd:pfam00564  83 PT 84
3a0801s09 super family cl36792
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 48-193 1.37e-10

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


The actual alignment was detected with superfamily member TIGR00990:

Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 64.62  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  48 LKEEGNKLFQKRDHGGALLKYEKALKLLPrnyiDVSYLrSNMAACYMqmGLSEYPRAIHECNLALEVTPLYSKALLKRAR 127
Cdd:TIGR00990 130 LKEKGNKAYRNKDFNKAIKLYSKAIECKP----DPVYY-SNRAACHN--ALGDWEKVVEDTTAALELDPDYSKALNRRAN 202

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2192205457 128 CYEALNRLDLAFRDVTTV-LNKEPKNimaAEIAERVKKELEKRGLRVNDTVIELPPEYVePPVASIA 193
Cdd:TIGR00990 203 AYDGLGKYADALLDLTAScIIDGFRN---EQSAQAVERLLKKFAESKAKEILETKPENL-PSVTFVG 265
 
Name Accession Description Interval E-value
PB1 pfam00564
PB1 domain;
263-340 1.73e-16

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 74.64  E-value: 1.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457 263 TVKLVFGEDI-RVAQLPLNSSLLQLREVISDRFPSCRA-VLIKYRDEEGDLVTITTDEELR--WAEASAEMQGSVRLFVV 338
Cdd:pfam00564   3 RLKLRYGGGIrRFLSVSRGISFEELRALVEQRFGLDDVdFKLKYPDEDGDLVSLTSDEDLEeaLEEARSLGSKSLRLHVF 82


                  ..
gi 2192205457 339 EV 340
Cdd:pfam00564  83 PT 84
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 263-338 3.20e-16

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.


Pssm-ID: 214770  Cd Length: 81  Bit Score: 73.78  E-value: 3.20e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2192205457  263 TVKLVFGEDIRVAQLPLNSSLLQLREVISDRFP-SCRAVLIKYRDEEGDLVTITTDEELR--WAEASAEMQGSVRLFVV 338
Cdd:smart00666   3 DVKLRYGGETRRLSVPRDISFEDLRSKVAKRFGlDNQSFTLKYQDEDGDLVSLTSDEDLEeaIEEYDSLGSKKLRLHVF 81
PB1 cd05992
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
 263-337 9.82e-13

The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as a noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99716 [Multi-domain]  Cd Length: 81  Bit Score: 63.84  E-value: 9.82e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2192205457 263 TVKLVFGEDIRVAQLPL-NSSLLQLREVISDRFPSCR-AVLIKYRDEEGDLVTITTDEELR--WAEASAEMQGSVRLFV 337
Cdd:cd05992     2 RVKVKYGGEIRRFVVVSrSISFEDLRSKIAEKFGLDAvSFKLKYPDEDGDLVTISSDEDLEeaIEEARRSGSKKLRLFV 80
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 48-193 1.37e-10

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 64.62  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  48 LKEEGNKLFQKRDHGGALLKYEKALKLLPrnyiDVSYLrSNMAACYMqmGLSEYPRAIHECNLALEVTPLYSKALLKRAR 127
Cdd:TIGR00990 130 LKEKGNKAYRNKDFNKAIKLYSKAIECKP----DPVYY-SNRAACHN--ALGDWEKVVEDTTAALELDPDYSKALNRRAN 202

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2192205457 128 CYEALNRLDLAFRDVTTV-LNKEPKNimaAEIAERVKKELEKRGLRVNDTVIELPPEYVePPVASIA 193
Cdd:TIGR00990 203 AYDGLGKYADALLDLTAScIIDGFRN---EQSAQAVERLLKKFAESKAKEILETKPENL-PSVTFVG 265
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
46-152 2.38e-09

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 58.00  E-value: 2.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  46 QELKEEGNKLFQKRDHGGALLKYEKALKLLPRNYIdvsyLRSNMAACYMQMGlsEYPRAIHECNLALEVTPLYSKALLKR 125
Cdd:COG4785    74 QLYYERGVAYDSLGDYDLAIADFDQALELDPDLAE----AYNNRGLAYLLLG--DYDAALEDFDRALELDPDYAYAYLNR 147

                          90       100
                  ....*....|....*....|....*..
gi 2192205457 126 ARCYEALNRLDLAFRDVTTVLNKEPKN 152
Cdd:COG4785   148 GIALYYLGRYELAIADLEKALELDPND 174
 
Name Accession Description Interval E-value
PB1 pfam00564
PB1 domain;
263-340 1.73e-16

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 74.64  E-value: 1.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457 263 TVKLVFGEDI-RVAQLPLNSSLLQLREVISDRFPSCRA-VLIKYRDEEGDLVTITTDEELR--WAEASAEMQGSVRLFVV 338
Cdd:pfam00564   3 RLKLRYGGGIrRFLSVSRGISFEELRALVEQRFGLDDVdFKLKYPDEDGDLVSLTSDEDLEeaLEEARSLGSKSLRLHVF 82


                  ..
gi 2192205457 339 EV 340
Cdd:pfam00564  83 PT 84
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 263-338 3.20e-16

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.


Pssm-ID: 214770  Cd Length: 81  Bit Score: 73.78  E-value: 3.20e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2192205457  263 TVKLVFGEDIRVAQLPLNSSLLQLREVISDRFP-SCRAVLIKYRDEEGDLVTITTDEELR--WAEASAEMQGSVRLFVV 338
Cdd:smart00666   3 DVKLRYGGETRRLSVPRDISFEDLRSKVAKRFGlDNQSFTLKYQDEDGDLVSLTSDEDLEeaIEEYDSLGSKKLRLHVF 81
PB1 cd05992
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
 263-337 9.82e-13

The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as a noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99716 [Multi-domain]  Cd Length: 81  Bit Score: 63.84  E-value: 9.82e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2192205457 263 TVKLVFGEDIRVAQLPL-NSSLLQLREVISDRFPSCR-AVLIKYRDEEGDLVTITTDEELR--WAEASAEMQGSVRLFV 337
Cdd:cd05992     2 RVKVKYGGEIRRFVVVSrSISFEDLRSKIAEKFGLDAvSFKLKYPDEDGDLVTISSDEDLEeaIEEARRSGSKKLRLFV 80
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 48-193 1.37e-10

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 64.62  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  48 LKEEGNKLFQKRDHGGALLKYEKALKLLPrnyiDVSYLrSNMAACYMqmGLSEYPRAIHECNLALEVTPLYSKALLKRAR 127
Cdd:TIGR00990 130 LKEKGNKAYRNKDFNKAIKLYSKAIECKP----DPVYY-SNRAACHN--ALGDWEKVVEDTTAALELDPDYSKALNRRAN 202

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2192205457 128 CYEALNRLDLAFRDVTTV-LNKEPKNimaAEIAERVKKELEKRGLRVNDTVIELPPEYVePPVASIA 193
Cdd:TIGR00990 203 AYDGLGKYADALLDLTAScIIDGFRN---EQSAQAVERLLKKFAESKAKEILETKPENL-PSVTFVG 265
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
46-152 2.38e-09

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 58.00  E-value: 2.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  46 QELKEEGNKLFQKRDHGGALLKYEKALKLLPRNYIdvsyLRSNMAACYMQMGlsEYPRAIHECNLALEVTPLYSKALLKR 125
Cdd:COG4785    74 QLYYERGVAYDSLGDYDLAIADFDQALELDPDLAE----AYNNRGLAYLLLG--DYDAALEDFDRALELDPDYAYAYLNR 147

                          90       100
                  ....*....|....*....|....*..
gi 2192205457 126 ARCYEALNRLDLAFRDVTTVLNKEPKN 152
Cdd:COG4785   148 GIALYYLGRYELAIADLEKALELDPND 174
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
52-155 6.96e-09

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 57.32  E-value: 6.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  52 GNKLFQKRDHGGALLKYEKALKLLPRNYidvsYLRSNMAACYMQMGlsEYPRAIHECNLALEVTPLYSKALLKRARCYEA 131
Cdd:COG0457    15 GLAYRRLGRYEEAIEDYEKALELDPDDA----EALYNLGLAYLRLG--RYEEALADYEQALELDPDDAEALNNLGLALQA 88

                          90       100
                  ....*....|....*....|....
gi 2192205457 132 LNRLDLAFRDVTTVLNKEPKNIMA 155
Cdd:COG0457    89 LGRYEEALEDYDKALELDPDDAEA 112
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 52-164 1.64e-08

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 53.47  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  52 GNKLFQKRDHGGALLKYEKALKLLPRNyidvSYLRSNMAACYMQMGlsEYPRAIHECNLALEVTPLYSKALLKRARCYEA 131
Cdd:COG4235    24 GRAYLRLGRYDEALAAYEKALRLDPDN----ADALLDLAEALLAAG--DTEEAEELLERALALDPDNPEALYLLGLAAFQ 97

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2192205457 132 LNRLDLAFRDVTTVLNKEPKNIMAAEIAERVKK 164
Cdd:COG4235    98 QGDYAEAIAAWQKLLALLPADAPARLLEASIAE 130
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 55-150 1.24e-07

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 51.88  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  55 LFQKRDHGGALLKYEKALKLLPRNyidvSYLRSNMAACYMQMGlsEYPRAIHECNLALEVTPLYSKALLKRARCYEALNR 134
Cdd:COG5010    64 YNKLGDFEESLALLEQALQLDPNN----PELYYNLALLYSRSG--DKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQ 137

                          90
                  ....*....|....*.
gi 2192205457 135 LDLAFRDVTTVLNKEP 150
Cdd:COG5010   138 DDEAKAALQRALGTSP 153
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 52-156 1.40e-07

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 55.00  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  52 GNKLFQKRDHGGALLKYEKALKLLPRNyidvSYLRSNMAACYMQMGlsEYPRAIHECNLALEVTPLYSKALLKRARCYEA 131
Cdd:COG3914   119 GNLLLALGRLEEALAALRRALALNPDF----AEAYLNLGEALRRLG--RLEEAIAALRRALELDPDNAEALNNLGNALQD 192

                          90       100
                  ....*....|....*....|....*
gi 2192205457 132 LNRLDLAFRDVTTVLNKEPKNIMAA 156
Cdd:COG3914   193 LGRLEEAIAAYRRALELDPDNADAH 217
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
52-155 1.82e-07

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 52.70  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  52 GNKLFQKRDHGGALLKYEKALKLLPRNYidvsYLRSNMAACYMQMGlsEYPRAIHECNLALEVTPLYSKALLKRARCYEA 131
Cdd:COG0457    49 GLAYLRLGRYEEALADYEQALELDPDDA----EALNNLGLALQALG--RYEEALEDYDKALELDPDDAEALYNLGLALLE 122

                          90       100
                  ....*....|....*....|....
gi 2192205457 132 LNRLDLAFRDVTTVLNKEPKNIMA 155
Cdd:COG0457   123 LGRYDEAIEAYERALELDPDDADA 146
PB1_p62 cd06402
The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) ...
 270-340 4.08e-07

The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) involved in cell signaling, receptor internalization, and protein turnover. The PB1 domain is a modular domain mediating specific protein-protein interaction which play roles in many critical cell processes. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99723  Cd Length: 87  Bit Score: 48.10  E-value: 4.08e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2192205457 270 EDIR--VAQLPLNSSLLQLREVISDRFPSCR--AVLIKYRDEEGDLVTITTDEELrwAEASAEMQGSV-RLFVVEV 340
Cdd:cd06402    14 AEIRrfAIDEDVSTSYEYLVEKVAAVFPSLRgkNFQLFWKDEEGDLVAFSSDEEL--VMALGSLNDDTfRIYIKEK 87
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 54-164 3.06e-06

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 46.52  E-value: 3.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  54 KLFQKRDHGGALLKYEKALKLLPRN-YIDVSYLRsnMAACYMQMGlsEYPRAIHECNLALEVTP---LYSKALLKRARCY 129
Cdd:COG1729     2 ALLKAGDYDEAIAAFKAFLKRYPNSpLAPDALYW--LGEAYYALG--DYDEAAEAFEKLLKRYPdspKAPDALLKLGLSY 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2192205457 130 EALNRLDLAFRDVTTVLNKEPKNIMAAEIAERVKK 164
Cdd:COG1729    78 LELGDYDKARATLEELIKKYPDSEAAKEARARLAR 112
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
55-151 3.42e-06

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 45.93  E-value: 3.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  55 LFQKRDHGGALLKYEKALKLLPRNyidvSYLRSNMAACYMQMGlsEYPRAIhECNLALEVTPLYSKALLKRARCYEALNR 134
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALELDPDN----ADALNNLGLLLLEQG--RYDEAI-ALEKALKLDPNNAEALLNLAELLLELGD 74

                          90
                  ....*....|....*..
gi 2192205457 135 LDLAFRDVTTVLNKEPK 151
Cdd:COG3063    75 YDEALAYLERALELDPS 91
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 55-152 3.55e-06

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 47.11  E-value: 3.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  55 LFQKRDHGGALLKYEKALKLLPRNyidvSYLRSNMAACYMQMGlsEYPRAIHECNLALEVTPLYSKALLKRARCYEALNR 134
Cdd:COG4783    48 LLQLGDLDEAIVLLHEALELDPDE----PEARLNLGLALLKAG--DYDEALALLEKALKLDPEHPEAYLRLARAYRALGR 121

                          90
                  ....*....|....*...
gi 2192205457 135 LDLAFRDVTTVLNKEPKN 152
Cdd:COG4783   122 PDEAIAALEKALELDPDD 139
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
52-175 4.02e-06

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 48.85  E-value: 4.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  52 GNKLFQKRDHGGALLKYEKALKLLPRNYidvsYLRSNMAACYMQMGlsEYPRAIHECNLALEVTPLYSKALLKRARCYEA 131
Cdd:COG0457    83 GLALQALGRYEEALEDYDKALELDPDDA----EALYNLGLALLELG--RYDEAIEAYERALELDPDDADALYNLGIALEK 156

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2192205457 132 LNRLDLAFRDVTTVLNKEPKNIMAAEIAERVKKELEKRGLRVND 175
Cdd:COG0457   157 LGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALL 200
PB1_TFG cd06401
The PB1 domain found in TFG protein, an oncogenic gene product and fusion partner to nerve ...
 264-337 4.60e-06

The PB1 domain found in TFG protein, an oncogenic gene product and fusion partner to nerve growth factor tyrosine kinase receptor TrkA and to the tyrosine kinase ALK. The PB1 domain is a modular domain mediating specific protein-protein interaction in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. The PB1 domains of TFG represent a type I/II PB1 domain. The physiological function of TFG remains unknown.


Pssm-ID: 99722  Cd Length: 81  Bit Score: 45.20  E-value: 4.60e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2192205457 264 VKLVFGEDIRVA-----QLPLNSSLLQLREVISDRFPSCRAVLIKYRDEEGDLVTITTDEELRWAEASAEMQgSVRLFV 337
Cdd:cd06401     3 LKAQLGDDIRRIpihneDITYDELLLMMQRVFRGKLGSSDDVLIKYKDEDGDLITIFDSSDLSFAIQCSRIL-KLTLFV 80
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 52-165 4.65e-06

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 48.96  E-value: 4.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  52 GNKLFQKRDHGGALLKYEKALKLLPrNYIDVSYLrsnMAACYMQMGlsEYPRAIHECNLALEVTPLYSKALLKRARCYEA 131
Cdd:COG2956   151 AELYLEQGDYDEAIEALEKALKLDP-DCARALLL---LAELYLEQG--DYEEAIAALERALEQDPDYLPALPRLAELYEK 224

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2192205457 132 LNRLDLAFRDVTTVLNKEPKNIMAAEIAERVKKE 165
Cdd:COG2956   225 LGDPEEALELLRKALELDPSDDLLLALADLLERK 258
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 50-168 6.26e-06

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 48.57  E-value: 6.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  50 EEGNKLFQKRDHGGALLKYEKALKLLPRNYidvsYLRSNMAACYMQMGlsEYPRAIHECNLALEVTPLYSKALLKRARCY 129
Cdd:COG2956    13 FKGLNYLLNGQPDKAIDLLEEALELDPETV----EAHLALGNLYRRRG--EYDRAIRIHQKLLERDPDRAEALLELAQDY 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2192205457 130 EALNRLDLAFRDVTTVLNKEPKNIMA----AEIAERvKKELEK 168
Cdd:COG2956    87 LKAGLLDRAEELLEKLLELDPDDAEAlrllAEIYEQ-EGDWEK 128
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 55-168 3.95e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 45.88  E-value: 3.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  55 LFQKRDHGGALLKYEKALKLLPRNyidvSYLRSNMAACYMQMGlsEYPRAIHECNLALEVTPLYSKALLKRARCYEALNR 134
Cdd:COG2956   120 YEQEGDWEKAIEVLERLLKLGPEN----AHAYCELAELYLEQG--DYDEAIEALEKALKLDPDCARALLLLAELYLEQGD 193

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2192205457 135 LDLAFRDVTTVLNKEPKNIMAAEIAERVKKELEK 168
Cdd:COG2956   194 YEEAIAALERALEQDPDYLPALPRLAELYEKLGD 227
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 43-170 7.66e-05

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 43.26  E-value: 7.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  43 GMSQELKEEGNKLFQKRDHGGALLKYEKALKLLPRNyidvSYLRSNMAACYMQMGlsEYPRAIHECNLALEVTPLYSKAL 122
Cdd:COG4783     2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDN----PEAFALLGEILLQLG--DLDEAIVLLHEALELDPDEPEAR 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2192205457 123 LKRARCYEALNRLDLAFRDVTTVLNKEPKNIMAAEIAERVKKELEKRG 170
Cdd:COG4783    76 LNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPD 123
PB1_NLP cd06407
A PB1 domain is present in NIN like proteins (NLP), a key enzyme in a process of establishment ...
 263-320 8.94e-05

A PB1 domain is present in NIN like proteins (NLP), a key enzyme in a process of establishment of symbiosis betweeen legumes and nitrogen fixing bacteria (Rhizobium). The PB1 domain is a modular domain mediating specific protein-protein interaction which play a role in many critical cell processes like osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99728  Cd Length: 82  Bit Score: 41.54  E-value: 8.94e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457 263 TVKLVFGEDIRVAQLPLNSSLLQLREVISDRF--PSCRAVLIKYRDEEGDLVTITTDEEL 320
Cdd:cd06407     2 RVKATYGEEKIRFRLPPSWGFTELKQEIAKRFklDDMSAFDLKYLDDDEEWVLLTCDADL 61
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 54-168 1.25e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 44.33  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  54 KLFQKR-DHGGALLKYEKALKLLPRNYidvsYLRSNMAACYMQMGLseYPRAIHECNLALEVTPLYSKALLKRARCYEAL 132
Cdd:COG2956    50 NLYRRRgEYDRAIRIHQKLLERDPDRA----EALLELAQDYLKAGL--LDRAEELLEKLLELDPDDAEALRLLAEIYEQE 123

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2192205457 133 NRLDLAFRDVTTVLNKEPKNIMA----AEIAERvKKELEK 168
Cdd:COG2956   124 GDWEKAIEVLERLLKLGPENAHAycelAELYLE-QGDYDE 162
PB1_aPKC cd06404
PB1 domain is an essential modular domain of the atypical protein kinase C (aPKC) which in ...
 263-337 4.67e-04

PB1 domain is an essential modular domain of the atypical protein kinase C (aPKC) which in complex with Par6 and Par3 proteins is crucial for establishment of apical-basal polarity of animal cells. PB1 domain is a modular domain mediating specific protein-protein interaction which play roles in many critical cell processes. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. The aPKC protein contains a type I/II PB1 domain.


Pssm-ID: 99725  Cd Length: 83  Bit Score: 39.64  E-value: 4.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457 263 TVKLVFGEDIRVAQLPLNSSLLQLREVISD--RFPSCRAVLIKYRDEEGDLVTITTDEEL----RWAEASAEMQGSVRLF 336
Cdd:cd06404     2 RVKAAYNGDIMITSIDPSISLEELCNEVRDmcRFHNDQPFTLKWIDEEGDPCTISSQMELeeafRLYELNKDSELNIHVF 81


                  .
gi 2192205457 337 V 337
Cdd:cd06404    82 P 82
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
56-155 2.42e-03

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 40.28  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457  56 FQKRDHGGALLKYEKALKLLPRNYIDVSYLRSNMAACYMQMG-----LSEYPRAIHECNLALEVTPLYSKALLKRARCYE 130
Cdd:COG4785    39 IALADLALALAAAALAAAALAAERIDRALALPDLAQLYYERGvaydsLGDYDLAIADFDQALELDPDLAEAYNNRGLAYL 118

                          90       100
                  ....*....|....*....|....*
gi 2192205457 131 ALNRLDLAFRDVTTVLNKEPKNIMA 155
Cdd:COG4785   119 LLGDYDAALEDFDRALELDPDYAYA 143
PB1_Joka2 cd06398
The PB1 domain is present in the Nicotiana plumbaginifolia Joka2 protein which interacts with ...
 264-341 3.70e-03

The PB1 domain is present in the Nicotiana plumbaginifolia Joka2 protein which interacts with sulfur stress inducible UP9 protein. The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99720  Cd Length: 91  Bit Score: 37.00  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2192205457 264 VKLVFGEDIR-----VAQLPLNSSLLQLREVISDRFP--SCRAVLIKYRDEEGDLVTITTDEELrwAEASAEMQGSVRLF 336
Cdd:cd06398     3 VKVKYGGTLRrftfpVAENQLDLNMDGLREKVEELFSlsPDADLSLTYTDEDGDVVTLVDDNDL--TDAIQYFCSGSRLN 80


                  ....*
gi 2192205457 337 VVEVN 341
Cdd:cd06398    81 PLRID 85
 
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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