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Conserved domains on  [gi|578806985|ref|XP_006713535|]
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protein TFG isoform X1 [Homo sapiens]

Protein Classification

PB1_TFG domain-containing protein( domain architecture ID 10157344)

PB1_TFG domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PB1_TFG cd06401
The PB1 domain found in TFG protein, an oncogenic gene product and fusion partner to nerve ...
 11-91 2.39e-49

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: 161.53  E-value: 2.39e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806985  11 LIIKAQLGEDIRRIPIHNEDITYDELVLMMQRVFRGKLLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFV 90
Cdd:cd06401    1 LILKAQLGDDIRRIPIHNEDITYDELLLMMQRVFRGKLGSSDDVLIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFV 80


                 .
gi 578806985  91 N 91
Cdd:cd06401   81 N 81
dnaA super family cl42516
chromosomal replication initiator protein DnaA;
325-400 9.84e-03

chromosomal replication initiator protein DnaA;


The actual alignment was detected with superfamily member PRK14086:

Pssm-ID: 455861 [Multi-domain]  Cd Length: 617  Bit Score: 38.27  E-value: 9.84e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806985 325 PAQTYTAQTSQPTNYTVAPASQPGMAPSQPGAY---QPRPGFTslPGSTMTPPPSGPNPYARNRPPFGQGYTQPGPGYR 400
Cdd:PRK14086 133 LPRQDQLPTARPAYPAYQQRPEPGAWPRAADDYgwqQQRLGFP--PRAPYASPASYAPEQERDREPYDAGRPEYDQRRR 209
 
Name Accession Description Interval E-value
PB1_TFG cd06401
The PB1 domain found in TFG protein, an oncogenic gene product and fusion partner to nerve ...
 11-91 2.39e-49

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: 161.53  E-value: 2.39e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806985  11 LIIKAQLGEDIRRIPIHNEDITYDELVLMMQRVFRGKLLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFV 90
Cdd:cd06401    1 LILKAQLGDDIRRIPIHNEDITYDELLLMMQRVFRGKLGSSDDVLIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFV 80


                 .
gi 578806985  91 N 91
Cdd:cd06401   81 N 81
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 13-89 5.92e-18

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: 78.01  E-value: 5.92e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806985    13 IKAQLGEDIRRIPIHnEDITYDELVLMMQRVFRgklLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQ-----CSRILKLT 87
Cdd:smart00666   4 VKLRYGGETRRLSVP-RDISFEDLRSKVAKRFG---LDNQSFTLKYQDEDGDLVSLTSDEDLEEAIEeydslGSKKLRLH 79


                   ..
gi 578806985    88 LF 89
Cdd:smart00666  80 VF 81
PB1 pfam00564
PB1 domain;
13-90 1.64e-10

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 56.92  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806985   13 IKAQLGEDIRRIPIHNEDITYDELVLMMQRVFrgKLLSNDeVTIKYKDEDGDLITIFDSSDLSFAIQ-----CSRILKLT 87
Cdd:pfam00564   4 LKLRYGGGIRRFLSVSRGISFEELRALVEQRF--GLDDVD-FKLKYPDEDGDLVSLTSDEDLEEALEearslGSKSLRLH 80


                  ...
gi 578806985   88 LFV 90
Cdd:pfam00564  81 VFP 83
dnaA PRK14086
chromosomal replication initiator protein DnaA;
325-400 9.84e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 38.27  E-value: 9.84e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806985 325 PAQTYTAQTSQPTNYTVAPASQPGMAPSQPGAY---QPRPGFTslPGSTMTPPPSGPNPYARNRPPFGQGYTQPGPGYR 400
Cdd:PRK14086 133 LPRQDQLPTARPAYPAYQQRPEPGAWPRAADDYgwqQQRLGFP--PRAPYASPASYAPEQERDREPYDAGRPEYDQRRR 209
 
Name Accession Description Interval E-value
PB1_TFG cd06401
The PB1 domain found in TFG protein, an oncogenic gene product and fusion partner to nerve ...
 11-91 2.39e-49

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: 161.53  E-value: 2.39e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806985  11 LIIKAQLGEDIRRIPIHNEDITYDELVLMMQRVFRGKLLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFV 90
Cdd:cd06401    1 LILKAQLGDDIRRIPIHNEDITYDELLLMMQRVFRGKLGSSDDVLIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFV 80


                 .
gi 578806985  91 N 91
Cdd:cd06401   81 N 81
PB1 cd05992
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
 11-90 1.60e-19

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: 82.33  E-value: 1.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806985  11 LIIKAQLGEDIRRIPIHNEDITYDELVLMMQRVFRgklLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQCSRIL---KLT 87
Cdd:cd05992    1 VRVKVKYGGEIRRFVVVSRSISFEDLRSKIAEKFG---LDAVSFKLKYPDEDGDLVTISSDEDLEEAIEEARRSgskKLR 77


                 ...
gi 578806985  88 LFV 90
Cdd:cd05992   78 LFV 80
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 13-89 5.92e-18

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: 78.01  E-value: 5.92e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806985    13 IKAQLGEDIRRIPIHnEDITYDELVLMMQRVFRgklLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQ-----CSRILKLT 87
Cdd:smart00666   4 VKLRYGGETRRLSVP-RDISFEDLRSKVAKRFG---LDNQSFTLKYQDEDGDLVSLTSDEDLEEAIEeydslGSKKLRLH 79


                   ..
gi 578806985    88 LF 89
Cdd:smart00666  80 VF 81
PB1 pfam00564
PB1 domain;
13-90 1.64e-10

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 56.92  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806985   13 IKAQLGEDIRRIPIHNEDITYDELVLMMQRVFrgKLLSNDeVTIKYKDEDGDLITIFDSSDLSFAIQ-----CSRILKLT 87
Cdd:pfam00564   4 LKLRYGGGIRRFLSVSRGISFEELRALVEQRF--GLDDVD-FKLKYPDEDGDLVSLTSDEDLEEALEearslGSKSLRLH 80


                  ...
gi 578806985   88 LFV 90
Cdd:pfam00564  81 VFP 83
PB1_Joka2 cd06398
The PB1 domain is present in the Nicotiana plumbaginifolia Joka2 protein which interacts with ...
 11-91 5.17e-06

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: 44.32  E-value: 5.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806985  11 LIIKAQLGEDIRRI--PIHNE--DITYDELVLMMQRVFrgKLLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQ--CSRIL 84
Cdd:cd06398    1 LVVKVKYGGTLRRFtfPVAENqlDLNMDGLREKVEELF--SLSPDADLSLTYTDEDGDVVTLVDDNDLTDAIQyfCSGSR 78


                 ....*..
gi 578806985  85 KLTLFVN 91
Cdd:cd06398   79 LNPLRID 85
PB1_p62 cd06402
The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) ...
 11-81 2.01e-05

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: 42.71  E-value: 2.01e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578806985  11 LIIKAQL-----GEDIRRIPIhNEDIT--YDELVLMMQRVFRGklLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQCS 81
Cdd:cd06402    1 LTVKAYLlgkdaNAEIRRFAI-DEDVStsYEYLVEKVAAVFPS--LRGKNFQLFWKDEEGDLVAFSSDEELVMALGSL 75
PB1_Par6 cd06403
The PB1 domain is an essential part of Par6 protein which in complex with Par3 and aPKC ...
 13-90 2.06e-04

The PB1 domain is an essential part of Par6 protein which in complex with Par3 and aPKC proteins is crucial for establishment of apical-basal polarity of animal cells. The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role 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 Par6 protein contains a type II PB1 domain.


Pssm-ID: 99724  Cd Length: 80  Bit Score: 39.61  E-value: 2.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806985  13 IKAQLGEDIRRIPIH-NEDITYDELVLMMQRVFRgklLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQCSRILkLTLFV 90
Cdd:cd06403    3 VKSKFDAEFRRFSLDrNKPGKFEDFYKLLEHLHH---IPNVDFLIGYTDPHGDLLPINNDDNFLKALSSANPL-LRIFI 77
PB1_P40 cd06399
The PB1 domain is essential part of the p40 adaptor protein which plays an important role in ...
 19-82 1.23e-03

The PB1 domain is essential part of the p40 adaptor protein which plays an important role in activating phagocyte NADPH oxidase during phagocytosis. The PB1 domain is a modular domain mediating specific protein-protein interaction 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. The PB1 domain of p40 represents a type I PB1 domain which interacts with the PB1 domain of oxidase activator p67 which belong to type II PB1 domain. 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: 99721  Cd Length: 92  Bit Score: 37.93  E-value: 1.23e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578806985  19 EDIRRIPIhneditYDELVLMMQRVFRgkllsNDEVTIKYKDEDGDLITIFDSSDLSFAIQCSR 82
Cdd:cd06399   22 EDLSSTPL------LKDLLELTRREFQ-----REDIALNYRDAEGDLIRLLSDEDVALMVRQSR 74
PB1_NoxR cd06408
The PB1 domain is present in the Epichloe festucae NoxR protein (NADPH oxidase regulator), a ...
 10-82 1.57e-03

The PB1 domain is present in the Epichloe festucae NoxR protein (NADPH oxidase regulator), a key regulator of NADPH oxidase isoform, NoxA. NoxA is essential for growth control of the fungal endophyte in plant tissue in the process of symbiotic interaction between a fungi and its plant host. The Epichloe festucae p67(phox)-like regulator, NoxR, dispensable in culture but essential in plants for the symbiotic interaction. Plants infected with a noxR deletion mutant show severe stunting and premature senescence, whereas hyphae in the meristematic tissues show increased branching leading to increased fungal colonization of pseudostem and leaf blade tissue. The PB1 domain is a modular domain mediating specific protein-protein interactions which a play 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 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: 99729  Cd Length: 86  Bit Score: 37.43  E-value: 1.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806985  10 KLIIKAQLGEDIRRIPIhNEDITYDELvlmMQRVfRGKLLSNDEVTIKYKDeDGDLITIFDSSDLSFAIQCSR 82
Cdd:cd06408    2 KIRVKVHAQDDTRYIMI-GPDTGFADF---EDKI-RDKFGFKRRLKIKMKD-DGDMITMGDQDDLDMAIDTAR 68
PB1_MUG70 cd06409
The MUG70 protein is a product of the meiotically up-regulated gene 70 which has a role in ...
 34-90 8.58e-03

The MUG70 protein is a product of the meiotically up-regulated gene 70 which has a role in meiosis and harbors a PB1 domain. 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 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domains depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic amino acid 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: 99730  Cd Length: 86  Bit Score: 35.37  E-value: 8.58e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806985  34 DELV-LMMQRVFRGKLLSNDeVTIKYKDEDGDLITIFDSSDLSFAIQCSRIL---KLTLFV 90
Cdd:cd06409   24 EELRtLISQRLGDDDFETHL-YALSYVDDEGDIVLITSDSDLVAAVLVARSAglkKLDLHL 83
PB1_aPKC cd06404
PB1 domain is an essential modular domain of the atypical protein kinase C (aPKC) which in ...
 13-80 9.29e-03

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: 35.01  E-value: 9.29e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806985  13 IKAQLGEDIRRIPIhNEDITYDELVLMMQRVFRgklLSNDEV-TIKYKDEDGDLITIFDSSDLSFAIQC 80
Cdd:cd06404    3 VKAAYNGDIMITSI-DPSISLEELCNEVRDMCR---FHNDQPfTLKWIDEEGDPCTISSQMELEEAFRL 67
dnaA PRK14086
chromosomal replication initiator protein DnaA;
325-400 9.84e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 38.27  E-value: 9.84e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806985 325 PAQTYTAQTSQPTNYTVAPASQPGMAPSQPGAY---QPRPGFTslPGSTMTPPPSGPNPYARNRPPFGQGYTQPGPGYR 400
Cdd:PRK14086 133 LPRQDQLPTARPAYPAYQQRPEPGAWPRAADDYgwqQQRLGFP--PRAPYASPASYAPEQERDREPYDAGRPEYDQRRR 209
 
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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