NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|295443057|ref|NP_594557|]
View 

translin [Schizosaccharomyces pombe]

Protein Classification

translin( domain architecture ID 10201870)

translin is a DNA-binding protein that specifically recognizes consensus sequences at the breakpoint junctions in chromosomal translocations, mostly involving immunoglobulin (Ig)/T-cell receptor gene segments

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Translin cd14819
Translin, also known as TB-RBP (testis brain RNA-binding protein); Translin (also known as ...
9-218 1.61e-80

Translin, also known as TB-RBP (testis brain RNA-binding protein); Translin (also known as TB-RBP for Testis Brain RNA-binding protein, a mouse ortholog), is a paralog of its binding partner protein TRAX (translin-associated factor-X) and together they form oligomeric complexes known as C3PO proteins (for component 3 promoter of RNA-induced silencing complex or RISC). DNA damage has been proposed to stimulate transport of Translin into nuclei. It binds to RNA and single-stranded DNA, and its selectivity is modulated by interactions with GTP and TRAX. Translin may also regulate dendritic trafficking of BDNF RNAs as well as function as a key activator of siRNA-mediated silencing in drosophila. Translin and Trax participate in a variety of nucleic acid metabolism pathways in addition to RNAi and have been implicated in a wide range of biological activities, including mRNA processing, cell growth regulation, spermatogenesis, neuronal development/function, genome stability regulation and carcinogenesis; however, their precise role in some of the processes remains unclear.


:

Pssm-ID: 271349  Cd Length: 206  Bit Score: 239.36  E-value: 1.61e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295443057   9 LQDQIDKEHSIREKLTAEVDLLDEKLRVLQLLLANCEQNLENQ-----EEILEALEIIKSKTRGLAELASNFPYYKYNGV 83
Cdd:cd14819    1 LQEELEKEQELREEIREIVRELDQTLREIQAILQRIHSTPSSQvpelcESARELIEEVKETLAELAELIPPHQYYKYNDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295443057  84 WDRSIQKVVYLYLLASWTGrldkslrpTYSLLSLSEVGQILQVPVFPEEStFHLSIEQYLHAVLSLCSELARQSVNSVIS 163
Cdd:cd14819   81 WRRILQRAVFLIALRHFLE--------TGRLLTLEEVAEILGVPVNLKDG-FHLDLEDYLHGLLSLVNELSRLAVNSVTL 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 295443057 164 GNYHIPFEALNTIQKVHSSFQVLSLKNDSLRRHFDGLKYDLKRSEDVVYDLRIHK 218
Cdd:cd14819  152 GDYERPLKISAFVKDLHAGFQLLNLKNDSLRKRFDGLKYDVKKVEEVVYDLSLRG 206
 
Name Accession Description Interval E-value
Translin cd14819
Translin, also known as TB-RBP (testis brain RNA-binding protein); Translin (also known as ...
9-218 1.61e-80

Translin, also known as TB-RBP (testis brain RNA-binding protein); Translin (also known as TB-RBP for Testis Brain RNA-binding protein, a mouse ortholog), is a paralog of its binding partner protein TRAX (translin-associated factor-X) and together they form oligomeric complexes known as C3PO proteins (for component 3 promoter of RNA-induced silencing complex or RISC). DNA damage has been proposed to stimulate transport of Translin into nuclei. It binds to RNA and single-stranded DNA, and its selectivity is modulated by interactions with GTP and TRAX. Translin may also regulate dendritic trafficking of BDNF RNAs as well as function as a key activator of siRNA-mediated silencing in drosophila. Translin and Trax participate in a variety of nucleic acid metabolism pathways in addition to RNAi and have been implicated in a wide range of biological activities, including mRNA processing, cell growth regulation, spermatogenesis, neuronal development/function, genome stability regulation and carcinogenesis; however, their precise role in some of the processes remains unclear.


Pssm-ID: 271349  Cd Length: 206  Bit Score: 239.36  E-value: 1.61e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295443057   9 LQDQIDKEHSIREKLTAEVDLLDEKLRVLQLLLANCEQNLENQ-----EEILEALEIIKSKTRGLAELASNFPYYKYNGV 83
Cdd:cd14819    1 LQEELEKEQELREEIREIVRELDQTLREIQAILQRIHSTPSSQvpelcESARELIEEVKETLAELAELIPPHQYYKYNDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295443057  84 WDRSIQKVVYLYLLASWTGrldkslrpTYSLLSLSEVGQILQVPVFPEEStFHLSIEQYLHAVLSLCSELARQSVNSVIS 163
Cdd:cd14819   81 WRRILQRAVFLIALRHFLE--------TGRLLTLEEVAEILGVPVNLKDG-FHLDLEDYLHGLLSLVNELSRLAVNSVTL 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 295443057 164 GNYHIPFEALNTIQKVHSSFQVLSLKNDSLRRHFDGLKYDLKRSEDVVYDLRIHK 218
Cdd:cd14819  152 GDYERPLKISAFVKDLHAGFQLLNLKNDSLRKRFDGLKYDVKKVEEVVYDLSLRG 206
Translin pfam01997
Translin family; Members of this family include Translin that interacts with DNA and forms a ...
19-218 2.42e-57

Translin family; Members of this family include Translin that interacts with DNA and forms a ring around the DNA. This family also includes Swiss:Q99598, that was found to interact with translin with yeast two-hybrid screen.


Pssm-ID: 460410 [Multi-domain]  Cd Length: 197  Bit Score: 180.01  E-value: 2.42e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295443057   19 IREKLTAEVDLLDEKLRVLQLLL-----ANCEQNLENQEEIlEALEIIKSKTRGLAELASNFPYYKYNGVWDRSIQKVVY 93
Cdd:pfam01997   2 RRERIIKISRDITALSKKIIFLLhrvhsTPSALNVLNPAKI-LAIKEAKERLAELAELLSKLNYYRYNRAWSPGLQEYIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295443057   94 LYLLASWTGrldkslrpTYSLLSLSEVGQILQVPVFPEESTFHLSIEQYLHAVLSLCSELARQSVNSVISGNYHIPFEAL 173
Cdd:pfam01997  81 ALTFAHYLE--------TGTLLTLEEVQEILGVPVNLDRDGFHLTIEDYLLGLFDLTGELMRLAINSVTLGDYERPLKIS 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 295443057  174 NTIQKVHSSFQVLSLKNDSLRRHFDGLKYDLKRSEDVVYDLRIHK 218
Cdd:pfam01997 153 QFLRDLYAGFQLLNLKNDDLRKKLDVLKYSVKKVEDVVYDLSVRG 197
 
Name Accession Description Interval E-value
Translin cd14819
Translin, also known as TB-RBP (testis brain RNA-binding protein); Translin (also known as ...
9-218 1.61e-80

Translin, also known as TB-RBP (testis brain RNA-binding protein); Translin (also known as TB-RBP for Testis Brain RNA-binding protein, a mouse ortholog), is a paralog of its binding partner protein TRAX (translin-associated factor-X) and together they form oligomeric complexes known as C3PO proteins (for component 3 promoter of RNA-induced silencing complex or RISC). DNA damage has been proposed to stimulate transport of Translin into nuclei. It binds to RNA and single-stranded DNA, and its selectivity is modulated by interactions with GTP and TRAX. Translin may also regulate dendritic trafficking of BDNF RNAs as well as function as a key activator of siRNA-mediated silencing in drosophila. Translin and Trax participate in a variety of nucleic acid metabolism pathways in addition to RNAi and have been implicated in a wide range of biological activities, including mRNA processing, cell growth regulation, spermatogenesis, neuronal development/function, genome stability regulation and carcinogenesis; however, their precise role in some of the processes remains unclear.


Pssm-ID: 271349  Cd Length: 206  Bit Score: 239.36  E-value: 1.61e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295443057   9 LQDQIDKEHSIREKLTAEVDLLDEKLRVLQLLLANCEQNLENQ-----EEILEALEIIKSKTRGLAELASNFPYYKYNGV 83
Cdd:cd14819    1 LQEELEKEQELREEIREIVRELDQTLREIQAILQRIHSTPSSQvpelcESARELIEEVKETLAELAELIPPHQYYKYNDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295443057  84 WDRSIQKVVYLYLLASWTGrldkslrpTYSLLSLSEVGQILQVPVFPEEStFHLSIEQYLHAVLSLCSELARQSVNSVIS 163
Cdd:cd14819   81 WRRILQRAVFLIALRHFLE--------TGRLLTLEEVAEILGVPVNLKDG-FHLDLEDYLHGLLSLVNELSRLAVNSVTL 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 295443057 164 GNYHIPFEALNTIQKVHSSFQVLSLKNDSLRRHFDGLKYDLKRSEDVVYDLRIHK 218
Cdd:cd14819  152 GDYERPLKISAFVKDLHAGFQLLNLKNDSLRKRFDGLKYDVKKVEEVVYDLSLRG 206
Translin pfam01997
Translin family; Members of this family include Translin that interacts with DNA and forms a ...
19-218 2.42e-57

Translin family; Members of this family include Translin that interacts with DNA and forms a ring around the DNA. This family also includes Swiss:Q99598, that was found to interact with translin with yeast two-hybrid screen.


Pssm-ID: 460410 [Multi-domain]  Cd Length: 197  Bit Score: 180.01  E-value: 2.42e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295443057   19 IREKLTAEVDLLDEKLRVLQLLL-----ANCEQNLENQEEIlEALEIIKSKTRGLAELASNFPYYKYNGVWDRSIQKVVY 93
Cdd:pfam01997   2 RRERIIKISRDITALSKKIIFLLhrvhsTPSALNVLNPAKI-LAIKEAKERLAELAELLSKLNYYRYNRAWSPGLQEYIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295443057   94 LYLLASWTGrldkslrpTYSLLSLSEVGQILQVPVFPEESTFHLSIEQYLHAVLSLCSELARQSVNSVISGNYHIPFEAL 173
Cdd:pfam01997  81 ALTFAHYLE--------TGTLLTLEEVQEILGVPVNLDRDGFHLTIEDYLLGLFDLTGELMRLAINSVTLGDYERPLKIS 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 295443057  174 NTIQKVHSSFQVLSLKNDSLRRHFDGLKYDLKRSEDVVYDLRIHK 218
Cdd:pfam01997 153 QFLRDLYAGFQLLNLKNDDLRKKLDVLKYSVKKVEDVVYDLSVRG 197
Translin-like cd14805
Translin and translin-associated factor-X (TRAX); Translin (also known as TB-RBP), and its ...
9-210 2.45e-28

Translin and translin-associated factor-X (TRAX); Translin (also known as TB-RBP), and its binding partner protein TRAX (translin-associated factor-X) are a paralogous pair of conserved proteins, and oligomeric complexes of TRAX and translin are known as C3PO proteins (for component 3 promoter of RNA-induced silencing complex or RISC). The Translin-Trax complex enhances the removal of the passenger strand in RNAi and the formation of active RISC. Translin and Trax participate in a variety of nucleic acid metabolism pathways in addition to RNAi and have been implicated in a wide range of biological activities, including mRNA processing, cell growth regulation, spermatogenesis, neuronal development/function, genome stability regulation and carcinogenesis; however, their precise role in some of the processes remains unclear. It has been shown that Trax subunit, but not Translin, possesses a Glu-Glu-Asp catalytic center with the capacity to digest RNA as well as DNA; this catalytic activity is required for passenger-strand removal and RISC activation in RNAi. In Archaeoglobus fulgidus, Trax-like-subunits assemble into an octameric structure, highly similar to human C3PO; its complex with duplex RNA reveals that the octamer entirely encapsulates a single 13-base-pair RNA duplex inside a large inner cavity.


Pssm-ID: 271348 [Multi-domain]  Cd Length: 197  Bit Score: 105.66  E-value: 2.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295443057   9 LQDQIDKEHSIREKLTAEVDLLDEKLRVLQLLLANCEQNLENQEEIL----EALEIIKSKTRGLAELASNFPYYKYNGVW 84
Cdd:cd14805    1 YQGELDAEQDIRERIRKVVRDIEQESKEIIFLLQGIHSGKGDIEKRClearEHLNTVKQKLTSLATELPAEQYYRFHEHW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295443057  85 DRSIQKVVYLYLLASWTgrldkslrPTYSLLSLSEVGQILQVPVFPEEStFHLSIEQYLHAVLSLCSELARQSVNSVISG 164
Cdd:cd14805   81 TFGLQRLVFAAAFVVYL--------ETETLVTREEVTEILGIEPDREKG-FHLDVEDYLLGVLDLASELSRLCINSVTAG 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 295443057 165 NYHIPFEALNTIQKVHSSFQVLSLKNDSLRRHFDGLKYDLKRSEDV 210
Cdd:cd14805  152 DYDRPLHISTFINELYSGFRLLNLKNDELRKRYDTLKYDVKKVEEV 197
TRAX cd14820
Translin-associated factor-X (TRAX); TRAX (translin-associated factor-X) is a paralog of its ...
50-213 3.87e-05

Translin-associated factor-X (TRAX); TRAX (translin-associated factor-X) is a paralog of its binding partner protein Translin and together they form oligomeric complexes known as C3PO proteins (for component 3 promoter of RNA-induced silencing complex or RISC). TRAX complexed with Translin is possibly involved in dendritic RNA processing and in DNA double-strand break repair as an interacting partner with C1D, an activator of the DNA-dependent protein kinase involved in the repair of DNA-double strand breaks. It has been shown that Trax subunit, but not Translin, possesses a Glu-Glu-Asp catalytic center with the capacity to digest RNA; this catalytic activity is required for passenger-strand removal and RISC activation in RNAi. In Archaeoglobus fulgidus, Trax-like-subunits assemble into an octameric structure, highly similar to human C3PO; its complex with duplex RNA reveals that the octamer entirely encapsulates a single 13-base-pair RNA duplex inside a large inner cavity. Translin and Trax participate in a variety of nucleic acid metabolism pathways in addition to RNAi and have been implicated in a wide range of biological activities, including mRNA processing, cell growth regulation, spermatogenesis, neuronal development/function, genome stability regulation and carcinogenesis; however, their precise role in some of the processes remains unclear.


Pssm-ID: 271350 [Multi-domain]  Cd Length: 182  Bit Score: 42.55  E-value: 3.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295443057  50 NQEEILEALEIIKSKTRGLAELASNFPYYKYNGVWDRSIQKVVYLYLLASW--TGRLdkslrPTYSLlslsevgqilQVP 127
Cdd:cd14820   40 DLEEAEELLKEARELLEELRELLKEEPDLLYSGAVSPALQEYVEALSFYHFlkEGRL-----PTPDE----------ELG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295443057 128 VFPEEstfhlsieqYLHAVLSLCSELARQSVNSVISGNYHIPFEALNTIQKVHSSFQVLSLKN-DSLRRHFDGLKYDLKR 206
Cdd:cd14820  105 VTPED---------YLLGLADLTGELMRYAIDSLRKGDLEEAEKYLEFMEEIYEGLMSFDYPDaLELRKKLDVDRQSLLK 175

                 ....*..
gi 295443057 207 SEDVVYD 213
Cdd:cd14820  176 EETRCYE 182
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH