NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24649795|ref|NP_733044|]
View 

katazuke [Drosophila melanogaster]

Protein Classification

E3 ubiquitin-protein transferase MAEA( domain architecture ID 12218107)

E3 ubiquitin-protein transferase MAEA is a core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1

CATH:  3.30.40.10
EC:  2.3.2.27
Gene Symbol:  MAEA
Gene Ontology:  GO:0008270|GO:0016567|GO:0004842
PubMed:  33947846|29911972|19489725|11007473
SCOP:  3000160

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 158-299 1.36e-43

CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X mental retardation protein (FMRP), but its functional significance has yet to be determined. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif.


:

Pssm-ID: 402305 [Multi-domain]  Cd Length: 143  Bit Score: 148.49  E-value: 1.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649795   158 IFQTSREVEDDLASHSTTKCVLWCIDNKSKLRKINSTIEFSLRVQEFIELVRQNQRFEAVKHSRRYFPAYEKTQLNEICH 237
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGKILEALEYARENLAPFNEEHLKELEK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24649795   238 VMALLAYPADAQAEHYRKYMDPQRWQKLVLDFRQENYRLFQLSSTSVFSAAVQAGLSALKTP 299
Cdd:pfam10607  81 LMGLLAFPDPTDSSPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSALKTL 142
RING-Ubox_Emp cd16659
U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and ...
 333-383 8.30e-23

U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and similar proteins; Emp, also known as cell proliferation-inducing gene 5 protein or macrophage erythroblast attacher (MAEA), is a key protein which functions in normal differentiation of erythroid cells and macrophages. It is a potential biomarker for hematopoietic evaluation of Hematopoietic stem cell transplantation (HSCT) patients. Emp was initially identified as a heparin-binding protein involved in the association of erythroblasts with macrophages. It promotes erythroid proliferation and maturation. It also plays an important role in erythroblastic island formation. Absence of Emp leads to failure of erythroblast nuclear extrusion. It is required in definitive erythropoiesis and plays a cell intrinsic role in the erythroid lineage. Emp contains a Lissencephaly type-1-like homology (LisH) motif, a C-terminal to LisH (CTLH) domain, and a RING-like U-box domain at the C-terminus.


:

Pssm-ID: 438321  Cd Length: 52  Bit Score: 90.32  E-value: 8.30e-23
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24649795 333 SRLICRVTGLPLNEHNQPMMLPNGQIFGQMALPDIT-KDDGTVTCPVTNTKF 383
Cdd:cd16659   1 SRLVCRITGEVMNEHNPPLALPNGYVYSEKALEEMAeKNDGKVVCPRTGESF 52
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 119-150 1.50e-05

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


:

Pssm-ID: 128913  Cd Length: 34  Bit Score: 41.65  E-value: 1.50e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 24649795    119 WKRIRLDRLVIEHLLRMGYYETAEELAAKSDV 150
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGL 32
 
Name Accession Description Interval E-value
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 158-299 1.36e-43

CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X mental retardation protein (FMRP), but its functional significance has yet to be determined. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif.


Pssm-ID: 402305 [Multi-domain]  Cd Length: 143  Bit Score: 148.49  E-value: 1.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649795   158 IFQTSREVEDDLASHSTTKCVLWCIDNKSKLRKINSTIEFSLRVQEFIELVRQNQRFEAVKHSRRYFPAYEKTQLNEICH 237
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGKILEALEYARENLAPFNEEHLKELEK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24649795   238 VMALLAYPADAQAEHYRKYMDPQRWQKLVLDFRQENYRLFQLSSTSVFSAAVQAGLSALKTP 299
Cdd:pfam10607  81 LMGLLAFPDPTDSSPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSALKTL 142
RING-Ubox_Emp cd16659
U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and ...
 333-383 8.30e-23

U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and similar proteins; Emp, also known as cell proliferation-inducing gene 5 protein or macrophage erythroblast attacher (MAEA), is a key protein which functions in normal differentiation of erythroid cells and macrophages. It is a potential biomarker for hematopoietic evaluation of Hematopoietic stem cell transplantation (HSCT) patients. Emp was initially identified as a heparin-binding protein involved in the association of erythroblasts with macrophages. It promotes erythroid proliferation and maturation. It also plays an important role in erythroblastic island formation. Absence of Emp leads to failure of erythroblast nuclear extrusion. It is required in definitive erythropoiesis and plays a cell intrinsic role in the erythroid lineage. Emp contains a Lissencephaly type-1-like homology (LisH) motif, a C-terminal to LisH (CTLH) domain, and a RING-like U-box domain at the C-terminus.


Pssm-ID: 438321  Cd Length: 52  Bit Score: 90.32  E-value: 8.30e-23
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24649795 333 SRLICRVTGLPLNEHNQPMMLPNGQIFGQMALPDIT-KDDGTVTCPVTNTKF 383
Cdd:cd16659   1 SRLVCRITGEVMNEHNPPLALPNGYVYSEKALEEMAeKNDGKVVCPRTGESF 52
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 158-215 3.71e-10

C-terminal to LisH motif; Alpha-helical motif of unknown function.


Pssm-ID: 128914  Cd Length: 58  Bit Score: 55.27  E-value: 3.71e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24649795    158 IFQTSREVEDDLASHSTTKCVLWCIDNKSKLRKINSTIEFSLRVQEFIELVRQNQRFE 215
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLEE 58
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 119-150 1.50e-05

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 41.65  E-value: 1.50e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 24649795    119 WKRIRLDRLVIEHLLRMGYYETAEELAAKSDV 150
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGL 32
COG5109 COG5109
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
22-387 7.02e-03

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227440 [Multi-domain]  Cd Length: 396  Bit Score: 38.45  E-value: 7.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649795  22 RFRSAQKIIDREVDQVINVSRQVEKALEAEEGPILAEVTKLVDNVAQKLQvLKRKAEEsinDELSVTQickRKLDH---- 97
Cdd:COG5109   2 KFYTDSNLEETNLQKCLDHTHEVDSKLKIDKRRLRKETMRSIDEIRSALS-LKNGQEF---DTLSHAE---ADLVGswks 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649795  98 -LKGITPPSSV-TGDLWQGSVDQWKRIRLDRLVIEHLLRMGYYETAEELAAKSDVRHLTN-LDIFQTSREVEDDLASHST 174
Cdd:COG5109  75 lLKEDCRPANFdVQVGNQIYPFSTQTVTYLVVYYLLENNCADVVERHISETKDGKDEIIKiRDGFVKLKKVISGISEKST 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649795 175 TKCVLWcIDNKSKLRKINSTIEFSL-------------RVQEFIELVRQNQRFEAVKHSRRYFPAYEKTQ---LNEICH- 237
Cdd:COG5109 155 FLLIEF-LQIEGYLSKGDTESELELylvsheslllihkRYDEALRLCFTKLASFVPKHIQDVKPLLRFLVnapTDCFRHr 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649795 238 -------VMALLAYPADAQAEHYRKYMDpQRWQKLVLDFRQENYRLFQLSSTSVFSAAVQAGLSALKTPHCYAQTCRNLN 310
Cdd:COG5109 234 ekelmqnIQEALKKSLIGQPIEDIDKVN-KSRKKLIELFKSEYCAANGMPNRSPLRELVETGTIAFLQLSKSGSILFDKH 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649795 311 CPVCQEDLNRIALKLPYSHCVQSRLICRVTGLPLNEHNQPMMLPNGQIFGQMALPDITKdDGTVT-----CPVtNTKFSN 385
Cdd:COG5109 313 VDWTDDSELPMEIKLPKGRHFHSLFICPVLKELCTDENPPVMLECGHVISKEALSVLSQ-NGVLSfkcpyCPE-MSKYEN 390


                ..
gi 24649795 386 PK 387
Cdd:COG5109 391 IL 392
 
Name Accession Description Interval E-value
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 158-299 1.36e-43

CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X mental retardation protein (FMRP), but its functional significance has yet to be determined. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif.


Pssm-ID: 402305 [Multi-domain]  Cd Length: 143  Bit Score: 148.49  E-value: 1.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649795   158 IFQTSREVEDDLASHSTTKCVLWCIDNKSKLRKINSTIEFSLRVQEFIELVRQNQRFEAVKHSRRYFPAYEKTQLNEICH 237
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGKILEALEYARENLAPFNEEHLKELEK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24649795   238 VMALLAYPADAQAEHYRKYMDPQRWQKLVLDFRQENYRLFQLSSTSVFSAAVQAGLSALKTP 299
Cdd:pfam10607  81 LMGLLAFPDPTDSSPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSALKTL 142
RING-Ubox_Emp cd16659
U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and ...
 333-383 8.30e-23

U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and similar proteins; Emp, also known as cell proliferation-inducing gene 5 protein or macrophage erythroblast attacher (MAEA), is a key protein which functions in normal differentiation of erythroid cells and macrophages. It is a potential biomarker for hematopoietic evaluation of Hematopoietic stem cell transplantation (HSCT) patients. Emp was initially identified as a heparin-binding protein involved in the association of erythroblasts with macrophages. It promotes erythroid proliferation and maturation. It also plays an important role in erythroblastic island formation. Absence of Emp leads to failure of erythroblast nuclear extrusion. It is required in definitive erythropoiesis and plays a cell intrinsic role in the erythroid lineage. Emp contains a Lissencephaly type-1-like homology (LisH) motif, a C-terminal to LisH (CTLH) domain, and a RING-like U-box domain at the C-terminus.


Pssm-ID: 438321  Cd Length: 52  Bit Score: 90.32  E-value: 8.30e-23
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24649795 333 SRLICRVTGLPLNEHNQPMMLPNGQIFGQMALPDIT-KDDGTVTCPVTNTKF 383
Cdd:cd16659   1 SRLVCRITGEVMNEHNPPLALPNGYVYSEKALEEMAeKNDGKVVCPRTGESF 52
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 158-215 3.71e-10

C-terminal to LisH motif; Alpha-helical motif of unknown function.


Pssm-ID: 128914  Cd Length: 58  Bit Score: 55.27  E-value: 3.71e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24649795    158 IFQTSREVEDDLASHSTTKCVLWCIDNKSKLRKINSTIEFSLRVQEFIELVRQNQRFE 215
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLEE 58
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 215-302 9.84e-09

CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi)


Pssm-ID: 214806  Cd Length: 99  Bit Score: 52.30  E-value: 9.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649795    215 EAVKHSRRYFPAYEKTQ---LNEICHVMALLAYPADAQAEHYRKYMDPQRWQKLVLDFRQE--NYrLFQLSSTSVFSAAV 289
Cdd:smart00757   5 EALAYARELLAPFAKEHekfLKELEKTMALLAYPDPTEPSPYKELLSPSQREKLAEELNSAilEL-LHGKSSESPLEILL 83

                           90
                   ....*....|...
gi 24649795    290 QAGLSALKTPHCY 302
Cdd:smart00757  84 SAGLAALKTLLEK 96
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 119-150 1.50e-05

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 41.65  E-value: 1.50e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 24649795    119 WKRIRLDRLVIEHLLRMGYYETAEELAAKSDV 150
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGL 32
COG5109 COG5109
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
22-387 7.02e-03

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227440 [Multi-domain]  Cd Length: 396  Bit Score: 38.45  E-value: 7.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649795  22 RFRSAQKIIDREVDQVINVSRQVEKALEAEEGPILAEVTKLVDNVAQKLQvLKRKAEEsinDELSVTQickRKLDH---- 97
Cdd:COG5109   2 KFYTDSNLEETNLQKCLDHTHEVDSKLKIDKRRLRKETMRSIDEIRSALS-LKNGQEF---DTLSHAE---ADLVGswks 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649795  98 -LKGITPPSSV-TGDLWQGSVDQWKRIRLDRLVIEHLLRMGYYETAEELAAKSDVRHLTN-LDIFQTSREVEDDLASHST 174
Cdd:COG5109  75 lLKEDCRPANFdVQVGNQIYPFSTQTVTYLVVYYLLENNCADVVERHISETKDGKDEIIKiRDGFVKLKKVISGISEKST 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649795 175 TKCVLWcIDNKSKLRKINSTIEFSL-------------RVQEFIELVRQNQRFEAVKHSRRYFPAYEKTQ---LNEICH- 237
Cdd:COG5109 155 FLLIEF-LQIEGYLSKGDTESELELylvsheslllihkRYDEALRLCFTKLASFVPKHIQDVKPLLRFLVnapTDCFRHr 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649795 238 -------VMALLAYPADAQAEHYRKYMDpQRWQKLVLDFRQENYRLFQLSSTSVFSAAVQAGLSALKTPHCYAQTCRNLN 310
Cdd:COG5109 234 ekelmqnIQEALKKSLIGQPIEDIDKVN-KSRKKLIELFKSEYCAANGMPNRSPLRELVETGTIAFLQLSKSGSILFDKH 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649795 311 CPVCQEDLNRIALKLPYSHCVQSRLICRVTGLPLNEHNQPMMLPNGQIFGQMALPDITKdDGTVT-----CPVtNTKFSN 385
Cdd:COG5109 313 VDWTDDSELPMEIKLPKGRHFHSLFICPVLKELCTDENPPVMLECGHVISKEALSVLSQ-NGVLSfkcpyCPE-MSKYEN 390


                ..
gi 24649795 386 PK 387
Cdd:COG5109 391 IL 392
 
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