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Conserved domains on  [gi|18407574|ref|NP_564794|]
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Octicosapeptide/Phox/Bem1p (PB1) domain-containing protein / tetratricopeptide repeat (TPR)-containing protein [Arabidopsis thaliana]

Protein Classification

PB1 domain-containing protein( domain architecture ID 10456513)

PB1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PB1 pfam00564
PB1 domain;
290-382 1.61e-15

PB1 domain;


:

Pssm-ID: 395447  Cd Length: 84  Bit Score: 71.94  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574   290 WRPLKFVYDHDI-RLGQMPVNCRFKELREIVSSRFPSSKA-VLIKYKDNDGDLVTITSTAELKLAESAADCILTKepdtd 367
Cdd:pfam00564   1 TVRLKLRYGGGIrRFLSVSRGISFEELRALVEQRFGLDDVdFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSK----- 75

                          90
                  ....*....|....*
gi 18407574   368 ksdsvgMLRLHVVDV 382
Cdd:pfam00564  76 ------SLRLHVFPT 84
3a0801s09 super family cl36792
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 37-151 8.99e-13

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: 71.55  E-value: 8.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574    37 NGGVDFDASIFL------KRAHELKEEGNKKFQARDYVGALEQYENGIKLIPKShpdraVFHSNRAACLMQMKpiDYESV 110
Cdd:TIGR00990 107 LPEIDESSVANLseeerkKYAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKPDP-----VYYSNRAACHNALG--DWEKV 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 18407574   111 ISECSMALKSQPGFTRALLRRARAFEAVGKFDLAVQDVNVL 151
Cdd:TIGR00990 180 VEDTTAALELDPDYSKALNRRANAYDGLGKYADALLDLTAS 220
TPR super family cl33886
Tetratricopeptide (TPR) repeat [General function prediction only];
464-638 6.67e-05

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


The actual alignment was detected with superfamily member COG0457:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 45.00  E-value: 6.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574 464 IDPDAHIDLHELGmelcsEALEETVTSEKAQPLFDKASAKFQEVAAlAFFNWGNVHmcAARKRIPLDESAGKEVVAAQLQ 543
Cdd:COG0457   3 LDPDDAEAYNNLG-----LAYRRLGRYEEAIEDYEKALELDPDDAE-ALYNLGLAY--LRLGRYEEALADYEQALELDPD 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574 544 TAYEWV--------KERYTLAKEKYEQALSIKPDFYEGLLALG-----QQQFEMAKLHWSYLLAqkIDISGWDPSETLNL 610
Cdd:COG0457  75 DAEALNnlglalqaLGRYEEALEDYDKALELDPDDAEALYNLGlalleLGRYDEAIEAYERALE--LDPDDADALYNLGI 152

                       170       180
                ....*....|....*....|....*...
gi 18407574 611 FDSAEAKMKDATEMWEKLEEQRMDDLKN 638
Cdd:COG0457 153 ALEKLGRYEEALELLEKLEAAALAALLA 180
 
Name Accession Description Interval E-value
PB1 pfam00564
PB1 domain;
290-382 1.61e-15

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 71.94  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574   290 WRPLKFVYDHDI-RLGQMPVNCRFKELREIVSSRFPSSKA-VLIKYKDNDGDLVTITSTAELKLAESAADCILTKepdtd 367
Cdd:pfam00564   1 TVRLKLRYGGGIrRFLSVSRGISFEELRALVEQRFGLDDVdFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSK----- 75

                          90
                  ....*....|....*
gi 18407574   368 ksdsvgMLRLHVVDV 382
Cdd:pfam00564  76 ------SLRLHVFPT 84
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 293-380 4.01e-15

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: 70.69  E-value: 4.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574    293 LKFVYDHDIRLGQMPVNCRFKELREIVSSRFPSSKA-VLIKYKDNDGDLVTITSTAELKLAESAADCILTKEpdtdksds 371
Cdd:smart00666   4 VKLRYGGETRRLSVPRDISFEDLRSKVAKRFGLDNQsFTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKK-------- 75


                   ....*....
gi 18407574    372 vgmLRLHVV 380
Cdd:smart00666  76 ---LRLHVF 81
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 37-151 8.99e-13

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: 71.55  E-value: 8.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574    37 NGGVDFDASIFL------KRAHELKEEGNKKFQARDYVGALEQYENGIKLIPKShpdraVFHSNRAACLMQMKpiDYESV 110
Cdd:TIGR00990 107 LPEIDESSVANLseeerkKYAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKPDP-----VYYSNRAACHNALG--DWEKV 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 18407574   111 ISECSMALKSQPGFTRALLRRARAFEAVGKFDLAVQDVNVL 151
Cdd:TIGR00990 180 VEDTTAALELDPDYSKALNRRANAYDGLGKYADALLDLTAS 220
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
49-162 4.10e-11

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 63.40  E-value: 4.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574  49 KRAHELKEEGNKKFQARDYVGALEQYENGIKLipksHPDRAVFHSNRAACLMQMKpiDYESVISECSMALKSQPGFTRAL 128
Cdd:COG4785  71 DLAQLYYERGVAYDSLGDYDLAIADFDQALEL----DPDLAEAYNNRGLAYLLLG--DYDAALEDFDRALELDPDYAYAY 144

                        90       100       110
                ....*....|....*....|....*....|....
gi 18407574 129 LRRARAFEAVGKFDLAVQDVNVLLGSDPNHKDAG 162
Cdd:COG4785 145 LNRGIALYYLGRYELAIADLEKALELDPNDPERA 178
PB1 cd05992
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
 293-352 3.23e-09

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: 54.21  E-value: 3.23e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18407574 293 LKFVYDHDIRLGQMPV-NCRFKELREIVSSRFP-SSKAVLIKYKDNDGDLVTITSTAELKLA 352
Cdd:cd05992   3 VKVKYGGEIRRFVVVSrSISFEDLRSKIAEKFGlDAVSFKLKYPDEDGDLVTISSDEDLEEA 64
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
464-638 6.67e-05

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 45.00  E-value: 6.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574 464 IDPDAHIDLHELGmelcsEALEETVTSEKAQPLFDKASAKFQEVAAlAFFNWGNVHmcAARKRIPLDESAGKEVVAAQLQ 543
Cdd:COG0457   3 LDPDDAEAYNNLG-----LAYRRLGRYEEAIEDYEKALELDPDDAE-ALYNLGLAY--LRLGRYEEALADYEQALELDPD 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574 544 TAYEWV--------KERYTLAKEKYEQALSIKPDFYEGLLALG-----QQQFEMAKLHWSYLLAqkIDISGWDPSETLNL 610
Cdd:COG0457  75 DAEALNnlglalqaLGRYEEALEDYDKALELDPDDAEALYNLGlalleLGRYDEAIEAYERALE--LDPDDADALYNLGI 152

                       170       180
                ....*....|....*....|....*...
gi 18407574 611 FDSAEAKMKDATEMWEKLEEQRMDDLKN 638
Cdd:COG0457 153 ALEKLGRYEEALELLEKLEAAALAALLA 180
 
Name Accession Description Interval E-value
PB1 pfam00564
PB1 domain;
290-382 1.61e-15

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 71.94  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574   290 WRPLKFVYDHDI-RLGQMPVNCRFKELREIVSSRFPSSKA-VLIKYKDNDGDLVTITSTAELKLAESAADCILTKepdtd 367
Cdd:pfam00564   1 TVRLKLRYGGGIrRFLSVSRGISFEELRALVEQRFGLDDVdFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSK----- 75

                          90
                  ....*....|....*
gi 18407574   368 ksdsvgMLRLHVVDV 382
Cdd:pfam00564  76 ------SLRLHVFPT 84
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 293-380 4.01e-15

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: 70.69  E-value: 4.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574    293 LKFVYDHDIRLGQMPVNCRFKELREIVSSRFPSSKA-VLIKYKDNDGDLVTITSTAELKLAESAADCILTKEpdtdksds 371
Cdd:smart00666   4 VKLRYGGETRRLSVPRDISFEDLRSKVAKRFGLDNQsFTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKK-------- 75


                   ....*....
gi 18407574    372 vgmLRLHVV 380
Cdd:smart00666  76 ---LRLHVF 81
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 37-151 8.99e-13

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: 71.55  E-value: 8.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574    37 NGGVDFDASIFL------KRAHELKEEGNKKFQARDYVGALEQYENGIKLIPKShpdraVFHSNRAACLMQMKpiDYESV 110
Cdd:TIGR00990 107 LPEIDESSVANLseeerkKYAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKPDP-----VYYSNRAACHNALG--DWEKV 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 18407574   111 ISECSMALKSQPGFTRALLRRARAFEAVGKFDLAVQDVNVL 151
Cdd:TIGR00990 180 VEDTTAALELDPDYSKALNRRANAYDGLGKYADALLDLTAS 220
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
49-162 4.10e-11

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 63.40  E-value: 4.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574  49 KRAHELKEEGNKKFQARDYVGALEQYENGIKLipksHPDRAVFHSNRAACLMQMKpiDYESVISECSMALKSQPGFTRAL 128
Cdd:COG4785  71 DLAQLYYERGVAYDSLGDYDLAIADFDQALEL----DPDLAEAYNNRGLAYLLLG--DYDAALEDFDRALELDPDYAYAY 144

                        90       100       110
                ....*....|....*....|....*....|....
gi 18407574 129 LRRARAFEAVGKFDLAVQDVNVLLGSDPNHKDAG 162
Cdd:COG4785 145 LNRGIALYYLGRYELAIADLEKALELDPNDPERA 178
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
58-161 2.86e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 58.48  E-value: 2.86e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574  58 GNKKFQARDYVGALEQYENGIKLipksHPDRAVFHSNRAACLMQMKpiDYESVISECSMALKSQPGFTRALLRRARAFEA 137
Cdd:COG0457  15 GLAYRRLGRYEEAIEDYEKALEL----DPDDAEALYNLGLAYLRLG--RYEEALADYEQALELDPDDAEALNNLGLALQA 88

                        90       100
                ....*....|....*....|....
gi 18407574 138 VGKFDLAVQDVNVLLGSDPNHKDA 161
Cdd:COG0457  89 LGRYEEALEDYDKALELDPDDAEA 112
PB1 cd05992
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
 293-352 3.23e-09

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: 54.21  E-value: 3.23e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18407574 293 LKFVYDHDIRLGQMPV-NCRFKELREIVSSRFP-SSKAVLIKYKDNDGDLVTITSTAELKLA 352
Cdd:cd05992   3 VKVKYGGEIRRFVVVSrSISFEDLRSKIAEKFGlDAVSFKLKYPDEDGDLVTISSDEDLEEA 64
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
62-157 7.38e-09

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 53.64  E-value: 7.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574  62 FQARDYVGALEQYENGIKLipksHPDRAVFHSNRAACLMQMKpiDYESVIsECSMALKSQPGFTRALLRRARAFEAVGKF 141
Cdd:COG3063   3 LKLGDLEEAEEYYEKALEL----DPDNADALNNLGLLLLEQG--RYDEAI-ALEKALKLDPNNAEALLNLAELLLELGDY 75

                        90
                ....*....|....*.
gi 18407574 142 DLAVQDVNVLLGSDPN 157
Cdd:COG3063  76 DEALAYLERALELDPS 91
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 62-171 2.51e-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: 53.09  E-value: 2.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574  62 FQARDYVGALEQYENGIKLipksHPDRAVFHSNRAACLMQMKpiDYESVISECSMALKSQPGFTRALLRRARAFEAVGKF 141
Cdd:COG4235  28 LRLGRYDEALAAYEKALRL----DPDNADALLDLAEALLAAG--DTEEAEELLERALALDPDNPEALYLLGLAAFQQGDY 101

                        90       100       110
                ....*....|....*....|....*....|
gi 18407574 142 DLAVQDVNVLLGSDPNHKDAGEISKRLKTA 171
Cdd:COG4235 102 AEAIAAWQKLLALLPADAPARLLEASIAEA 131
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
41-177 5.01e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 54.63  E-value: 5.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574  41 DFDASI-FLKRAHELKEE--------GNKKFQARDYVGALEQYENGIKLipksHPDRAVFHSNRAACLMQMKpiDYESVI 111
Cdd:COG0457  23 RYEEAIeDYEKALELDPDdaealynlGLAYLRLGRYEEALADYEQALEL----DPDDAEALNNLGLALQALG--RYEEAL 96

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18407574 112 SECSMALKSQPGFTRALLRRARAFEAVGKFDLAVQDVNVLLGSDPNHKDAGEISKRLKTALGPHQD 177
Cdd:COG0457  97 EDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEE 162
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 51-161 5.79e-08

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 56.15  E-value: 5.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574  51 AHELKEEGNKKFQARDYVGALEQYENGIKLipksHPDRAVFHSNRAACLMQMKpiDYESVISECSMALKSQPGFTRALLR 130
Cdd:COG3914  78 AALLELAALLLQALGRYEEALALYRRALAL----NPDNAEALFNLGNLLLALG--RLEEALAALRRALALNPDFAEAYLN 151

                        90       100       110
                ....*....|....*....|....*....|.
gi 18407574 131 RARAFEAVGKFDLAVQDVNVLLGSDPNHKDA 161
Cdd:COG3914 152 LGEALRRLGRLEEAIAALRRALELDPDNAEA 182
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 62-156 8.91e-08

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: 52.27  E-value: 8.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574  62 FQARDYVGALEQYENGIKLipksHPDRAVFHSNRAACLMQMKpiDYESVISECSMALKSQPGFTRALLRRARAFEAVGKF 141
Cdd:COG5010  65 NKLGDFEESLALLEQALQL----DPNNPELYYNLALLYSRSG--DKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQD 138

                        90
                ....*....|....*
gi 18407574 142 DLAVQDVNVLLGSDP 156
Cdd:COG5010 139 DEAKAALQRALGTSP 153
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 62-161 2.56e-07

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: 52.81  E-value: 2.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574  62 FQARDYVGALEQYEngiKLIpKSHPDRAVFHSNRAACLMQMKpiDYESVISECSMALKSQPGFTRALLRRARAFEAVGKF 141
Cdd:COG2956 121 EQEGDWEKAIEVLE---RLL-KLGPENAHAYCELAELYLEQG--DYDEAIEALEKALKLDPDCARALLLLAELYLEQGDY 194

                        90       100
                ....*....|....*....|
gi 18407574 142 DLAVQDVNVLLGSDPNHKDA 161
Cdd:COG2956 195 EEAIAALERALEQDPDYLPA 214
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 62-158 1.09e-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: 48.65  E-value: 1.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574  62 FQARDYVGALEQYENGIKLipksHPDRAVFHSNRAACLMQMKpiDYESVISECSMALKSQPGFTRALLRRARAFEAVGKF 141
Cdd:COG4783  49 LQLGDLDEAIVLLHEALEL----DPDEPEARLNLGLALLKAG--DYDEALALLEKALKLDPEHPEAYLRLARAYRALGRP 122

                        90
                ....*....|....*..
gi 18407574 142 DLAVQDVNVLLGSDPNH 158
Cdd:COG4783 123 DEAIAALEKALELDPDD 139
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
41-149 2.78e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 49.23  E-value: 2.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574  41 DFDASI-FLKRAHELKEE--------GNKKFQARDYVGALEQYENGIKLipksHPDRAVFHSNRAACLMQMKpiDYESVI 111
Cdd:COG0457  57 RYEEALaDYEQALELDPDdaealnnlGLALQALGRYEEALEDYDKALEL----DPDDAEALYNLGLALLELG--RYDEAI 130

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 18407574 112 SECSMALKSQPGFTRALLRRARAFEAVGKFDLAVQDVN 149
Cdd:COG0457 131 EAYERALELDPDDADALYNLGIALEKLGRYEEALELLE 168
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 50-161 6.15e-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: 46.34  E-value: 6.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574  50 RAHELKEEGNKKFQARDYVGALEQYENGIKLipksHPDRAVFHSNRAACLMQMKpiDYESVISECSMALKSQPGFTRALL 129
Cdd:COG4783   3 CAEALYALAQALLLAGDYDEAEALLEKALEL----DPDNPEAFALLGEILLQLG--DLDEAIVLLHEALELDPDEPEARL 76

                        90       100       110
                ....*....|....*....|....*....|..
gi 18407574 130 RRARAFEAVGKFDLAVQDVNVLLGSDPNHKDA 161
Cdd:COG4783  77 NLGLALLKAGDYDEALALLEKALKLDPEHPEA 108
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 62-161 6.02e-05

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 46.52  E-value: 6.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574  62 FQARDYVGALEQYENGIKLipksHPDRAVFHSNRAACLMQMKpiDYESVISECSMALKSQPGFTRALLRRARAFEAVGKF 141
Cdd:COG3914 123 LALGRLEEALAALRRALAL----NPDFAEAYLNLGEALRRLG--RLEEAIAALRRALELDPDNAEALNNLGNALQDLGRL 196

                        90       100
                ....*....|....*....|
gi 18407574 142 DLAVQDVNVLLGSDPNHKDA 161
Cdd:COG3914 197 EEAIAAYRRALELDPDNADA 216
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
464-638 6.67e-05

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 45.00  E-value: 6.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574 464 IDPDAHIDLHELGmelcsEALEETVTSEKAQPLFDKASAKFQEVAAlAFFNWGNVHmcAARKRIPLDESAGKEVVAAQLQ 543
Cdd:COG0457   3 LDPDDAEAYNNLG-----LAYRRLGRYEEAIEDYEKALELDPDDAE-ALYNLGLAY--LRLGRYEEALADYEQALELDPD 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574 544 TAYEWV--------KERYTLAKEKYEQALSIKPDFYEGLLALG-----QQQFEMAKLHWSYLLAqkIDISGWDPSETLNL 610
Cdd:COG0457  75 DAEALNnlglalqaLGRYEEALEDYDKALELDPDDAEALYNLGlalleLGRYDEAIEAYERALE--LDPDDADALYNLGI 152

                       170       180
                ....*....|....*....|....*...
gi 18407574 611 FDSAEAKMKDATEMWEKLEEQRMDDLKN 638
Cdd:COG0457 153 ALEKLGRYEEALELLEKLEAAALAALLA 180
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 62-171 1.28e-04

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: 41.90  E-value: 1.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574  62 FQARDYVGALEQYENGIKLIPKS-HPDRAVFhsNRAACLMQMKpiDYESVISECSMALKSQPGFTR---ALLRRARAFEA 137
Cdd:COG1729   4 LKAGDYDEAIAAFKAFLKRYPNSpLAPDALY--WLGEAYYALG--DYDEAAEAFEKLLKRYPDSPKapdALLKLGLSYLE 79

                        90       100       110
                ....*....|....*....|....*....|....
gi 18407574 138 VGKFDLAVQDVNVLLGSDPNHKDAGEISKRLKTA 171
Cdd:COG1729  80 LGDYDKARATLEELIKKYPDSEAAKEARARLARL 113
PB1_p62 cd06402
The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) ...
 281-352 1.80e-04

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: 40.78  E-value: 1.80e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18407574 281 GKVQEKRIRwrplKFVYDHDirlgqmpVNCRFKELREIVSSRFPS--SKAVLIKYKDNDGDLVTITSTAELKLA 352
Cdd:cd06402   9 GKDANAEIR----RFAIDED-------VSTSYEYLVEKVAAVFPSlrGKNFQLFWKDEEGDLVAFSSDEELVMA 71
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 41-176 6.08e-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: 42.41  E-value: 6.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574  41 DFDASI-FLKRAHELKEE--------GNKKFQARDYVGALEQYENGIKLIPKSHpdRAVFhsNRAACLMQMKpiDYESVI 111
Cdd:COG2956 125 DWEKAIeVLERLLKLGPEnahaycelAELYLEQGDYDEAIEALEKALKLDPDCA--RALL--LLAELYLEQG--DYEEAI 198

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18407574 112 SECSMALKSQPGFTRALLRRARAFEAVGKFDLAVQDVNVLLGSDPNHKDAGEISKRLKTALGPHQ 176
Cdd:COG2956 199 AALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALADLLERKEGLEA 263
PB1_TFG cd06401
The PB1 domain found in TFG protein, an oncogenic gene product and fusion partner to nerve ...
 312-352 7.19e-04

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: 39.03  E-value: 7.19e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 18407574 312 FKELR----EIVSSRFPSSKAVLIKYKDNDGDLVTITSTAELKLA 352
Cdd:cd06401  23 YDELLlmmqRVFRGKLGSSDDVLIKYKDEDGDLITIFDSSDLSFA 67
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 56-161 1.38e-03

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: 41.25  E-value: 1.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18407574  56 EEGNKKFQARDYVGALEQYENGIKLipksHPDRAVFHSNRAACLMQMKpiDYESVISECSMALKSQPGFTRALLRRARAF 135
Cdd:COG2956  13 FKGLNYLLNGQPDKAIDLLEEALEL----DPETVEAHLALGNLYRRRG--EYDRAIRIHQKLLERDPDRAEALLELAQDY 86

                        90       100
                ....*....|....*....|....*.
gi 18407574 136 EAVGKFDLAVQDVNVLLGSDPNHKDA 161
Cdd:COG2956  87 LKAGLLDRAEELLEKLLELDPDDAEA 112
 
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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