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Conserved domains on  [gi|571031354|ref|NP_001275723|]
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E3 ubiquitin-protein transferase RMND5B isoform a [Homo sapiens]

Protein Classification

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 ...
155-299 3.03e-45

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: 152.73  E-value: 3.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571031354  155 PFLELNRILEALHEQDLGPALEWAVSHRQRLLELNSSLEFKLHRLHFIRLLAGGpaKQLEALSYAR-HFQPFARLHQREI 233
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSG--KILEALEYAReNLAPFNEEHLKEL 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 571031354  234 QVMMGSLVYLRLgLEKSPYCHLLDSSHWAEICETFTRDACSLLGLSVESPLSVSFASGCVALPVLM 299
Cdd:pfam10607  79 EKLMGLLAFPDP-TDSSPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSALKTLS 143
dRING_RMD5B cd16795
Degenerated RING finger found in protein RMD5 homolog B (RMD5B); RMD5B is one of the ...
335-393 5.78e-42

Degenerated RING finger found in protein RMD5 homolog B (RMD5B); RMD5B is one of the vertebrate homologs of yeast Rmd5p. The biological function of RMD5B remains unclear. RMD5B contains 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.


:

Pssm-ID: 438449  Cd Length: 59  Bit Score: 141.30  E-value: 5.78e-42
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 571031354 335 VFACPILRQQTSDSNPPIKLICGHVISRDALNKLINGGKLKCPYCPMEQNPADGKRIIF 393
Cdd:cd16795    1 VFACPILRQQTTDSNPPMKLICGHVISRDALNKLINGGKLKCPYCPMEQNPADAKRIYF 59
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
116-148 2.14e-03

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: 35.49  E-value: 2.14e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 571031354   116 QQQILQMAIVEHLYQQGMLSVAEELCQESTLNV 148
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGLSL 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 ...
155-299 3.03e-45

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: 152.73  E-value: 3.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571031354  155 PFLELNRILEALHEQDLGPALEWAVSHRQRLLELNSSLEFKLHRLHFIRLLAGGpaKQLEALSYAR-HFQPFARLHQREI 233
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSG--KILEALEYAReNLAPFNEEHLKEL 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 571031354  234 QVMMGSLVYLRLgLEKSPYCHLLDSSHWAEICETFTRDACSLLGLSVESPLSVSFASGCVALPVLM 299
Cdd:pfam10607  79 EKLMGLLAFPDP-TDSSPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSALKTLS 143
dRING_RMD5B cd16795
Degenerated RING finger found in protein RMD5 homolog B (RMD5B); RMD5B is one of the ...
335-393 5.78e-42

Degenerated RING finger found in protein RMD5 homolog B (RMD5B); RMD5B is one of the vertebrate homologs of yeast Rmd5p. The biological function of RMD5B remains unclear. RMD5B contains 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.


Pssm-ID: 438449  Cd Length: 59  Bit Score: 141.30  E-value: 5.78e-42
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 571031354 335 VFACPILRQQTSDSNPPIKLICGHVISRDALNKLINGGKLKCPYCPMEQNPADGKRIIF 393
Cdd:cd16795    1 VFACPILRQQTTDSNPPMKLICGHVISRDALNKLINGGKLKCPYCPMEQNPADAKRIYF 59
COG5109 COG5109
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
60-393 7.74e-35

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


Pssm-ID: 227440 [Multi-domain]  Cd Length: 396  Bit Score: 132.44  E-value: 7.74e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571031354  60 VMSQCCRKIKDTVQKLASDHKDIHSSVSRVGKAIDR--NFDSEICGVVSDAVWDAREqqqqiLQMAIVEHLYQQGMLSVA 137
Cdd:COG5109   46 IRSALSLKNGQEFDTLSHAEADLVGSWKSLLKEDCRpaNFDVQVGNQIYPFSTQTVT-----YLVVYYLLENNCADVVER 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571031354 138 EELCQESTLNVDLDFKQPFLELNRILEALHEQDLGPALEWAvSHRQRLLELNSSLEFKLHRLHFIRLLAGGPAkQLEALS 217
Cdd:COG5109  121 HISETKDGKDEIIKIRDGFVKLKKVISGISEKSTFLLIEFL-QIEGYLSKGDTESELELYLVSHESLLLIHKR-YDEALR 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571031354 218 YAR-HFQPFARLHQREIQVMMGSLVYLRLGLEKSPYCHLLDSSH---------------------WAEICETFTRDACSL 275
Cdd:COG5109  199 LCFtKLASFVPKHIQDVKPLLRFLVNAPTDCFRHREKELMQNIQealkksligqpiedidkvnksRKKLIELFKSEYCAA 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571031354 276 LGLSVESPLSVSFASGCVALPVLMNIKAVIEQRQCTgvWNHKDELPIEIELGMKCWYHSVFACPILRQQTSDSNPPIKLI 355
Cdd:COG5109  279 NGMPNRSPLRELVETGTIAFLQLSKSGSILFDKHVD--WTDDSELPMEIKLPKGRHFHSLFICPVLKELCTDENPPVMLE 356
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 571031354 356 CGHVISRDALNKLINGGKL--KCPYCPMEQNPADGKRIIF 393
Cdd:COG5109  357 CGHVISKEALSVLSQNGVLsfKCPYCPEMSKYENILRVRF 396
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
211-304 1.09e-19

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


Pssm-ID: 214806  Cd Length: 99  Bit Score: 83.11  E-value: 1.09e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571031354   211 KQLEALSYAR-HFQPFARLH---QREIQVMMGSLVYLRLgLEKSPYCHLLDSSHWAEICETFTRDACSLL-GLSVESPLS 285
Cdd:smart00757   2 KIEEALAYAReLLAPFAKEHekfLKELEKTMALLAYPDP-TEPSPYKELLSPSQREKLAEELNSAILELLhGKSSESPLE 80
                           90
                   ....*....|....*....
gi 571031354   286 VSFASGCVALPVLMNIKAV 304
Cdd:smart00757  81 ILLSAGLAALKTLLEKGGV 99
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
116-148 2.14e-03

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: 35.49  E-value: 2.14e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 571031354   116 QQQILQMAIVEHLYQQGMLSVAEELCQESTLNV 148
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGLSL 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 ...
155-299 3.03e-45

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: 152.73  E-value: 3.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571031354  155 PFLELNRILEALHEQDLGPALEWAVSHRQRLLELNSSLEFKLHRLHFIRLLAGGpaKQLEALSYAR-HFQPFARLHQREI 233
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSG--KILEALEYAReNLAPFNEEHLKEL 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 571031354  234 QVMMGSLVYLRLgLEKSPYCHLLDSSHWAEICETFTRDACSLLGLSVESPLSVSFASGCVALPVLM 299
Cdd:pfam10607  79 EKLMGLLAFPDP-TDSSPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSALKTLS 143
dRING_RMD5B cd16795
Degenerated RING finger found in protein RMD5 homolog B (RMD5B); RMD5B is one of the ...
335-393 5.78e-42

Degenerated RING finger found in protein RMD5 homolog B (RMD5B); RMD5B is one of the vertebrate homologs of yeast Rmd5p. The biological function of RMD5B remains unclear. RMD5B contains 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.


Pssm-ID: 438449  Cd Length: 59  Bit Score: 141.30  E-value: 5.78e-42
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 571031354 335 VFACPILRQQTSDSNPPIKLICGHVISRDALNKLINGGKLKCPYCPMEQNPADGKRIIF 393
Cdd:cd16795    1 VFACPILRQQTTDSNPPMKLICGHVISRDALNKLINGGKLKCPYCPMEQNPADAKRIYF 59
COG5109 COG5109
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
60-393 7.74e-35

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


Pssm-ID: 227440 [Multi-domain]  Cd Length: 396  Bit Score: 132.44  E-value: 7.74e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571031354  60 VMSQCCRKIKDTVQKLASDHKDIHSSVSRVGKAIDR--NFDSEICGVVSDAVWDAREqqqqiLQMAIVEHLYQQGMLSVA 137
Cdd:COG5109   46 IRSALSLKNGQEFDTLSHAEADLVGSWKSLLKEDCRpaNFDVQVGNQIYPFSTQTVT-----YLVVYYLLENNCADVVER 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571031354 138 EELCQESTLNVDLDFKQPFLELNRILEALHEQDLGPALEWAvSHRQRLLELNSSLEFKLHRLHFIRLLAGGPAkQLEALS 217
Cdd:COG5109  121 HISETKDGKDEIIKIRDGFVKLKKVISGISEKSTFLLIEFL-QIEGYLSKGDTESELELYLVSHESLLLIHKR-YDEALR 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571031354 218 YAR-HFQPFARLHQREIQVMMGSLVYLRLGLEKSPYCHLLDSSH---------------------WAEICETFTRDACSL 275
Cdd:COG5109  199 LCFtKLASFVPKHIQDVKPLLRFLVNAPTDCFRHREKELMQNIQealkksligqpiedidkvnksRKKLIELFKSEYCAA 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571031354 276 LGLSVESPLSVSFASGCVALPVLMNIKAVIEQRQCTgvWNHKDELPIEIELGMKCWYHSVFACPILRQQTSDSNPPIKLI 355
Cdd:COG5109  279 NGMPNRSPLRELVETGTIAFLQLSKSGSILFDKHVD--WTDDSELPMEIKLPKGRHFHSLFICPVLKELCTDENPPVMLE 356
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 571031354 356 CGHVISRDALNKLINGGKL--KCPYCPMEQNPADGKRIIF 393
Cdd:COG5109  357 CGHVISKEALSVLSQNGVLsfKCPYCPEMSKYENILRVRF 396
dRING_RMD5A cd16794
Degenerated RING finger found in protein RMD5 homolog A (RMD5A); RMD5A is one of the ...
334-393 1.60e-34

Degenerated RING finger found in protein RMD5 homolog A (RMD5A); RMD5A is one of the vertebrate homologs of yeast Rmd5p. The biological function of RMD5A remains unclear. RMD5A contains 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.


Pssm-ID: 438448  Cd Length: 60  Bit Score: 122.07  E-value: 1.60e-34
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 571031354 334 SVFACPILRQQTSDSNPPIKLICGHVISRDALNKLINGGKLKCPYCPMEQNPADGKRIIF 393
Cdd:cd16794    1 SIFACPILRQQTTENNPPMKLVCGHIISRDALNKMFNGSKLKCPYCPMEQSPGDAKQIFF 60
dRING_Rmd5p-like cd16652
Degenerated RING (dRING) finger found in Saccharomyces cerevisiae required for meiotic nuclear ...
336-382 1.82e-25

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: 97.32  E-value: 1.82e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 571031354 336 FACPILRQQTSDSNPPIKLICGHVISRDALNKLI--NGGKLKCPYCPME 382
Cdd:cd16652    1 FACPVSREQSTEENPPMRLPCGHVISKDSLKKLSknNGNKFKCPYCPVE 49
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
211-304 1.09e-19

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


Pssm-ID: 214806  Cd Length: 99  Bit Score: 83.11  E-value: 1.09e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571031354   211 KQLEALSYAR-HFQPFARLH---QREIQVMMGSLVYLRLgLEKSPYCHLLDSSHWAEICETFTRDACSLL-GLSVESPLS 285
Cdd:smart00757   2 KIEEALAYAReLLAPFAKEHekfLKELEKTMALLAYPDP-TEPSPYKELLSPSQREKLAEELNSAILELLhGKSSESPLE 80
                           90
                   ....*....|....*....
gi 571031354   286 VSFASGCVALPVLMNIKAV 304
Cdd:smart00757  81 ILLSAGLAALKTLLEKGGV 99
RING_Ubox cd00162
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
338-379 1.88e-12

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. 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. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enable efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438111 [Multi-domain]  Cd Length: 42  Bit Score: 61.32  E-value: 1.88e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 571031354 338 CPILRQQTSDSNPPIKLICGHVISRDALNKLINGGKLKCPYC 379
Cdd:cd00162    1 CPICREEMNDRRPVVLLSCGHTFSRSAIARWLEGSKQKCPFC 42
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
156-212 1.45e-11

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


Pssm-ID: 128914  Cd Length: 58  Bit Score: 59.12  E-value: 1.45e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 571031354   156 FLELNRILEALHEQDLGPALEWAVSHRQRLLELNSSLEFKLHRLHFIRLLAGGPAKQ 212
Cdd:smart00668   2 FDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLEE 58
RING-Ubox_Emp cd16659
U-box domain, a modified RING finger, found in erythroblast macrophage protein (Emp) and ...
334-378 8.46e-04

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: 37.17  E-value: 8.46e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 571031354 334 SVFACPILRQQTSDSNPPIKLICGHVISRDALNKL--INGGKLKCPY 378
Cdd:cd16659    1 SRLVCRITGEVMNEHNPPLALPNGYVYSEKALEEMaeKNDGKVVCPR 47
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
116-148 2.14e-03

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: 35.49  E-value: 2.14e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 571031354   116 QQQILQMAIVEHLYQQGMLSVAEELCQESTLNV 148
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
 
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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