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Conserved domains on  [gi|2477801363|gb|KAJ8233345|]
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hypothetical protein LV160_006513 [Aspergillus fumigatus]

Protein Classification

ubiquitin family protein( domain architecture ID 12119644)

ubiquitin family protein belongs to an diverse class of protein modifier and gene expression regulatory proteins that participate in a number of cellular processes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Blt1 pfam12754
Blt1 N-terminal domain; During size-dependent cell cycle transitions controlled by the ...
 48-198 8.36e-92

Blt1 N-terminal domain; During size-dependent cell cycle transitions controlled by the ubiquitous cyclin-dependent kinase Cdk1, Blt1 has been shown to co-localize with Cdr2 in the medial interphase nodes, as well as with Mid1 which was previously shown to localize to similar interphase structures. Physical interactions between Blt1-Mid1, Blt1-Cdr2 and Cdr2-Mid1 were detected, indicating that medial cortical nodes are formed by the ordered, Cdr2-dependent assembly of multiple interacting proteins during interphase. This domain show similarity to ubiquitin family proteins.


:

Pssm-ID: 372291  Cd Length: 150  Bit Score: 267.74  E-value: 8.36e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477801363  48 FVKSYLSTLDSRPIKLRSDHVFDPEQVGLRVPYTLPRLHAPHPEMPKKTKQPLAPGSSKSITVHLKSARNPALEFSLPNT 127
Cdd:pfam12754   1 FTKSFLSALDSRPVKLPADHVFDPRSYPARVPYTLPRLSDPHPPMPKKVKNAAAPGSSKSITVHLKSARNPALEITLDNV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2477801363 128 ALTTTSVQDLKDAVRERVTDaQGNKISLDKIKILYKRKPVTGKTIAEVLADEPGMLSGGKEVEFGVMIIGG 198
Cdd:pfam12754  81 PLSTTSVQDLKEAVQERVVD-QDASVPLDKIKILYKKKPVSGKTLAEVLGSEPEVLSGGKEVEFGVMIMGG 150
Blt1_C pfam17183
Get5 carboxyl domain; During size-dependent cell cycle transitions controlled by the ...
 221-271 9.18e-29

Get5 carboxyl domain; During size-dependent cell cycle transitions controlled by the ubiquitous cyclin-dependent kinase Cdk1, Blt1 has been shown to co-localize with Cdr2 in the medial interphase nodes, as well as with Mid1 which was previously shown to localize to similar interphase structures. Physical interactions between Blt1-Mid1, Blt1-Cdr2 and Cdr2-Mid1 were detected, indicating that medial cortical nodes are formed by the ordered, Cdr2-dependent assembly of multiple interacting proteins during interphase. This entry corresponds to the C-terminal dimerization domain.


:

Pssm-ID: 375036  Cd Length: 51  Bit Score: 103.58  E-value: 9.18e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2477801363 221 PPKPAVGPSGESVVATEAFWDDLQGFLEQRLKDYDEANKLRVLFKEAWRSS 271
Cdd:pfam17183   1 APKAAVGPSGEEVLATEEFWDDLEGFLEQRLKDEEEASRLRGVFRGAWESS 51
 
Name Accession Description Interval E-value
Blt1 pfam12754
Blt1 N-terminal domain; During size-dependent cell cycle transitions controlled by the ...
 48-198 8.36e-92

Blt1 N-terminal domain; During size-dependent cell cycle transitions controlled by the ubiquitous cyclin-dependent kinase Cdk1, Blt1 has been shown to co-localize with Cdr2 in the medial interphase nodes, as well as with Mid1 which was previously shown to localize to similar interphase structures. Physical interactions between Blt1-Mid1, Blt1-Cdr2 and Cdr2-Mid1 were detected, indicating that medial cortical nodes are formed by the ordered, Cdr2-dependent assembly of multiple interacting proteins during interphase. This domain show similarity to ubiquitin family proteins.


Pssm-ID: 372291  Cd Length: 150  Bit Score: 267.74  E-value: 8.36e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477801363  48 FVKSYLSTLDSRPIKLRSDHVFDPEQVGLRVPYTLPRLHAPHPEMPKKTKQPLAPGSSKSITVHLKSARNPALEFSLPNT 127
Cdd:pfam12754   1 FTKSFLSALDSRPVKLPADHVFDPRSYPARVPYTLPRLSDPHPPMPKKVKNAAAPGSSKSITVHLKSARNPALEITLDNV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2477801363 128 ALTTTSVQDLKDAVRERVTDaQGNKISLDKIKILYKRKPVTGKTIAEVLADEPGMLSGGKEVEFGVMIIGG 198
Cdd:pfam12754  81 PLSTTSVQDLKEAVQERVVD-QDASVPLDKIKILYKKKPVSGKTLAEVLGSEPEVLSGGKEVEFGVMIMGG 150
Blt1_C pfam17183
Get5 carboxyl domain; During size-dependent cell cycle transitions controlled by the ...
 221-271 9.18e-29

Get5 carboxyl domain; During size-dependent cell cycle transitions controlled by the ubiquitous cyclin-dependent kinase Cdk1, Blt1 has been shown to co-localize with Cdr2 in the medial interphase nodes, as well as with Mid1 which was previously shown to localize to similar interphase structures. Physical interactions between Blt1-Mid1, Blt1-Cdr2 and Cdr2-Mid1 were detected, indicating that medial cortical nodes are formed by the ordered, Cdr2-dependent assembly of multiple interacting proteins during interphase. This entry corresponds to the C-terminal dimerization domain.


Pssm-ID: 375036  Cd Length: 51  Bit Score: 103.58  E-value: 9.18e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2477801363 221 PPKPAVGPSGESVVATEAFWDDLQGFLEQRLKDYDEANKLRVLFKEAWRSS 271
Cdd:pfam17183   1 APKAAVGPSGEEVLATEEFWDDLEGFLEQRLKDEEEASRLRGVFRGAWESS 51
 
Name Accession Description Interval E-value
Blt1 pfam12754
Blt1 N-terminal domain; During size-dependent cell cycle transitions controlled by the ...
 48-198 8.36e-92

Blt1 N-terminal domain; During size-dependent cell cycle transitions controlled by the ubiquitous cyclin-dependent kinase Cdk1, Blt1 has been shown to co-localize with Cdr2 in the medial interphase nodes, as well as with Mid1 which was previously shown to localize to similar interphase structures. Physical interactions between Blt1-Mid1, Blt1-Cdr2 and Cdr2-Mid1 were detected, indicating that medial cortical nodes are formed by the ordered, Cdr2-dependent assembly of multiple interacting proteins during interphase. This domain show similarity to ubiquitin family proteins.


Pssm-ID: 372291  Cd Length: 150  Bit Score: 267.74  E-value: 8.36e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2477801363  48 FVKSYLSTLDSRPIKLRSDHVFDPEQVGLRVPYTLPRLHAPHPEMPKKTKQPLAPGSSKSITVHLKSARNPALEFSLPNT 127
Cdd:pfam12754   1 FTKSFLSALDSRPVKLPADHVFDPRSYPARVPYTLPRLSDPHPPMPKKVKNAAAPGSSKSITVHLKSARNPALEITLDNV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2477801363 128 ALTTTSVQDLKDAVRERVTDaQGNKISLDKIKILYKRKPVTGKTIAEVLADEPGMLSGGKEVEFGVMIIGG 198
Cdd:pfam12754  81 PLSTTSVQDLKEAVQERVVD-QDASVPLDKIKILYKKKPVSGKTLAEVLGSEPEVLSGGKEVEFGVMIMGG 150
Blt1_C pfam17183
Get5 carboxyl domain; During size-dependent cell cycle transitions controlled by the ...
 221-271 9.18e-29

Get5 carboxyl domain; During size-dependent cell cycle transitions controlled by the ubiquitous cyclin-dependent kinase Cdk1, Blt1 has been shown to co-localize with Cdr2 in the medial interphase nodes, as well as with Mid1 which was previously shown to localize to similar interphase structures. Physical interactions between Blt1-Mid1, Blt1-Cdr2 and Cdr2-Mid1 were detected, indicating that medial cortical nodes are formed by the ordered, Cdr2-dependent assembly of multiple interacting proteins during interphase. This entry corresponds to the C-terminal dimerization domain.


Pssm-ID: 375036  Cd Length: 51  Bit Score: 103.58  E-value: 9.18e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2477801363 221 PPKPAVGPSGESVVATEAFWDDLQGFLEQRLKDYDEANKLRVLFKEAWRSS 271
Cdd:pfam17183   1 APKAAVGPSGEEVLATEEFWDDLEGFLEQRLKDEEEASRLRGVFRGAWESS 51
 
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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