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Conserved domains on  [gi|661860325|ref|NP_001284362|]
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E3 ubiquitin-protein transferase MAEA isoform 6 [Homo sapiens]

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

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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 ...
 112-253 3.10e-51

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: 166.98  E-value: 3.10e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661860325  112 FLTAKEVEESLERRETATCLAWCHDNKSRLRKMKSCLEFSLRIQEFIELIRQNKRLDAVRHARKHFSQAEGSQLDEVRQA 191
Cdd:pfam10607   2 FKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGKILEALEYARENLAPFNEEHLKELEKL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 661860325  192 MGMLAFPPDTHISPYKDLLDPARWRMLIQQFRYDNYRLHQLGNNSVFTLTLQAGLSAIKTPQ 253
Cdd:pfam10607  82 MGLLAFPDPTDSSPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSALKTLS 143
RING-Ubox_Emp cd16659
U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and ...
 288-337 2.08e-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: 101.88  E-value: 2.08e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 661860325 288 SRLVCKISGDVMNENNPPMMLPNGYVYGYNSLLSIRQ--DDKVVCPRTKEVF 337
Cdd:cd16659    1 SRLVCRITGEVMNEHNPPLALPNGYVYSEKALEEMAEknDGKVVCPRTGESF 52
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 72-105 1.12e-06

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: 44.35  E-value: 1.12e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 661860325    72 WKRKRMDRMMVEHLLRCGYYNTAVKLARQSGIED 105
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
 
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 ...
 112-253 3.10e-51

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: 166.98  E-value: 3.10e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661860325  112 FLTAKEVEESLERRETATCLAWCHDNKSRLRKMKSCLEFSLRIQEFIELIRQNKRLDAVRHARKHFSQAEGSQLDEVRQA 191
Cdd:pfam10607   2 FKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGKILEALEYARENLAPFNEEHLKELEKL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 661860325  192 MGMLAFPPDTHISPYKDLLDPARWRMLIQQFRYDNYRLHQLGNNSVFTLTLQAGLSAIKTPQ 253
Cdd:pfam10607  82 MGLLAFPDPTDSSPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSALKTLS 143
RING-Ubox_Emp cd16659
U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and ...
 288-337 2.08e-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: 101.88  E-value: 2.08e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 661860325 288 SRLVCKISGDVMNENNPPMMLPNGYVYGYNSLLSIRQ--DDKVVCPRTKEVF 337
Cdd:cd16659    1 SRLVCRITGEVMNEHNPPLALPNGYVYSEKALEEMAEknDGKVVCPRTGESF 52
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 164-256 2.06e-16

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


Pssm-ID: 214806  Cd Length: 99  Bit Score: 73.87  E-value: 2.06e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661860325   164 NKRLDAVRHARKHFSQAEGSQ---LDEVRQAMGMLAFPPDTHISPYKDLLDPARWRMLIQQFRYD--NYrLHQLGNNSVF 238
Cdd:smart00757   1 GKIEEALAYARELLAPFAKEHekfLKELEKTMALLAYPDPTEPSPYKELLSPSQREKLAEELNSAilEL-LHGKSSESPL 79

                           90
                   ....*....|....*...
gi 661860325   239 TLTLQAGLSAIKTPQCYK 256
Cdd:smart00757  80 EILLSAGLAALKTLLEKG 97
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 72-105 1.12e-06

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: 44.35  E-value: 1.12e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 661860325    72 WKRKRMDRMMVEHLLRCGYYNTAVKLARQSGIED 105
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
COG5109 COG5109
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
73-347 6.06e-03

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


Pssm-ID: 227440 [Multi-domain]  Cd Length: 396  Bit Score: 38.07  E-value: 6.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661860325  73 KRKRMDRMMVEHLLRCGYYNTAVKLARQSGIEDLVNI-EMFLTAKEVEESLERRETATCLAWCHdNKSRLRKMKSCLEFS 151
Cdd:COG5109   99 QTVTYLVVYYLLENNCADVVERHISETKDGKDEIIKIrDGFVKLKKVISGISEKSTFLLIEFLQ-IEGYLSKGDTESELE 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661860325 152 LRIQEFIELIRQNKRLD-AVRHARKHFSQAEGSQLDEVRQAMGMLAFPP-DTHISPYKDLLD------------------ 211
Cdd:COG5109  178 LYLVSHESLLLIHKRYDeALRLCFTKLASFVPKHIQDVKPLLRFLVNAPtDCFRHREKELMQniqealkksligqpiedi 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661860325 212 ---PARWRMLIQQFRYDNYRLHQLGNNSVFTLTLQAGLSAIktPQCYKEDGSSKSPDCPVCSRSLNKLAQPLPMAHCANS 288
Cdd:COG5109  258 dkvNKSRKKLIELFKSEYCAANGMPNRSPLRELVETGTIAF--LQLSKSGSILFDKHVDWTDDSELPMEIKLPKGRHFHS 335

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 661860325 289 RLVCKISGDVMNENNPPMMLPNGYVYGYNSLLSIRQDDKVV--CPRTKEVFHFSQAEKVYI 347
Cdd:COG5109  336 LFICPVLKELCTDENPPVMLECGHVISKEALSVLSQNGVLSfkCPYCPEMSKYENILRVRF 396
 
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 ...
 112-253 3.10e-51

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: 166.98  E-value: 3.10e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661860325  112 FLTAKEVEESLERRETATCLAWCHDNKSRLRKMKSCLEFSLRIQEFIELIRQNKRLDAVRHARKHFSQAEGSQLDEVRQA 191
Cdd:pfam10607   2 FKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGKILEALEYARENLAPFNEEHLKELEKL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 661860325  192 MGMLAFPPDTHISPYKDLLDPARWRMLIQQFRYDNYRLHQLGNNSVFTLTLQAGLSAIKTPQ 253
Cdd:pfam10607  82 MGLLAFPDPTDSSPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSALKTLS 143
RING-Ubox_Emp cd16659
U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and ...
 288-337 2.08e-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: 101.88  E-value: 2.08e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 661860325 288 SRLVCKISGDVMNENNPPMMLPNGYVYGYNSLLSIRQ--DDKVVCPRTKEVF 337
Cdd:cd16659    1 SRLVCRITGEVMNEHNPPLALPNGYVYSEKALEEMAEknDGKVVCPRTGESF 52
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 164-256 2.06e-16

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


Pssm-ID: 214806  Cd Length: 99  Bit Score: 73.87  E-value: 2.06e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661860325   164 NKRLDAVRHARKHFSQAEGSQ---LDEVRQAMGMLAFPPDTHISPYKDLLDPARWRMLIQQFRYD--NYrLHQLGNNSVF 238
Cdd:smart00757   1 GKIEEALAYARELLAPFAKEHekfLKELEKTMALLAYPDPTEPSPYKELLSPSQREKLAEELNSAilEL-LHGKSSESPL 79

                           90
                   ....*....|....*...
gi 661860325   239 TLTLQAGLSAIKTPQCYK 256
Cdd:smart00757  80 EILLSAGLAALKTLLEKG 97
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 111-168 5.73e-14

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


Pssm-ID: 128914  Cd Length: 58  Bit Score: 65.67  E-value: 5.73e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 661860325   111 MFLTAKEVEESLERRETATCLAWCHDNKSRLRKMKSCLEFSLRIQEFIELIRQNKRLD 168
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLEE 58
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
 290-337 1.45e-07

U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that also includes the HECT family and the RING finger family. The E3 enzyme is ubiquitin-protein ligase that cooperates with a ubiquitin-activating enzyme (E1) and a ubiquitin-conjugating enzyme (E2), and plays a central role in determining the specificity of the ubiquitination system. It removes the ubiquitin molecule from the E2 enzyme and attaches it to the target substrate, forming a covalent bond between ubiquitin and the target. U-box proteins are characterized by the presence of a U-box domain of approximately 70 amino acids. The U-box is a modified form of the RING finger domain that lacks metal chelating cysteines and histidines. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms.


Pssm-ID: 438117 [Multi-domain]  Cd Length: 44  Bit Score: 47.16  E-value: 1.45e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 661860325 290 LVCKISGDVMNEnnpPMMLPNGYVYGYNSLLSIRQDDKvVCPRTKEVF 337
Cdd:cd16453    1 FLCPISGELMKD---PVITPSGITYDRSAIERWLLSDN-TDPFTREPL 44
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 72-105 1.12e-06

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: 44.35  E-value: 1.12e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 661860325    72 WKRKRMDRMMVEHLLRCGYYNTAVKLARQSGIED 105
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
dRING_Rmd5p-like cd16652
Degenerated RING (dRING) finger found in Saccharomyces cerevisiae required for meiotic nuclear ...
 291-331 1.04e-03

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: 36.46  E-value: 1.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 661860325 291 VCKISGDVMNENNPPMMLPNGYVYGYNSL--LSIRQDDKVVCP 331
Cdd:cd16652    2 ACPVSREQSTEENPPMRLPCGHVISKDSLkkLSKNNGNKFKCP 44
COG5109 COG5109
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
73-347 6.06e-03

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


Pssm-ID: 227440 [Multi-domain]  Cd Length: 396  Bit Score: 38.07  E-value: 6.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661860325  73 KRKRMDRMMVEHLLRCGYYNTAVKLARQSGIEDLVNI-EMFLTAKEVEESLERRETATCLAWCHdNKSRLRKMKSCLEFS 151
Cdd:COG5109   99 QTVTYLVVYYLLENNCADVVERHISETKDGKDEIIKIrDGFVKLKKVISGISEKSTFLLIEFLQ-IEGYLSKGDTESELE 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661860325 152 LRIQEFIELIRQNKRLD-AVRHARKHFSQAEGSQLDEVRQAMGMLAFPP-DTHISPYKDLLD------------------ 211
Cdd:COG5109  178 LYLVSHESLLLIHKRYDeALRLCFTKLASFVPKHIQDVKPLLRFLVNAPtDCFRHREKELMQniqealkksligqpiedi 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661860325 212 ---PARWRMLIQQFRYDNYRLHQLGNNSVFTLTLQAGLSAIktPQCYKEDGSSKSPDCPVCSRSLNKLAQPLPMAHCANS 288
Cdd:COG5109  258 dkvNKSRKKLIELFKSEYCAANGMPNRSPLRELVETGTIAF--LQLSKSGSILFDKHVDWTDDSELPMEIKLPKGRHFHS 335

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 661860325 289 RLVCKISGDVMNENNPPMMLPNGYVYGYNSLLSIRQDDKVV--CPRTKEVFHFSQAEKVYI 347
Cdd:COG5109  336 LFICPVLKELCTDENPPVMLECGHVISKEALSVLSQNGVLSfkCPYCPEMSKYENILRVRF 396
 
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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