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Conserved domains on  [gi|1776070578|ref|XP_031443919|]
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ancient ubiquitous protein 1 [Phasianus colchicus]

Protein Classification

lipid droplet-regulating VLDL assembly factor AUP1( domain architecture ID 10353897)

lipid droplet-regulating VLDL assembly factor AUP1 (ancient ubiquitous protein 1) plays a role in the translocation of terminally misfolded proteins from the endoplasmic reticulum lumen to the cytoplasm and their degradation by the proteasome

CATH:  1.10.8.10
Gene Symbol:  AUP1
Gene Ontology:  GO:0043130|GO:0016020
PubMed:  21127063|12042322|12628920|12787494
SCOP:  4003786

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LPLAT super family cl17185
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
 66-265 5.88e-28

Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; Lysophospholipid acyltransferase (LPLAT) superfamily members are acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis. These proteins catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this superfamily are LPLATs such as glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB), 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), lysophosphatidylcholine acyltransferase 1 (LPCAT-1), lysophosphatidylethanolamine acyltransferase (LPEAT, also known as, MBOAT2, membrane-bound O-acyltransferase domain-containing protein 2), lipid A biosynthesis lauroyl/myristoyl acyltransferase, 2-acylglycerol O-acyltransferase (MGAT), dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and Tafazzin (the protein product of the Barth syndrome (TAZ) gene).


The actual alignment was detected with superfamily member cd07991:

Pssm-ID: 473073 [Multi-domain]  Cd Length: 211  Bit Score: 110.00  E-value: 5.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776070578  66 VRVMCSVLGLF-VQQSGPRPRDAAVQVYIANHVTHFDHnVInlLTSCNTPAL-----NGAPGFICWSrgfmeLGVTG--- 136
Cdd:cd07991     1 ARVLLFAFGFYvIKVHGKPDPPEAPRIIVANHTSFIDP-LI--LFSDLFPSIvakkeLGKLPFIGTI-----LRALGcif 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776070578 137 -------SRAELVDSLKAYSSHRGNPPLLLFPEEAATNGRAgLLRFSSWPFSILDVVQPVALQVQRPLITVSVADSSWIT 209
Cdd:cd07991    73 vdrsepkDRKKVVEEIKERATDPNWPPILIFPEGTTTNGKA-LIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSS 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1776070578 210 E--LFWTFFVPFTVYQVRWMPSV-PRRAEELSEDFALRVQELLAMELGVVSTQLTAADK 265
Cdd:cd07991   152 LmyLFRLLTQPANVLEVEFLPVYtPSEEGEDPKEFANRVRLIMANKLGLPATDWTGEDK 210
CUE_AUP1 cd14420
CUE domain found in ancient ubiquitous protein 1 (AUP1) and similar proteins; AUP1 is a ...
 310-354 1.51e-24

CUE domain found in ancient ubiquitous protein 1 (AUP1) and similar proteins; AUP1 is a component of the HRD1-SEL1L endoplasmic reticulum (ER) quality control complex and is essential for US11-mediated dislocation of class I MHC heavy chains. It also binds to the membrane-proximal KVGFFKR motif of the cytoplasmic tail of the integrin alphaCTs that plays a crucial role in the inside-out signaling of alpha(IIb)beta(3). AUP1 is found in both the ER and in lipid droplets. It contains two conserved cytoplasmic domains, an acyltransferase domain, a CUE domain and an E2 ubiquitin conjugase G2 (Ube2g2)-binding domain (G2BR). The acyltransferase domain transfers fatty acids onto phospholipids and CUE domain participates in ubiquitin binding or in recruitment of ubiquitin-conjugating enzymes to the site of dislocation.


:

Pssm-ID: 270603  Cd Length: 45  Bit Score: 95.37  E-value: 1.51e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1776070578 310 RITTMAQQVKEVLPHVPLEVIRTDLAQTNCVDTTIANLLEGRVPF 354
Cdd:cd14420     1 RLARMAQQVKEVLPHVPLHVIRRDLEKTRNVDTTITNILEGRVKF 45
 
Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 66-265 5.88e-28

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lysophosphatidylcholine acyltransferase 1 (LPCAT-1), glycerol-3-phosphate acyltransferase 3 (GPAT3), and similar sequences.


Pssm-ID: 153253 [Multi-domain]  Cd Length: 211  Bit Score: 110.00  E-value: 5.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776070578  66 VRVMCSVLGLF-VQQSGPRPRDAAVQVYIANHVTHFDHnVInlLTSCNTPAL-----NGAPGFICWSrgfmeLGVTG--- 136
Cdd:cd07991     1 ARVLLFAFGFYvIKVHGKPDPPEAPRIIVANHTSFIDP-LI--LFSDLFPSIvakkeLGKLPFIGTI-----LRALGcif 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776070578 137 -------SRAELVDSLKAYSSHRGNPPLLLFPEEAATNGRAgLLRFSSWPFSILDVVQPVALQVQRPLITVSVADSSWIT 209
Cdd:cd07991    73 vdrsepkDRKKVVEEIKERATDPNWPPILIFPEGTTTNGKA-LIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSS 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1776070578 210 E--LFWTFFVPFTVYQVRWMPSV-PRRAEELSEDFALRVQELLAMELGVVSTQLTAADK 265
Cdd:cd07991   152 LmyLFRLLTQPANVLEVEFLPVYtPSEEGEDPKEFANRVRLIMANKLGLPATDWTGEDK 210
CUE_AUP1 cd14420
CUE domain found in ancient ubiquitous protein 1 (AUP1) and similar proteins; AUP1 is a ...
 310-354 1.51e-24

CUE domain found in ancient ubiquitous protein 1 (AUP1) and similar proteins; AUP1 is a component of the HRD1-SEL1L endoplasmic reticulum (ER) quality control complex and is essential for US11-mediated dislocation of class I MHC heavy chains. It also binds to the membrane-proximal KVGFFKR motif of the cytoplasmic tail of the integrin alphaCTs that plays a crucial role in the inside-out signaling of alpha(IIb)beta(3). AUP1 is found in both the ER and in lipid droplets. It contains two conserved cytoplasmic domains, an acyltransferase domain, a CUE domain and an E2 ubiquitin conjugase G2 (Ube2g2)-binding domain (G2BR). The acyltransferase domain transfers fatty acids onto phospholipids and CUE domain participates in ubiquitin binding or in recruitment of ubiquitin-conjugating enzymes to the site of dislocation.


Pssm-ID: 270603  Cd Length: 45  Bit Score: 95.37  E-value: 1.51e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1776070578 310 RITTMAQQVKEVLPHVPLEVIRTDLAQTNCVDTTIANLLEGRVPF 354
Cdd:cd14420     1 RLARMAQQVKEVLPHVPLHVIRRDLEKTRNVDTTITNILEGRVKF 45
CUE pfam02845
CUE domain; CUE domains have been shown to bind ubiquitin. It has been suggested that CUE ...
 314-351 9.74e-09

CUE domain; CUE domains have been shown to bind ubiquitin. It has been suggested that CUE domains are related to pfam00627 and this has been confirmed by the structure of the domain. CUE domains also occur in two protein of the IL-1 signal transduction pathway, tollip and TAB2.


Pssm-ID: 427018  Cd Length: 42  Bit Score: 50.94  E-value: 9.74e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1776070578 314 MAQQVKEVLPHVPLEVIRTDL-AQTNCVDTTIANLLEGR 351
Cdd:pfam02845   4 MLETLKEMFPDLDEEVIRAVLeASNGNVEAAINALLEGS 42
CUE smart00546
Domain that may be involved in binding ubiquitin-conjugating enzymes (UBCs); CUE domains also ...
 311-351 6.65e-08

Domain that may be involved in binding ubiquitin-conjugating enzymes (UBCs); CUE domains also occur in two protein of the IL-1 signal transduction pathway, tollip and TAB2. Ponting (Biochem. J.) "Proteins of the Endoplasmic reticulum" (in press)


Pssm-ID: 214715  Cd Length: 43  Bit Score: 48.64  E-value: 6.65e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1776070578  311 ITTMAQQVKEVLPHVPLEVIRTDL-AQTNCVDTTIANLLEGR 351
Cdd:smart00546   2 NDEALHDLKEMFPNLDEEVIEAVLeANTGNVEATINNLLEGS 43
PLN02833 PLN02833
glycerol acyltransferase family protein
 22-255 1.16e-05

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 47.08  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776070578  22 GFVLLALLLYaPVGLCLLV------LRLFIGVHVFLVGCILPDGMLRRLiVRVMCSVL----GLFVQQSGPRPRDAAVQV 91
Cdd:PLN02833   89 GVVIRYGILF-PVRVLLLAigwiifLSAFIPVHFLLKGHKLRKKIERKL-VELICSAFvaswTGVIKYHGPRPSRRPKQV 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776070578  92 YIANHVTHFDHNVINLLTSCNTpALNGAPGFIcwsrGFMELGVTGS-------RAELVD------SLKAYSSHRGNPPLL 158
Cdd:PLN02833  167 FVANHTSMIDFIVLEQMTPFAV-IMQKHPGWV----GFLQNTILESvgciwfnRTEAKDrevvakKLRDHVQDPDRNPLL 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776070578 159 LFPEEAATNGRAGLLrFSSWPFSILDVVQPVALQVQRPLItvsvadsswitELFW-TFFVPFTVYQVRWMPS-------- 229
Cdd:PLN02833  242 IFPEGTCVNNEYTVM-FKKGAFELGCTVCPIAIKYNKIFV-----------DAFWnSRKQSFTMHLLRLMTSwavvcdvw 309

                         250       260       270
                  ....*....|....*....|....*....|
gi 1776070578 230 --VPR--RAEELSEDFALRVQELLAMELGV 255
Cdd:PLN02833  310 ylEPQtlRPGETPIEFAERVRDMIAKRAGL 339
 
Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 66-265 5.88e-28

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lysophosphatidylcholine acyltransferase 1 (LPCAT-1), glycerol-3-phosphate acyltransferase 3 (GPAT3), and similar sequences.


Pssm-ID: 153253 [Multi-domain]  Cd Length: 211  Bit Score: 110.00  E-value: 5.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776070578  66 VRVMCSVLGLF-VQQSGPRPRDAAVQVYIANHVTHFDHnVInlLTSCNTPAL-----NGAPGFICWSrgfmeLGVTG--- 136
Cdd:cd07991     1 ARVLLFAFGFYvIKVHGKPDPPEAPRIIVANHTSFIDP-LI--LFSDLFPSIvakkeLGKLPFIGTI-----LRALGcif 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776070578 137 -------SRAELVDSLKAYSSHRGNPPLLLFPEEAATNGRAgLLRFSSWPFSILDVVQPVALQVQRPLITVSVADSSWIT 209
Cdd:cd07991    73 vdrsepkDRKKVVEEIKERATDPNWPPILIFPEGTTTNGKA-LIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSS 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1776070578 210 E--LFWTFFVPFTVYQVRWMPSV-PRRAEELSEDFALRVQELLAMELGVVSTQLTAADK 265
Cdd:cd07991   152 LmyLFRLLTQPANVLEVEFLPVYtPSEEGEDPKEFANRVRLIMANKLGLPATDWTGEDK 210
CUE_AUP1 cd14420
CUE domain found in ancient ubiquitous protein 1 (AUP1) and similar proteins; AUP1 is a ...
 310-354 1.51e-24

CUE domain found in ancient ubiquitous protein 1 (AUP1) and similar proteins; AUP1 is a component of the HRD1-SEL1L endoplasmic reticulum (ER) quality control complex and is essential for US11-mediated dislocation of class I MHC heavy chains. It also binds to the membrane-proximal KVGFFKR motif of the cytoplasmic tail of the integrin alphaCTs that plays a crucial role in the inside-out signaling of alpha(IIb)beta(3). AUP1 is found in both the ER and in lipid droplets. It contains two conserved cytoplasmic domains, an acyltransferase domain, a CUE domain and an E2 ubiquitin conjugase G2 (Ube2g2)-binding domain (G2BR). The acyltransferase domain transfers fatty acids onto phospholipids and CUE domain participates in ubiquitin binding or in recruitment of ubiquitin-conjugating enzymes to the site of dislocation.


Pssm-ID: 270603  Cd Length: 45  Bit Score: 95.37  E-value: 1.51e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1776070578 310 RITTMAQQVKEVLPHVPLEVIRTDLAQTNCVDTTIANLLEGRVPF 354
Cdd:cd14420     1 RLARMAQQVKEVLPHVPLHVIRRDLEKTRNVDTTITNILEGRVKF 45
CUE_AUP1_AMFR_like cd14376
CUE domain found in ancient ubiquitous protein 1 (AUP1), autocrine motility factor receptor ...
 312-348 1.90e-12

CUE domain found in ancient ubiquitous protein 1 (AUP1), autocrine motility factor receptor (AMFR) and similar proteins; AUP1 is a component of the HRD1-SEL1L endoplasmic reticulum (ER) quality control complex and is essential for US11-mediated dislocation of class I MHC heavy chains. AMFR is an internalizing cell surface glycoprotein that is localized in both plasma membrane caveolae and the ER, and involves in the regulation of cellular adhesion, proliferation, motility and apoptosis, as well as in the process of learning and memory. Cue1p is an N-terminally membrane-anchored endoplasmic reticulum (ER) protein essential for the activity of the two major yeast RING finger ubiquitin ligases (E3s) implicated in ER-associated degradation (ERAD). This family also includes plant E3 ubiquitin protein ligases RIN2, RIN3, and similar proteins. Comparing with other CUE domain-containing proteins, some family members from higher eukaryotes do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains.


Pssm-ID: 270559  Cd Length: 37  Bit Score: 61.34  E-value: 1.90e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1776070578 312 TTMAQQVKEVLPHVPLEVIRTDLAQTNCVDTTIANLL 348
Cdd:cd14376     1 EEMVEQVQEVFPHIPREAIRRDLQRTNSVDLTINNIL 37
CUE_AMFR cd14421
CUE domain found in autocrine motility factor receptor (AMFR) and similar proteins; AMFR is an ...
 313-352 6.27e-11

CUE domain found in autocrine motility factor receptor (AMFR) and similar proteins; AMFR is an internalizing cell surface glycoprotein that is localized in both plasma membrane caveolae and the endoplasmic reticulum (ER), and involves in the regulation of cellular adhesion, proliferation, motility and apoptosis, as well as in the process of learning and memory. It is also called ER-protein gp78 that has been identified as a RING finger-dependent ubiquitin protein ligase (E3) implicated in degradation from the ER. AMFR contains an N-terminal RING-finger domain and a C-terminal CUE domain.


Pssm-ID: 270604  Cd Length: 41  Bit Score: 56.89  E-value: 6.27e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1776070578 313 TMAQQVKEVLPHVPLEVIRTDLAQTNCVDTTIANLLEGRV 352
Cdd:cd14421     2 AMAHQVQEMFPQVPLSVILADLRLTRSVEVTIENILEGRL 41
CUE_RIN3_plant cd14422
CUE domain found in plant E3 ubiquitin protein ligases RIN2, RIN3 and similar proteins; RIN2 ...
 311-348 7.86e-09

CUE domain found in plant E3 ubiquitin protein ligases RIN2, RIN3 and similar proteins; RIN2 and RIN3 are two closely related RPM1-interacting proteins conserved in higher eukaryotes. They are orthologs of the mammalian autocrine motility factor receptor (AMFR), a cytokine receptor localized in both plasma membrane caveolae and the endoplasmic reticulum (ER). RIN2 and RIN3 have been identified as membrane-bound RING-finger type ubiquitin ligases with six apparent transmembrane domains, a RING-finger domain and a CUE domain. They act as positive regulators of RPM1- and RPS2-dependent hypersensitive response (HR).


Pssm-ID: 270605  Cd Length: 38  Bit Score: 51.14  E-value: 7.86e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1776070578 311 ITTMAQQVKEVLPHVPLEVIRTDLAQTNCVDTTIANLL 348
Cdd:cd14422     1 ILAMVGMVREVLPHVPDEIIFQDLQRTNSVTATVNNLL 38
CUE pfam02845
CUE domain; CUE domains have been shown to bind ubiquitin. It has been suggested that CUE ...
 314-351 9.74e-09

CUE domain; CUE domains have been shown to bind ubiquitin. It has been suggested that CUE domains are related to pfam00627 and this has been confirmed by the structure of the domain. CUE domains also occur in two protein of the IL-1 signal transduction pathway, tollip and TAB2.


Pssm-ID: 427018  Cd Length: 42  Bit Score: 50.94  E-value: 9.74e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1776070578 314 MAQQVKEVLPHVPLEVIRTDL-AQTNCVDTTIANLLEGR 351
Cdd:pfam02845   4 MLETLKEMFPDLDEEVIRAVLeASNGNVEAAINALLEGS 42
CUE smart00546
Domain that may be involved in binding ubiquitin-conjugating enzymes (UBCs); CUE domains also ...
 311-351 6.65e-08

Domain that may be involved in binding ubiquitin-conjugating enzymes (UBCs); CUE domains also occur in two protein of the IL-1 signal transduction pathway, tollip and TAB2. Ponting (Biochem. J.) "Proteins of the Endoplasmic reticulum" (in press)


Pssm-ID: 214715  Cd Length: 43  Bit Score: 48.64  E-value: 6.65e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1776070578  311 ITTMAQQVKEVLPHVPLEVIRTDL-AQTNCVDTTIANLLEGR 351
Cdd:smart00546   2 NDEALHDLKEMFPNLDEEVIEAVLeANTGNVEATINNLLEGS 43
PLN02833 PLN02833
glycerol acyltransferase family protein
 22-255 1.16e-05

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 47.08  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776070578  22 GFVLLALLLYaPVGLCLLV------LRLFIGVHVFLVGCILPDGMLRRLiVRVMCSVL----GLFVQQSGPRPRDAAVQV 91
Cdd:PLN02833   89 GVVIRYGILF-PVRVLLLAigwiifLSAFIPVHFLLKGHKLRKKIERKL-VELICSAFvaswTGVIKYHGPRPSRRPKQV 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776070578  92 YIANHVTHFDHNVINLLTSCNTpALNGAPGFIcwsrGFMELGVTGS-------RAELVD------SLKAYSSHRGNPPLL 158
Cdd:PLN02833  167 FVANHTSMIDFIVLEQMTPFAV-IMQKHPGWV----GFLQNTILESvgciwfnRTEAKDrevvakKLRDHVQDPDRNPLL 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776070578 159 LFPEEAATNGRAGLLrFSSWPFSILDVVQPVALQVQRPLItvsvadsswitELFW-TFFVPFTVYQVRWMPS-------- 229
Cdd:PLN02833  242 IFPEGTCVNNEYTVM-FKKGAFELGCTVCPIAIKYNKIFV-----------DAFWnSRKQSFTMHLLRLMTSwavvcdvw 309

                         250       260       270
                  ....*....|....*....|....*....|
gi 1776070578 230 --VPR--RAEELSEDFALRVQELLAMELGV 255
Cdd:PLN02833  310 ylEPQtlRPGETPIEFAERVRDMIAKRAGL 339
CUE_Cue1p_like cd14424
CUE domain found in yeast ubiquitin-binding protein CUE1 (Cue1p), CUE4 (Cue4p) and similar ...
 314-348 1.38e-04

CUE domain found in yeast ubiquitin-binding protein CUE1 (Cue1p), CUE4 (Cue4p) and similar proteins; Cue1p, also called coupling of ubiquitin conjugation to ER degradation protein 1 or kinetochore-defect suppressor 4, is encoded by the open reading frame (ORF) YMR264W in yeast. It is an N-terminally membrane-anchored endoplasmic reticulum (ER) protein essential for the activity of the two major yeast RING finger ubiquitin ligases (E3s) implicated in ER-associated degradation (ERAD). It interacts with the ERAD ubiquitin-conjugating enzyme (E2) Ubc7p in vivo, stimulates Ubc7p E2 activity, and further activates ER-associated protein degradation. Cue1p contains a CUE domain which binds ubiquitin much more weakly than those of other CUE domain containing proteins. It also has an Ubc7p binding-domain at the C-terminal region which is required for Ubc7p-dependent ubiquitylation and for degradation of substrates in the ER. This family also includes Cue4p, also called coupling of ubiquitin conjugation to ER degradation protein 4. It is encoded by the open reading frame (ORF) YML101C in yeast. Cue4p contains a CUE domain which shows high level of similarity with that of Cue1p.


Pssm-ID: 270607  Cd Length: 37  Bit Score: 39.03  E-value: 1.38e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1776070578 314 MAQQVKEVLPHVPLEVIRTDLAQTNCVDTTIANLL 348
Cdd:cd14424     3 MIESVQTMFPQLSVAQIRYDLLRTGSVEATVERIL 37
CUE cd14279
CUE domain found in ubiquitin-binding CUE proteins; This family includes many coupling of ...
 316-348 4.05e-03

CUE domain found in ubiquitin-binding CUE proteins; This family includes many coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domain containing proteins that are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. CUE domains form three-helix bundle structures and are distantly related to the ubiquitin-associated (UBA) domains which are widely occurring ubiquitin-binding motifs found in a broad range of cellular proteins in species ranging from yeast to human. The majority of family members contain one CUE domain, but some family members from fungi harbor two CUE domains.


Pssm-ID: 270465  Cd Length: 38  Bit Score: 34.75  E-value: 4.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1776070578 316 QQVKEVLPHVPLEVIRTDLAQTNC-VDTTIANLL 348
Cdd:cd14279     5 EQLQEMFPDLDEEVLEDVLEANNGdVEAAIDALL 38
LPLAT_AGPAT-like cd07989
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ...
 66-247 6.57e-03

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), Tafazzin (product of Barth syndrome gene), and similar proteins.


Pssm-ID: 153251 [Multi-domain]  Cd Length: 184  Bit Score: 37.64  E-value: 6.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776070578  66 VRVMCSVLGLFVQQSG--PRPRDAAVqVYIANHVTHFDHNVINLltscntpALNGAPGFIC----WSRGFMELGVTGSRA 139
Cdd:cd07989     1 LRLLLRLLGVRVRVEGleNLPPKGPV-IIVANHQSYLDPLVLGA-------ALPRPIRFVAkkelFKIPFLGWLLRLLGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776070578 140 ELVDSLKAYSSH----------RGNPPLLLFPeEAATNGRAGLLRFSSWPFSIldvvqpvALQVQRPLITVSVADSSWIT 209
Cdd:cd07989    73 IPIDRGNGRSARealreaiealKEGESVVIFP-EGTRSRDGELLPFKSGAFRL-------AKEAGVPIVPVAISGTWGSL 144

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1776070578 210 ELFWTFFVPFTVYqVRWMPSVPRRAEELSEDFALRVQE 247
Cdd:cd07989   145 PKGKKLPRPGRVT-VRIGEPIPPEGLELAEEDRKELRE 181
 
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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