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Conserved domains on  [gi|119623298|gb|EAX02893|]
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nuclear RNA export factor 5, isoform CRA_b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tap-RNA_bind pfam09162
Tap, RNA-binding; Members of this family adopt a structure consisting of an alpha+beta ...
 13-92 4.83e-49

Tap, RNA-binding; Members of this family adopt a structure consisting of an alpha+beta sandwich with an antiparallel beta-sheet, arranged in a 2(beta-alpha-beta) motif. They are mainly found in mRNA export factors, and mediate the sequence nonspecific nuclear export of cellular mRNAs as well as the sequence-specific export of retroviral mRNAs bearing the constitutive transport element.


:

Pssm-ID: 462696  Cd Length: 80  Bit Score: 160.41  E-value: 4.83e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623298   13 WFKVTIPYGIKYDKAWLMNSIQSNCSVPFTPVDFHYIRNRACFFVQVASAASALKDVSYKIYDDENQKICIFVSHFTAPY 92
Cdd:pfam09162   1 WFKVTIPYGKKYDKKWLLNSIQSLCSVPFTPVDFHYEKNRAVFFVEDASTASALKKVSRKITDEDGRKISIFVNPSAPPY 80
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 116-252 1.06e-03

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


The actual alignment was detected with superfamily member cd21340:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 220  Bit Score: 40.15  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623298 116 VSQQALDL-QNLRFDPDLMgrdidiilnrrNCMAATLKIiernfpellsLNLCNNKLYQLDGLSDITekapKVKTLNLSK 194
Cdd:cd21340   97 IENQRLPPgEKLTFDPRSL-----------AALSNSLRV----------LNISGNNIDSLEPLAPLR----NLEQLDASN 151

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623298 195 NKLESAWELGKVKG--LKLEELWLEGNPLCStfsdQSAYVSAIRDCFPKLLRLDGRELSA 252
Cdd:cd21340  152 NQISDLEELLDLLSswPSLRELDLTGNPVCK----KPKYRDKIILASKSLEVLDGKEITD 207
 
Name Accession Description Interval E-value
Tap-RNA_bind pfam09162
Tap, RNA-binding; Members of this family adopt a structure consisting of an alpha+beta ...
 13-92 4.83e-49

Tap, RNA-binding; Members of this family adopt a structure consisting of an alpha+beta sandwich with an antiparallel beta-sheet, arranged in a 2(beta-alpha-beta) motif. They are mainly found in mRNA export factors, and mediate the sequence nonspecific nuclear export of cellular mRNAs as well as the sequence-specific export of retroviral mRNAs bearing the constitutive transport element.


Pssm-ID: 462696  Cd Length: 80  Bit Score: 160.41  E-value: 4.83e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623298   13 WFKVTIPYGIKYDKAWLMNSIQSNCSVPFTPVDFHYIRNRACFFVQVASAASALKDVSYKIYDDENQKICIFVSHFTAPY 92
Cdd:pfam09162   1 WFKVTIPYGKKYDKKWLLNSIQSLCSVPFTPVDFHYEKNRAVFFVEDASTASALKKVSRKITDEDGRKISIFVNPSAPPY 80
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 116-252 1.06e-03

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 40.15  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623298 116 VSQQALDL-QNLRFDPDLMgrdidiilnrrNCMAATLKIiernfpellsLNLCNNKLYQLDGLSDITekapKVKTLNLSK 194
Cdd:cd21340   97 IENQRLPPgEKLTFDPRSL-----------AALSNSLRV----------LNISGNNIDSLEPLAPLR----NLEQLDASN 151

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623298 195 NKLESAWELGKVKG--LKLEELWLEGNPLCStfsdQSAYVSAIRDCFPKLLRLDGRELSA 252
Cdd:cd21340  152 NQISDLEELLDLLSswPSLRELDLTGNPVCK----KPKYRDKIILASKSLEVLDGKEITD 207
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
157-221 1.72e-03

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.30  E-value: 1.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119623298 157 NFPELLSLNLCNNklyQLDGLSDITEKAPKVKTLNLSKNKLES-AWELGKVKglKLEELWLEGNPL 221
Cdd:COG4886  157 NLTNLKSLDLSNN---QLTDLPEELGNLTNLKELDLSNNQITDlPEPLGNLT--NLEELDLSGNQL 217
 
Name Accession Description Interval E-value
Tap-RNA_bind pfam09162
Tap, RNA-binding; Members of this family adopt a structure consisting of an alpha+beta ...
 13-92 4.83e-49

Tap, RNA-binding; Members of this family adopt a structure consisting of an alpha+beta sandwich with an antiparallel beta-sheet, arranged in a 2(beta-alpha-beta) motif. They are mainly found in mRNA export factors, and mediate the sequence nonspecific nuclear export of cellular mRNAs as well as the sequence-specific export of retroviral mRNAs bearing the constitutive transport element.


Pssm-ID: 462696  Cd Length: 80  Bit Score: 160.41  E-value: 4.83e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623298   13 WFKVTIPYGIKYDKAWLMNSIQSNCSVPFTPVDFHYIRNRACFFVQVASAASALKDVSYKIYDDENQKICIFVSHFTAPY 92
Cdd:pfam09162   1 WFKVTIPYGKKYDKKWLLNSIQSLCSVPFTPVDFHYEKNRAVFFVEDASTASALKKVSRKITDEDGRKISIFVNPSAPPY 80
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 116-252 1.06e-03

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 40.15  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623298 116 VSQQALDL-QNLRFDPDLMgrdidiilnrrNCMAATLKIiernfpellsLNLCNNKLYQLDGLSDITekapKVKTLNLSK 194
Cdd:cd21340   97 IENQRLPPgEKLTFDPRSL-----------AALSNSLRV----------LNISGNNIDSLEPLAPLR----NLEQLDASN 151

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119623298 195 NKLESAWELGKVKG--LKLEELWLEGNPLCStfsdQSAYVSAIRDCFPKLLRLDGRELSA 252
Cdd:cd21340  152 NQISDLEELLDLLSswPSLRELDLTGNPVCK----KPKYRDKIILASKSLEVLDGKEITD 207
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
157-221 1.72e-03

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.30  E-value: 1.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119623298 157 NFPELLSLNLCNNklyQLDGLSDITEKAPKVKTLNLSKNKLES-AWELGKVKglKLEELWLEGNPL 221
Cdd:COG4886  157 NLTNLKSLDLSNN---QLTDLPEELGNLTNLKELDLSNNQITDlPEPLGNLT--NLEELDLSGNQL 217
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
157-221 1.94e-03

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.30  E-value: 1.94e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119623298 157 NFPELLSLNLCNNKLYQLDGLSditeKAPKVKTLNLSKNKLESAWELGKVKglKLEELWLEGNPL 221
Cdd:COG4886  226 NLTNLETLDLSNNQLTDLPELG----NLTNLEELDLSNNQLTDLPPLANLT--NLKTLDLSNNQL 284
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
157-221 2.66e-03

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 39.53  E-value: 2.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119623298 157 NFPELLSLNLCNNKLYQL-DGLSDITekapKVKTLNLSKNKLESAWELGKVKglKLEELWLEGNPL 221
Cdd:COG4886  203 NLTNLEELDLSGNQLTDLpEPLANLT----NLETLDLSNNQLTDLPELGNLT--NLEELDLSNNQL 262
 
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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