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Conserved domains on  [gi|147902314|ref|NP_001080668|]
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THO complex subunit 5 homolog B [Xenopus laevis]

Protein Classification

FimP domain-containing protein( domain architecture ID 11184601)

FimP domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FmiP_Thoc5 pfam09766
Fms-interacting protein/Thoc5; This entry carries part of the crucial 144 N-terminal residues ...
98-447 1.32e-158

Fms-interacting protein/Thoc5; This entry carries part of the crucial 144 N-terminal residues of the FmiP (Fms interacting protein). A member of the THO (suppressors of the transcriptional defects of hpr1delta by overexpression) complex which is a subcomplex of the transcription/export (TREX) complex. It is essential for the binding of the protein to the cytoplasmic domain of activated Fms-molecules in M-CSF induced haematopoietic differentiation of macrophages. Fmip is also known as THOC5 (THO complex subunit 5) a 683 amino acids long protein which contains a nuclear localization sequence (NLS), a leucine zipper and a PEST like sequence (aa. 303-319) that carries three ataxia-telangiectasia mutated (ATM) kinase specific phosphorylation sites. The C-terminus contains a THOC1 binding site. The level of FMIP/Thoc5 expression might form a threshold that determines whether cells differentiate into macrophages or into granulocytes.


:

Pssm-ID: 462889  Cd Length: 347  Bit Score: 460.63  E-value: 1.32e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902314   98 RLANIRLKKARDQTHEAKQKVDAYNLQLQNLLYEVMHLQKEITKCLEFKSKHEEIELVSVEEFYSDAPAAISKPEITSTD 177
Cdd:pfam09766   1 RLAKIRLKTGRDETHEAKQKVDSLHLQLQNLLYEKSHLKKEIKKCLDFKSKDEDIELVPEEEFYAEAPEDISKPELTKDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902314  178 PHQQTLSRLDWELEQRKRLAEKYKECLASKEKILKEIEIKKEYLNTLQPQLNSIMQASLPVQEYLSMPFDCMHKQYETAR 257
Cdd:pfam09766  81 EHQLMLARLEWELEQRKELAKQLKELEQSKKKLLQEIESKKKRLSSLPPALKSLLKATKPLQEALGLPLDKERKQHELAS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902314  258 HLPAPLYVLFVQASAYSQACDQKLVVAIEGNVEEARALFKPPEDSQDDESDSDAEEEQTT---KRRRPTLGVQLDDKRKE 334
Cdd:pfam09766 161 LLPKPLYVLYIQLTAYQEACDKNLTVEIVGDVEEAKAFKEATNQQEEDSSDSDAEGEELNrrkKRRRKTREGKQEEKSSK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902314  335 MLKRHPLCVTLTLMCKEGSTLTLTFYFLMNLNILTVKVKiqpafeLSTAISAGDLLNPDLILGCLYQGDDGKTTPNPANK 414
Cdd:pfam09766 241 LLKPHPLSVELTIKCKDDTKLKLQFRYLPKLNIVTVKAQ------LTLDSSAGDLLSDESLLSNLFPGDTGLESPNPANK 314
                         330       340       350
                  ....*....|....*....|....*....|...
gi 147902314  415 YQFDKIGILSLSDYISELGHPYVWAQTMGGLHF 447
Cdd:pfam09766 315 YQLQNLGLDEFNDNFSELGKPYKWAQRLCGLDF 347
 
Name Accession Description Interval E-value
FmiP_Thoc5 pfam09766
Fms-interacting protein/Thoc5; This entry carries part of the crucial 144 N-terminal residues ...
98-447 1.32e-158

Fms-interacting protein/Thoc5; This entry carries part of the crucial 144 N-terminal residues of the FmiP (Fms interacting protein). A member of the THO (suppressors of the transcriptional defects of hpr1delta by overexpression) complex which is a subcomplex of the transcription/export (TREX) complex. It is essential for the binding of the protein to the cytoplasmic domain of activated Fms-molecules in M-CSF induced haematopoietic differentiation of macrophages. Fmip is also known as THOC5 (THO complex subunit 5) a 683 amino acids long protein which contains a nuclear localization sequence (NLS), a leucine zipper and a PEST like sequence (aa. 303-319) that carries three ataxia-telangiectasia mutated (ATM) kinase specific phosphorylation sites. The C-terminus contains a THOC1 binding site. The level of FMIP/Thoc5 expression might form a threshold that determines whether cells differentiate into macrophages or into granulocytes.


Pssm-ID: 462889  Cd Length: 347  Bit Score: 460.63  E-value: 1.32e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902314   98 RLANIRLKKARDQTHEAKQKVDAYNLQLQNLLYEVMHLQKEITKCLEFKSKHEEIELVSVEEFYSDAPAAISKPEITSTD 177
Cdd:pfam09766   1 RLAKIRLKTGRDETHEAKQKVDSLHLQLQNLLYEKSHLKKEIKKCLDFKSKDEDIELVPEEEFYAEAPEDISKPELTKDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902314  178 PHQQTLSRLDWELEQRKRLAEKYKECLASKEKILKEIEIKKEYLNTLQPQLNSIMQASLPVQEYLSMPFDCMHKQYETAR 257
Cdd:pfam09766  81 EHQLMLARLEWELEQRKELAKQLKELEQSKKKLLQEIESKKKRLSSLPPALKSLLKATKPLQEALGLPLDKERKQHELAS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902314  258 HLPAPLYVLFVQASAYSQACDQKLVVAIEGNVEEARALFKPPEDSQDDESDSDAEEEQTT---KRRRPTLGVQLDDKRKE 334
Cdd:pfam09766 161 LLPKPLYVLYIQLTAYQEACDKNLTVEIVGDVEEAKAFKEATNQQEEDSSDSDAEGEELNrrkKRRRKTREGKQEEKSSK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902314  335 MLKRHPLCVTLTLMCKEGSTLTLTFYFLMNLNILTVKVKiqpafeLSTAISAGDLLNPDLILGCLYQGDDGKTTPNPANK 414
Cdd:pfam09766 241 LLKPHPLSVELTIKCKDDTKLKLQFRYLPKLNIVTVKAQ------LTLDSSAGDLLSDESLLSNLFPGDTGLESPNPANK 314
                         330       340       350
                  ....*....|....*....|....*....|...
gi 147902314  415 YQFDKIGILSLSDYISELGHPYVWAQTMGGLHF 447
Cdd:pfam09766 315 YQLQNLGLDEFNDNFSELGKPYKWAQRLCGLDF 347
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
26-226 8.14e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 8.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902314    26 EQEGRYYSEEAEVDVRDSREDYQLYKDTcvaLQRLMSEIQDLKSK-GSKDSAMEIEEKKIQscvhfmTLKKLNRLANIRL 104
Cdd:TIGR02169  779 EALNDLEARLSHSRIPEIQAELSKLEEE---VSRIEARLREIEQKlNRLTLEKEYLEKEIQ------ELQEQRIDLKEQI 849
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902314   105 KKARDQTHEAKQKVDAYNLQLQNLLYEVMHLQKEITKCLEFKSKHEEiELVSVEEFYSDAPAAISKPE--ITSTDPHQQT 182
Cdd:TIGR02169  850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA-QLRELERKIEELEAQIEKKRkrLSELKAKLEA 928
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 147902314   183 LSRLDWELEQRKRLAEKYKECLASKEKILKEIEIKKEYLNTLQP 226
Cdd:TIGR02169  929 LEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEP 972
 
Name Accession Description Interval E-value
FmiP_Thoc5 pfam09766
Fms-interacting protein/Thoc5; This entry carries part of the crucial 144 N-terminal residues ...
98-447 1.32e-158

Fms-interacting protein/Thoc5; This entry carries part of the crucial 144 N-terminal residues of the FmiP (Fms interacting protein). A member of the THO (suppressors of the transcriptional defects of hpr1delta by overexpression) complex which is a subcomplex of the transcription/export (TREX) complex. It is essential for the binding of the protein to the cytoplasmic domain of activated Fms-molecules in M-CSF induced haematopoietic differentiation of macrophages. Fmip is also known as THOC5 (THO complex subunit 5) a 683 amino acids long protein which contains a nuclear localization sequence (NLS), a leucine zipper and a PEST like sequence (aa. 303-319) that carries three ataxia-telangiectasia mutated (ATM) kinase specific phosphorylation sites. The C-terminus contains a THOC1 binding site. The level of FMIP/Thoc5 expression might form a threshold that determines whether cells differentiate into macrophages or into granulocytes.


Pssm-ID: 462889  Cd Length: 347  Bit Score: 460.63  E-value: 1.32e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902314   98 RLANIRLKKARDQTHEAKQKVDAYNLQLQNLLYEVMHLQKEITKCLEFKSKHEEIELVSVEEFYSDAPAAISKPEITSTD 177
Cdd:pfam09766   1 RLAKIRLKTGRDETHEAKQKVDSLHLQLQNLLYEKSHLKKEIKKCLDFKSKDEDIELVPEEEFYAEAPEDISKPELTKDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902314  178 PHQQTLSRLDWELEQRKRLAEKYKECLASKEKILKEIEIKKEYLNTLQPQLNSIMQASLPVQEYLSMPFDCMHKQYETAR 257
Cdd:pfam09766  81 EHQLMLARLEWELEQRKELAKQLKELEQSKKKLLQEIESKKKRLSSLPPALKSLLKATKPLQEALGLPLDKERKQHELAS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902314  258 HLPAPLYVLFVQASAYSQACDQKLVVAIEGNVEEARALFKPPEDSQDDESDSDAEEEQTT---KRRRPTLGVQLDDKRKE 334
Cdd:pfam09766 161 LLPKPLYVLYIQLTAYQEACDKNLTVEIVGDVEEAKAFKEATNQQEEDSSDSDAEGEELNrrkKRRRKTREGKQEEKSSK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902314  335 MLKRHPLCVTLTLMCKEGSTLTLTFYFLMNLNILTVKVKiqpafeLSTAISAGDLLNPDLILGCLYQGDDGKTTPNPANK 414
Cdd:pfam09766 241 LLKPHPLSVELTIKCKDDTKLKLQFRYLPKLNIVTVKAQ------LTLDSSAGDLLSDESLLSNLFPGDTGLESPNPANK 314
                         330       340       350
                  ....*....|....*....|....*....|...
gi 147902314  415 YQFDKIGILSLSDYISELGHPYVWAQTMGGLHF 447
Cdd:pfam09766 315 YQLQNLGLDEFNDNFSELGKPYKWAQRLCGLDF 347
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
26-226 8.14e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 8.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902314    26 EQEGRYYSEEAEVDVRDSREDYQLYKDTcvaLQRLMSEIQDLKSK-GSKDSAMEIEEKKIQscvhfmTLKKLNRLANIRL 104
Cdd:TIGR02169  779 EALNDLEARLSHSRIPEIQAELSKLEEE---VSRIEARLREIEQKlNRLTLEKEYLEKEIQ------ELQEQRIDLKEQI 849
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147902314   105 KKARDQTHEAKQKVDAYNLQLQNLLYEVMHLQKEITKCLEFKSKHEEiELVSVEEFYSDAPAAISKPE--ITSTDPHQQT 182
Cdd:TIGR02169  850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA-QLRELERKIEELEAQIEKKRkrLSELKAKLEA 928
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 147902314   183 LSRLDWELEQRKRLAEKYKECLASKEKILKEIEIKKEYLNTLQP 226
Cdd:TIGR02169  929 LEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEP 972
 
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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