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Conserved domains on  [gi|15233170|ref|NP_191067|]
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LisH/CRA/RING-U-box domains-containing protein [Arabidopsis thaliana]

Protein Classification

MAEA family protein( domain architecture ID 12107818)

MAEA (macrophage erythroblast attacher) family protein containing CTLH (C-terminal to LisH motif) and U-box domains, may function as an E3 ubiquitin-protein transferase

CATH:  3.30.40.10
Gene Ontology:  GO:0061630
PubMed:  19489725
SCOP:  3000160

Graphical summary

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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 ...
 179-324 1.21e-50

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: 167.36  E-value: 1.21e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233170   179 IFREAKKVIDALKNREVASALTWCADNKTRLKKSKSKFEFQLRLQEFIELVRVDtaeSYKKAIQYARKHLASWGTTHMKE 258
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSG---KILEALEYARENLAPFNEEHLKE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15233170   259 LQHVLATLAFKSTTECSKYKVLFELRQWDVLVDQFKQEFCKLYGMTMEPLLNIYLQAGLSALKTPY 324
Cdd:pfam10607  78 LEKLMGLLAFPDPTDSSPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSALKTLS 143
RING-Ubox_Emp cd16659
U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and ...
 356-407 2.89e-27

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: 102.65  E-value: 2.89e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15233170 356 SKLVCYISKELMDTENPPQVLPNGYVYSTKALKEMAEKNGGKITCPRTGLVC 407
Cdd:cd16659   1 SRLVCRITGEVMNEHNPPLALPNGYVYSEKALEEMAEKNDGKVVCPRTGESF 52
 
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 ...
 179-324 1.21e-50

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: 167.36  E-value: 1.21e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233170   179 IFREAKKVIDALKNREVASALTWCADNKTRLKKSKSKFEFQLRLQEFIELVRVDtaeSYKKAIQYARKHLASWGTTHMKE 258
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSG---KILEALEYARENLAPFNEEHLKE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15233170   259 LQHVLATLAFKSTTECSKYKVLFELRQWDVLVDQFKQEFCKLYGMTMEPLLNIYLQAGLSALKTPY 324
Cdd:pfam10607  78 LEKLMGLLAFPDPTDSSPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSALKTLS 143
RING-Ubox_Emp cd16659
U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and ...
 356-407 2.89e-27

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: 102.65  E-value: 2.89e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15233170 356 SKLVCYISKELMDTENPPQVLPNGYVYSTKALKEMAEKNGGKITCPRTGLVC 407
Cdd:cd16659   1 SRLVCRITGEVMNEHNPPLALPNGYVYSEKALEEMAEKNDGKVVCPRTGESF 52
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 235-323 7.49e-22

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


Pssm-ID: 214806  Cd Length: 99  Bit Score: 89.28  E-value: 7.49e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233170    235 ESYKKAIQYARKHLASWGTTH---MKELQHVLATLAFKSTTECSKYKVLFELRQWDVLVDQFKQEFCKLY-GMTMEPLLN 310
Cdd:smart00757   1 GKIEEALAYARELLAPFAKEHekfLKELEKTMALLAYPDPTEPSPYKELLSPSQREKLAEELNSAILELLhGKSSESPLE 80

                           90
                   ....*....|...
gi 15233170    311 IYLQAGLSALKTP 323
Cdd:smart00757  81 ILLSAGLAALKTL 93
COG5109 COG5109
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
168-417 4.63e-13

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


Pssm-ID: 227440 [Multi-domain]  Cd Length: 396  Bit Score: 70.04  E-value: 4.63e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233170 168 SSNIMDLVDI-DIFREAKKVIDALKNREVASALTWcADNKTRLKKSKSKFEFQLRLQEFIELVRVDTAesYKKAIQYARK 246
Cdd:COG5109 126 KDGKDEIIKIrDGFVKLKKVISGISEKSTFLLIEF-LQIEGYLSKGDTESELELYLVSHESLLLIHKR--YDEALRLCFT 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233170 247 HLASWGTTHMKELQHVLATLAFKSTTEC-SKYKVLFE---------------------LRQWDVLVDQFKQEFCKLYGMT 304
Cdd:COG5109 203 KLASFVPKHIQDVKPLLRFLVNAPTDCFrHREKELMQniqealkksligqpiedidkvNKSRKKLIELFKSEYCAANGMP 282

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233170 305 MEPLLNIYLQAGLSALktPYGLEEGCTKEDPlSQENFRKLALP----LPFSKQHHSKLVCYISKELMDTENPPQVLPNGY 380
Cdd:COG5109 283 NRSPLRELVETGTIAF--LQLSKSGSILFDK-HVDWTDDSELPmeikLPKGRHFHSLFICPVLKELCTDENPPVMLECGH 359

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15233170 381 VYSTKALKEMAEKNGGKITCPRTGLVCNYTELVKAYI 417
Cdd:COG5109 360 VISKEALSVLSQNGVLSFKCPYCPEMSKYENILRVRF 396
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
 360-401 2.29e-04

RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.


Pssm-ID: 463881 [Multi-domain]  Cd Length: 38  Bit Score: 38.54  E-value: 2.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 15233170   360 CYISKELMDteNPpqVLPNGYVYSTKALKEMAEKNGGKITCP 401
Cdd:pfam13445   1 CPICLELFT--DP--VLPCGHTFCRECLEEMSQKKGGKFKCP 38
 
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 ...
 179-324 1.21e-50

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: 167.36  E-value: 1.21e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233170   179 IFREAKKVIDALKNREVASALTWCADNKTRLKKSKSKFEFQLRLQEFIELVRVDtaeSYKKAIQYARKHLASWGTTHMKE 258
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSG---KILEALEYARENLAPFNEEHLKE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15233170   259 LQHVLATLAFKSTTECSKYKVLFELRQWDVLVDQFKQEFCKLYGMTMEPLLNIYLQAGLSALKTPY 324
Cdd:pfam10607  78 LEKLMGLLAFPDPTDSSPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSALKTLS 143
RING-Ubox_Emp cd16659
U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and ...
 356-407 2.89e-27

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: 102.65  E-value: 2.89e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15233170 356 SKLVCYISKELMDTENPPQVLPNGYVYSTKALKEMAEKNGGKITCPRTGLVC 407
Cdd:cd16659   1 SRLVCRITGEVMNEHNPPLALPNGYVYSEKALEEMAEKNDGKVVCPRTGESF 52
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 235-323 7.49e-22

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


Pssm-ID: 214806  Cd Length: 99  Bit Score: 89.28  E-value: 7.49e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233170    235 ESYKKAIQYARKHLASWGTTH---MKELQHVLATLAFKSTTECSKYKVLFELRQWDVLVDQFKQEFCKLY-GMTMEPLLN 310
Cdd:smart00757   1 GKIEEALAYARELLAPFAKEHekfLKELEKTMALLAYPDPTEPSPYKELLSPSQREKLAEELNSAILELLhGKSSESPLE 80

                           90
                   ....*....|...
gi 15233170    311 IYLQAGLSALKTP 323
Cdd:smart00757  81 ILLSAGLAALKTL 93
COG5109 COG5109
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
168-417 4.63e-13

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


Pssm-ID: 227440 [Multi-domain]  Cd Length: 396  Bit Score: 70.04  E-value: 4.63e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233170 168 SSNIMDLVDI-DIFREAKKVIDALKNREVASALTWcADNKTRLKKSKSKFEFQLRLQEFIELVRVDTAesYKKAIQYARK 246
Cdd:COG5109 126 KDGKDEIIKIrDGFVKLKKVISGISEKSTFLLIEF-LQIEGYLSKGDTESELELYLVSHESLLLIHKR--YDEALRLCFT 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233170 247 HLASWGTTHMKELQHVLATLAFKSTTEC-SKYKVLFE---------------------LRQWDVLVDQFKQEFCKLYGMT 304
Cdd:COG5109 203 KLASFVPKHIQDVKPLLRFLVNAPTDCFrHREKELMQniqealkksligqpiedidkvNKSRKKLIELFKSEYCAANGMP 282

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233170 305 MEPLLNIYLQAGLSALktPYGLEEGCTKEDPlSQENFRKLALP----LPFSKQHHSKLVCYISKELMDTENPPQVLPNGY 380
Cdd:COG5109 283 NRSPLRELVETGTIAF--LQLSKSGSILFDK-HVDWTDDSELPmeikLPKGRHFHSLFICPVLKELCTDENPPVMLECGH 359

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15233170 381 VYSTKALKEMAEKNGGKITCPRTGLVCNYTELVKAYI 417
Cdd:COG5109 360 VISKEALSVLSQNGVLSFKCPYCPEMSKYENILRVRF 396
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 179-236 7.37e-12

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


Pssm-ID: 128914  Cd Length: 58  Bit Score: 59.89  E-value: 7.37e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 15233170    179 IFREAKKVIDALKNREVASALTWCADNKTRLKKSKSKFEFQLRLQEFIELVRVDTAES 236
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLEE 58
dRING_Rmd5p-like cd16652
Degenerated RING (dRING) finger found in Saccharomyces cerevisiae required for meiotic nuclear ...
 359-401 4.74e-07

Degenerated RING (dRING) finger found in Saccharomyces cerevisiae required for meiotic nuclear division protein 5 (Rmd5p) and similar proteins; Rmd5p, also known as glucose-induced degradation protein 2 (Gid2) or sporulation protein RMD5, is an E3 ubiquitin ligase containing a Lissencephaly type-1-like homology motif (LisH), a C-terminal to LisH motif (CTLH) domain, and a degenerated RING finger that is characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers. It forms the heterodimeric E3 ligase unit of the glucose induced degradation deficient (GID) complex with Gid9 (also known as Fyv10), which has a degenerated RING finger as well. The GID complex triggers polyubiquitylation and subsequent proteasomal degradation of the gluconeogenic enzymes fructose-1, 6-bisphosphate by fructose-1, 6-bisphosphatase (FBPase), phosphoenolpyruvate carboxykinase (PEPCK), and cytoplasmic malate dehydrogenase (c-MDH). Moreover, Rmd5p can form the GID complex with the other six Gid proteins, including Gid1/Vid30, Gid4/Vid24, Gid5/Vid28, Gid7, Gid8, and Gid9/Fyv10. The GID complex in which the seven Gid proteins reside functions as a novel ubiquitin ligase (E3) involved in the regulation of carbohydrate metabolism.


Pssm-ID: 438314  Cd Length: 49  Bit Score: 46.09  E-value: 4.74e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 15233170 359 VCYISKELMDTENPPQVLPNGYVYSTKALKEMAEKNGGKITCP 401
Cdd:cd16652   2 ACPVSREQSTEENPPMRLPCGHVISKDSLKKLSKNNGNKFKCP 44
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
 360-401 2.29e-04

RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.


Pssm-ID: 463881 [Multi-domain]  Cd Length: 38  Bit Score: 38.54  E-value: 2.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 15233170   360 CYISKELMDteNPpqVLPNGYVYSTKALKEMAEKNGGKITCP 401
Cdd:pfam13445   1 CPICLELFT--DP--VLPCGHTFCRECLEEMSQKKGGKFKCP 38
 
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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