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Conserved domains on  [gi|205829194|sp|A9JRX0|]
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RecName: Full=Male-specific lethal 1-like 1; Short=MSL1-like 1; AltName: Full=Male-specific lethal-1 homolog 1; Short=MSL-1

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PEHE pfam15275
PEHE domain; This domain was first identified in drosophila MSL1 (male-specific lethal 1). In ...
348-466 6.86e-27

PEHE domain; This domain was first identified in drosophila MSL1 (male-specific lethal 1). In drosophila it binds to the histone acetyltransferase males-absent on the first protein (MOF) and to protein male-specific lethal-3 (MSL3).


:

Pssm-ID: 464607  Cd Length: 128  Bit Score: 104.88  E-value: 6.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205829194  348 VEVPSWRESILEPLGQKEAS-DILECLDDSVFLKRHSKLEldEKRRKRWDIQRIREQRMFQRLQQRMNRRKVI--QESEP 424
Cdd:pfam15275   1 ILTPSWRVVDLNPLEDSEEDeDEIEDLSDEVFSKRHQKYE--EKERKRWDLWRIREQRRRESLRSRSYPSRNTpvPLGPQ 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 205829194  425 ELLSFHAEPEDVEYiMVTPFLPVVAfgSPLPNLKQQD-----------FDLPW 466
Cdd:pfam15275  79 PSSPFYPSPEDIED-QSVLEVPVQA--SPLPPLSPETssllseevqewFSLPW 128
MSL1_dimer pfam16801
dimerization domain of Male-specific-Lethal 1; MSL1_dimer is the short coiled dimerization ...
168-203 5.81e-05

dimerization domain of Male-specific-Lethal 1; MSL1_dimer is the short coiled dimerization domain of higher eukaryotic MSL1, part of the MSL or Male-Specific Lethal complex. This complex regulates the dosage compensation of the male X chromosome in Drosophila and other eukaryotes. The structure of the MSL1/MSL2 core shows that two MSL2 subunits bind to a dimer formed by two molecules of MSL1. MSL11 is a substrate for MSL2 E3 ubiquitin ligase activity.


:

Pssm-ID: 435590  Cd Length: 37  Bit Score: 40.34  E-value: 5.81e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 205829194  168 VDPQTSCIRQILLLQLELIEQQQKHLHNKNKEIEDL 203
Cdd:pfam16801   2 NSNQTSCLRQILLLQLELIEQQQQQLQNKNKEIDDL 37
 
Name Accession Description Interval E-value
PEHE pfam15275
PEHE domain; This domain was first identified in drosophila MSL1 (male-specific lethal 1). In ...
348-466 6.86e-27

PEHE domain; This domain was first identified in drosophila MSL1 (male-specific lethal 1). In drosophila it binds to the histone acetyltransferase males-absent on the first protein (MOF) and to protein male-specific lethal-3 (MSL3).


Pssm-ID: 464607  Cd Length: 128  Bit Score: 104.88  E-value: 6.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205829194  348 VEVPSWRESILEPLGQKEAS-DILECLDDSVFLKRHSKLEldEKRRKRWDIQRIREQRMFQRLQQRMNRRKVI--QESEP 424
Cdd:pfam15275   1 ILTPSWRVVDLNPLEDSEEDeDEIEDLSDEVFSKRHQKYE--EKERKRWDLWRIREQRRRESLRSRSYPSRNTpvPLGPQ 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 205829194  425 ELLSFHAEPEDVEYiMVTPFLPVVAfgSPLPNLKQQD-----------FDLPW 466
Cdd:pfam15275  79 PSSPFYPSPEDIED-QSVLEVPVQA--SPLPPLSPETssllseevqewFSLPW 128
MSL1_dimer pfam16801
dimerization domain of Male-specific-Lethal 1; MSL1_dimer is the short coiled dimerization ...
168-203 5.81e-05

dimerization domain of Male-specific-Lethal 1; MSL1_dimer is the short coiled dimerization domain of higher eukaryotic MSL1, part of the MSL or Male-Specific Lethal complex. This complex regulates the dosage compensation of the male X chromosome in Drosophila and other eukaryotes. The structure of the MSL1/MSL2 core shows that two MSL2 subunits bind to a dimer formed by two molecules of MSL1. MSL11 is a substrate for MSL2 E3 ubiquitin ligase activity.


Pssm-ID: 435590  Cd Length: 37  Bit Score: 40.34  E-value: 5.81e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 205829194  168 VDPQTSCIRQILLLQLELIEQQQKHLHNKNKEIEDL 203
Cdd:pfam16801   2 NSNQTSCLRQILLLQLELIEQQQQQLQNKNKEIDDL 37
 
Name Accession Description Interval E-value
PEHE pfam15275
PEHE domain; This domain was first identified in drosophila MSL1 (male-specific lethal 1). In ...
348-466 6.86e-27

PEHE domain; This domain was first identified in drosophila MSL1 (male-specific lethal 1). In drosophila it binds to the histone acetyltransferase males-absent on the first protein (MOF) and to protein male-specific lethal-3 (MSL3).


Pssm-ID: 464607  Cd Length: 128  Bit Score: 104.88  E-value: 6.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205829194  348 VEVPSWRESILEPLGQKEAS-DILECLDDSVFLKRHSKLEldEKRRKRWDIQRIREQRMFQRLQQRMNRRKVI--QESEP 424
Cdd:pfam15275   1 ILTPSWRVVDLNPLEDSEEDeDEIEDLSDEVFSKRHQKYE--EKERKRWDLWRIREQRRRESLRSRSYPSRNTpvPLGPQ 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 205829194  425 ELLSFHAEPEDVEYiMVTPFLPVVAfgSPLPNLKQQD-----------FDLPW 466
Cdd:pfam15275  79 PSSPFYPSPEDIED-QSVLEVPVQA--SPLPPLSPETssllseevqewFSLPW 128
MSL1_dimer pfam16801
dimerization domain of Male-specific-Lethal 1; MSL1_dimer is the short coiled dimerization ...
168-203 5.81e-05

dimerization domain of Male-specific-Lethal 1; MSL1_dimer is the short coiled dimerization domain of higher eukaryotic MSL1, part of the MSL or Male-Specific Lethal complex. This complex regulates the dosage compensation of the male X chromosome in Drosophila and other eukaryotes. The structure of the MSL1/MSL2 core shows that two MSL2 subunits bind to a dimer formed by two molecules of MSL1. MSL11 is a substrate for MSL2 E3 ubiquitin ligase activity.


Pssm-ID: 435590  Cd Length: 37  Bit Score: 40.34  E-value: 5.81e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 205829194  168 VDPQTSCIRQILLLQLELIEQQQKHLHNKNKEIEDL 203
Cdd:pfam16801   2 NSNQTSCLRQILLLQLELIEQQQQQLQNKNKEIDDL 37
 
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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