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Conserved domains on  [gi|530406691|ref|XP_005254844|]
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ubiquitin-conjugating enzyme E2 Q2 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UBCc_UBE2Q cd23802
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Q1, ...
 207-298 3.89e-43

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Q1, Q2, and related proteins; The E2Q subfamily includes mammalian ubiquitin-conjugating enzymes E2 Q1 (UBE2Q1/NICE5/UBE2Q), Q2 (UBE2Q2), and similar proteins. They are ubiquitin-conjugating (EC 2.3.2.23) enzymes that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2Q1 may be involved in hormonal homeostasis in females. It is involved in regulation of B4GALT1 cell surface expression, B4GALT1-mediated cell adhesion to laminin and embryoid body formation. In vitro, UBE2Q2 catalyzes 'Lys-48'-linked polyubiquitination. This subfamily also includes ubiquitin-conjugating enzyme E2Q-like protein 1 (UBE2QL1), which is a probable E2 ubiquitin-protein ligase that may facilitate the monoubiquitination and degradation of MTOR and CCNE1 through interaction with FBXW7.


:

Pssm-ID: 467422  Cd Length: 157  Bit Score: 145.47  E-value: 3.89e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691 207 DRLMKELRDIYRSQSYKTGiYSVELINDSLYDWHVKLQKVDPDSPLHSDLQILKEKEGIEYILLNFSFKDNFPFDPPFVR 286
Cdd:cd23802    1 KRLMKELKDLMKSQSKKLG-FSVDPVDDNLYHWEVKLFGFDPDSPLAKDLKKLKKKHGYDYIELELRFPDLYPFYPPFVR 79

                         90
                 ....*....|..
gi 530406691 287 VVLPVLSGGLVH 298
Cdd:cd23802   80 VVRPRLKGGTGH 91
RWD super family cl02687
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
 9-89 5.59e-04

RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.


The actual alignment was detected with superfamily member pfam05773:

Pssm-ID: 413438  Cd Length: 111  Bit Score: 38.84  E-value: 5.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691    9 ELKFLASIFDKNHERFRIVSWKLDELHCQFLVPQQGSPHSLPPPLTLHCNITESYPSSSPIWFVDS----EDPNLTSVLE 84
Cdd:pfam05773   6 ELEALESIYPDEFEVISDSPYESLEIEIKLSLDSDESDSSHLPPLVLKFTLPEDYPDEPPKISLSSpwnlSDEQVLSLLE 85


                  ....*
gi 530406691   85 RLEDT 89
Cdd:pfam05773  86 ELEEL 90
 
Name Accession Description Interval E-value
UBCc_UBE2Q cd23802
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Q1, ...
 207-298 3.89e-43

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Q1, Q2, and related proteins; The E2Q subfamily includes mammalian ubiquitin-conjugating enzymes E2 Q1 (UBE2Q1/NICE5/UBE2Q), Q2 (UBE2Q2), and similar proteins. They are ubiquitin-conjugating (EC 2.3.2.23) enzymes that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2Q1 may be involved in hormonal homeostasis in females. It is involved in regulation of B4GALT1 cell surface expression, B4GALT1-mediated cell adhesion to laminin and embryoid body formation. In vitro, UBE2Q2 catalyzes 'Lys-48'-linked polyubiquitination. This subfamily also includes ubiquitin-conjugating enzyme E2Q-like protein 1 (UBE2QL1), which is a probable E2 ubiquitin-protein ligase that may facilitate the monoubiquitination and degradation of MTOR and CCNE1 through interaction with FBXW7.


Pssm-ID: 467422  Cd Length: 157  Bit Score: 145.47  E-value: 3.89e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691 207 DRLMKELRDIYRSQSYKTGiYSVELINDSLYDWHVKLQKVDPDSPLHSDLQILKEKEGIEYILLNFSFKDNFPFDPPFVR 286
Cdd:cd23802    1 KRLMKELKDLMKSQSKKLG-FSVDPVDDNLYHWEVKLFGFDPDSPLAKDLKKLKKKHGYDYIELELRFPDLYPFYPPFVR 79

                         90
                 ....*....|..
gi 530406691 287 VVLPVLSGGLVH 298
Cdd:cd23802   80 VVRPRLKGGTGH 91
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 208-314 1.01e-08

Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for proteasome-mediated degradation may be ubiquitinated. Ubiquitination follows conjugation of ubiquitin to a conserved cysteine residue of UBC homologues. This pathway functions in regulating many fundamental processes required for cell viability.TSG101 is one of several UBC homologues that lacks this active site cysteine.


Pssm-ID: 214562 [Multi-domain]  Cd Length: 145  Bit Score: 53.07  E-value: 1.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691   208 RLMKELRDIYRSQsyKTGIYSVELINDSLYDWHVKLqkVDPDSPLHSDLQILkekegieyilLNFSFKDNFPFDPPFVRV 287
Cdd:smart00212   1 RLLKELKELRKDP--PPGFTAYPVDDENLLEWTGTI--VGPPGTPYEGGVFK----------LTIEFPEDYPFKPPKVKF 66

                           90       100       110
                   ....*....|....*....|....*....|
gi 530406691   288 VLPVLsgglvHP---SKGRwlnvltvVCLD 314
Cdd:smart00212  67 ITKIY-----HPnvdSSGE-------ICLD 84
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
 208-314 1.99e-04

Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ubiquitinated. Ubiquitination follows conjugation of ubiquitin to a conserved cysteine residue of UBC homologs. TSG101 is one of several UBC homologs that lacks this active site cysteine.


Pssm-ID: 459701 [Multi-domain]  Cd Length: 139  Bit Score: 40.64  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691  208 RLMKELRDIyrsQSYKTGIYSVELINDSLYDWHVKLQkVDPDSPLhsdlqilkekEGIEYILlNFSFKDNFPFDPPFVRV 287
Cdd:pfam00179   1 RLQKELKEL---LKDPPPGISAGPVDDNLFEWKVTII-GPDGTPY----------EGGVFKL-SVEFPEDYPFKPPKVKF 65

                          90       100       110
                  ....*....|....*....|....*....|
gi 530406691  288 VLPVLsgglvHP---SKGRwlnvltvVCLD 314
Cdd:pfam00179  66 TTKIY-----HPnvdSSGE-------VCLD 83
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
 9-89 5.59e-04

RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.


Pssm-ID: 399058  Cd Length: 111  Bit Score: 38.84  E-value: 5.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691    9 ELKFLASIFDKNHERFRIVSWKLDELHCQFLVPQQGSPHSLPPPLTLHCNITESYPSSSPIWFVDS----EDPNLTSVLE 84
Cdd:pfam05773   6 ELEALESIYPDEFEVISDSPYESLEIEIKLSLDSDESDSSHLPPLVLKFTLPEDYPDEPPKISLSSpwnlSDEQVLSLLE 85


                  ....*
gi 530406691   85 RLEDT 89
Cdd:pfam05773  86 ELEEL 90
 
Name Accession Description Interval E-value
UBCc_UBE2Q cd23802
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Q1, ...
 207-298 3.89e-43

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Q1, Q2, and related proteins; The E2Q subfamily includes mammalian ubiquitin-conjugating enzymes E2 Q1 (UBE2Q1/NICE5/UBE2Q), Q2 (UBE2Q2), and similar proteins. They are ubiquitin-conjugating (EC 2.3.2.23) enzymes that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2Q1 may be involved in hormonal homeostasis in females. It is involved in regulation of B4GALT1 cell surface expression, B4GALT1-mediated cell adhesion to laminin and embryoid body formation. In vitro, UBE2Q2 catalyzes 'Lys-48'-linked polyubiquitination. This subfamily also includes ubiquitin-conjugating enzyme E2Q-like protein 1 (UBE2QL1), which is a probable E2 ubiquitin-protein ligase that may facilitate the monoubiquitination and degradation of MTOR and CCNE1 through interaction with FBXW7.


Pssm-ID: 467422  Cd Length: 157  Bit Score: 145.47  E-value: 3.89e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691 207 DRLMKELRDIYRSQSYKTGiYSVELINDSLYDWHVKLQKVDPDSPLHSDLQILKEKEGIEYILLNFSFKDNFPFDPPFVR 286
Cdd:cd23802    1 KRLMKELKDLMKSQSKKLG-FSVDPVDDNLYHWEVKLFGFDPDSPLAKDLKKLKKKHGYDYIELELRFPDLYPFYPPFVR 79

                         90
                 ....*....|..
gi 530406691 287 VVLPVLSGGLVH 298
Cdd:cd23802   80 VVRPRLKGGTGH 91
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 208-314 1.01e-08

Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for proteasome-mediated degradation may be ubiquitinated. Ubiquitination follows conjugation of ubiquitin to a conserved cysteine residue of UBC homologues. This pathway functions in regulating many fundamental processes required for cell viability.TSG101 is one of several UBC homologues that lacks this active site cysteine.


Pssm-ID: 214562 [Multi-domain]  Cd Length: 145  Bit Score: 53.07  E-value: 1.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691   208 RLMKELRDIYRSQsyKTGIYSVELINDSLYDWHVKLqkVDPDSPLHSDLQILkekegieyilLNFSFKDNFPFDPPFVRV 287
Cdd:smart00212   1 RLLKELKELRKDP--PPGFTAYPVDDENLLEWTGTI--VGPPGTPYEGGVFK----------LTIEFPEDYPFKPPKVKF 66

                           90       100       110
                   ....*....|....*....|....*....|
gi 530406691   288 VLPVLsgglvHP---SKGRwlnvltvVCLD 314
Cdd:smart00212  67 ITKIY-----HPnvdSSGE-------ICLD 84
UBCc_ScCDC34-like cd23811
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae CDC34 and ...
 205-299 4.38e-08

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae CDC34 and related proteins; Saccharomyces cerevisiae CDC34 (EC 2.3.2.23), also called ubiquitin-conjugating enzyme E2-34 kDa, cell division control protein 34, E2 ubiquitin-conjugating enzyme 3 (UBC3), DNA6, or ubiquitin ligase complex SCF subunit CDC34, catalyzes the covalent attachment of ubiquitin to other proteins. In vitro, it may ubiquitinate histone H2A. CDC34 mediates the initiation of DNA replication (transition of G1 to S phase in cell cycle). It is the catalytic subunit of an SCF ubiquitin-protein ligase complex (together with Skp1p, Rbx1p, CDC53, and an F-box protein) that regulates cell cycle progression by targeting key substrates for degradation. Moreover, CDC34 is involved in the regulation of methionine biosynthesis genes and in the degradation of CDC6 together with CDC4 and CDC53.


Pssm-ID: 467431  Cd Length: 170  Bit Score: 52.06  E-value: 4.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691 205 ASDRLMKELRDIYRSQSYKTgiYSVELINDSLYDWHVKLQKVDPDSPLHSDlqilkekegieYILLNFSFKDNFPFDPPF 284
Cdd:cd23811    1 AAKILMKEYKELTKPKTGPW--VHIELVNDNIFTWTVGLMVLNPDSIYNGG-----------YFKAEMVFPRDYPFSPPS 67

                         90
                 ....*....|....*
gi 530406691 285 VRVVLPVLsgglvHP 299
Cdd:cd23811   68 FRFLPPIF-----HP 77
UBCc_UEV cd00195
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain; ...
 208-314 2.39e-07

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain; The family includes ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain and ubiquitin (Ub) E2 variant (UEV) domain. They belong to the ubiquitin-conjugating (UBC) superfamily that represents a structural domain with an alpha-beta(4)-alpha(3) core fold. E2 is part of the ubiquitin-mediated protein degradation pathway in which a thioester linkage forms between a conserved cysteine and the C-terminus of ubiquitin, and complexes with ubiquitin protein ligase enzymes, E3. This pathway regulates many fundamental cellular processes. There are also other E2s which form thioester linkages without the use of E3s. Several UBC homologs (TSG101, Mms2, Croc-1 and similar proteins) contains the UEV domain, which lacks the active site cysteine essential for ubiquitination and appear to function in DNA repair pathways.


Pssm-ID: 467407 [Multi-domain]  Cd Length: 112  Bit Score: 48.45  E-value: 2.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691 208 RLMKELRDIyrsQSYKTGIYSVELINDSLYDWHVKLqKVDPDSPLhsdlqilkekEGiEYILLNFSFKDNFPFDPPFVRV 287
Cdd:cd00195    2 RLQKELKEL---QKNPPPGISVEPVDDDLFHWKATI-KGPEGTPY----------EG-GVFKLDIEFPDDYPFKPPKVRF 66

                         90       100
                 ....*....|....*....|....*....
gi 530406691 288 VLPVlsgglVHPskgrwlNVLT--VVCLD 314
Cdd:cd00195   67 LTPI-----YHP------NVDPdgEICLD 84
UBCc_TcUBE-like cd23828
Ubiquitin-conjugating enzyme E2, putative catalytic (UBCc) domain of Trypanosoma cruzi ...
 208-293 7.87e-06

Ubiquitin-conjugating enzyme E2, putative catalytic (UBCc) domain of Trypanosoma cruzi putative ubiquitin-conjugating enzyme E2 and related proteins; This subfamily includes uncharacterized Trypanosoma cruzi putative ubiquitin-conjugating enzyme E2 and similar proteins. They may function as ubiquitin-conjugating enzymes (EC 2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins.


Pssm-ID: 467437  Cd Length: 121  Bit Score: 44.30  E-value: 7.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691 208 RLMKELR----DIYRSQSYKTGIYSVELIN-DSLYDWHVKLqKVDPDSPLHSdlqilkekeGIEYILLnFSFKDNFPFDP 282
Cdd:cd23828    2 RIGKDLRllleSIKTGTEVDPAGSLIASVDsDSLFHWRVVV-KPPANSIVYA---------GNTYELL-VIFSDDYPHEP 70

                         90
                 ....*....|.
gi 530406691 283 PFVRVVLPVLS 293
Cdd:cd23828   71 PKVRFLTPIYS 81
UBCc_UBE2W cd23808
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 W ...
 208-314 1.04e-04

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 W and related enzymes; The E2W subfamily includes mammalian ubiquitin-conjugating enzymes E2 W (UBE2W/UBC16), plant ubiquitin-conjugating enzyme E2 15-18 (UBC15-18), and similar proteins. They are ubiquitin-conjugating enzymes (EC 2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2W, also called FLJ11011, E2 ubiquitin-conjugating enzyme W, N-terminal E2 ubiquitin-conjugating enzyme (EC 2.3.2.25), N-terminus-conjugating E2, ubiquitin carrier protein W, ubiquitin-conjugating enzyme 16 (UBC-16), or ubiquitin-protein ligase W, specifically monoubiquitinates the N-terminus of various substrates, including ATXN3, MAPT/TAU, POLR2H/RPB8 and STUB1/CHIP, by recognizing backbone atoms of disordered N-termini. In vitro, UBE2W catalyzes 'Lys-11'-linked polyubiquitination. UBE2W is an important protein for early postnatal survival and for the normal functioning of multiple organ systems.


Pssm-ID: 467428 [Multi-domain]  Cd Length: 119  Bit Score: 40.97  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691 208 RLMKELRDIyrSQSYKTGIySVELINDSLYDWHVKLQkvDPDSPLHsdlqilkekEGIEYiLLNFSFKDNFPFDPP---F 284
Cdd:cd23808    3 RLQKELKEL--QKNPPPGI-TLDVADNNLTEWIVTIE--GAPGTLY---------EGEKF-RLRFKFPPDYPIESPevvF 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 530406691 285 VRVVLPvlsgglVHP---SKGR---------WLNVLTV--VCLD 314
Cdd:cd23808   68 VGPPIP------VHPhvySNGHiclsilyddWSPALTVssVCLS 105
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
 208-314 1.99e-04

Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ubiquitinated. Ubiquitination follows conjugation of ubiquitin to a conserved cysteine residue of UBC homologs. TSG101 is one of several UBC homologs that lacks this active site cysteine.


Pssm-ID: 459701 [Multi-domain]  Cd Length: 139  Bit Score: 40.64  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691  208 RLMKELRDIyrsQSYKTGIYSVELINDSLYDWHVKLQkVDPDSPLhsdlqilkekEGIEYILlNFSFKDNFPFDPPFVRV 287
Cdd:pfam00179   1 RLQKELKEL---LKDPPPGISAGPVDDNLFEWKVTII-GPDGTPY----------EGGVFKL-SVEFPEDYPFKPPKVKF 65

                          90       100       110
                  ....*....|....*....|....*....|
gi 530406691  288 VLPVLsgglvHP---SKGRwlnvltvVCLD 314
Cdd:pfam00179  66 TTKIY-----HPnvdSSGE-------VCLD 83
UBCc_invertebrate cd23955
ubiquitin-conjugating enzyme family protein; This subfamily includes ubiquitin-conjugating ...
 208-314 2.87e-04

ubiquitin-conjugating enzyme family protein; This subfamily includes ubiquitin-conjugating enzyme E2, catalytic (UBCc) domains mostly found in non-vertebrate eukaryotes. They belong to the ubiquitin-conjugating (UBC) superfamily that represents a structural domain with an alpha-beta(4)-alpha(3) core fold. E2 is part of the ubiquitin-mediated protein degradation pathway in which a thioester linkage forms between a conserved cysteine and the C-terminus of ubiquitin and complexes with ubiquitin protein ligase enzymes, E3. This pathway regulates many fundamental cellular processes. There are also other E2s which form thioester linkages without the use of E3s.


Pssm-ID: 467440 [Multi-domain]  Cd Length: 120  Bit Score: 39.93  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691 208 RLMKELRDIYRSQSykTGIySVELINDSLYDWHVKLqkVDPDSPLHSdlqilkekeGIEYILLNFSfkDNFPFDPPFVRv 287
Cdd:cd23955    2 RLLRDLKELQEEPL--PGV-SAEPLENDLFEWHVNI--RGPDGPYSG---------VILHLELTFP--EDYPNSPPSVR- 64

                         90       100
                 ....*....|....*....|....*....
gi 530406691 288 vlpvLSGGLVHPskgrwlNV--LTVVCLD 314
Cdd:cd23955   65 ----LLTPLPHP------NVftGNYICLD 83
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
 9-89 5.59e-04

RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.


Pssm-ID: 399058  Cd Length: 111  Bit Score: 38.84  E-value: 5.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691    9 ELKFLASIFDKNHERFRIVSWKLDELHCQFLVPQQGSPHSLPPPLTLHCNITESYPSSSPIWFVDS----EDPNLTSVLE 84
Cdd:pfam05773   6 ELEALESIYPDEFEVISDSPYESLEIEIKLSLDSDESDSSHLPPLVLKFTLPEDYPDEPPKISLSSpwnlSDEQVLSLLE 85


                  ....*
gi 530406691   85 RLEDT 89
Cdd:pfam05773  86 ELEEL 90
UEV_Morgue-like cd23826
ubiquitin E2 variant (UEV) domain of Drosophila melanogaster Morgue and related proteins; ...
 208-314 6.59e-04

ubiquitin E2 variant (UEV) domain of Drosophila melanogaster Morgue and related proteins; Morgue is an F-box/ubiquitin conjugase domain protein important for grim-reaper mediated apoptosis. It contains both an F-box and a UEV domain that is homologous to E2 ubiquitin ligases but lacks the conserved cysteine residue required for catalytic activity.


Pssm-ID: 467436 [Multi-domain]  Cd Length: 147  Bit Score: 39.53  E-value: 6.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691 208 RLMKELRDIYrsQSYKTGIYSVELINDSLYDWHVKLQKvDPDSPLhsdlqilkeKEGIEYilLNFSFKDNFPFDPPFVRV 287
Cdd:cd23826    5 RLRRELKALH--SDDPPEGISARPLDRSLLHLLATIEG-PPGSPY---------EGGIFF--LRIQIPESYPFRPPKVRF 70

                         90       100
                 ....*....|....*....|....*....
gi 530406691 288 VLPVLsgglvHPskgrwlNVLT--VVCLD 314
Cdd:cd23826   71 LTKIY-----HP------NISRhgDICLD 88
UBCc_UBE2T cd23805
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 T ...
 208-310 1.11e-03

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 T and related enzymes; The E2T subfamily includes mammalian ubiquitin-conjugating enzymes E2 T (UBE2T/HSPC150/PIG50), plant ubiquitin-conjugating enzyme E2 37 (UBC37), and similar proteins. They are ubiquitin-conjugating enzymes (EC 2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2T, also called cell proliferation-inducing gene 50 protein, catalyzes monoubiquitination. It is involved in mitomycin-C (MMC)-induced DNA repair. It acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. UBE2T also mediates monoubiquitination of FANCL and FANCI. It may contribute to ubiquitination and degradation of BRCA1. In vitro, UBE2T can promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination.


Pssm-ID: 467425  Cd Length: 146  Bit Score: 38.66  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691 208 RLMKELRDIYRSQSYktGIySVELINDSLYDWHVKLQKvDPDSPLHSdlqilkekeGIeyILLNFSFKDNFPFDPPFVRV 287
Cdd:cd23805    2 RLKRELQLLQKDPPP--GI-SCWPKDDSLDELEAQIQG-PEGTPYEG---------GV--FKLEITIPERYPFEPPKVRF 66

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 530406691 288 VLPVL-----SGG------LVHPSKGRW---LNVLTV 310
Cdd:cd23805   67 LTPIYhpnidSAGricldiLKMPPKGSWkpsLNISTV 103
UBCc_UBE2K cd23800
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 K ...
 208-314 1.90e-03

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 K and related proteins; The E2J subfamily includes mammalian ubiquitin-conjugating enzymes E2 K (UBE2K/HIP2/LIG), yeast ubiquitin-conjugating enzyme E2 1 (UBC1), and plant ubiquitin-conjugating enzyme E2 27 (UBC27). They are ubiquitin-conjugating enzymes (EC 2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2K is also called huntingtin-interacting protein 2 (HIP-2), ubiquitin-conjugating enzyme E2-25 kDa, or ubiquitin-conjugating enzyme E2(25K). In vitro, in the presence or absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, UBE2K catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. It does not transfer ubiquitin directly, but elongates monoubiquitinated substrate proteins. Saccharomyces cerevisiae UBC1, also called ubiquitin-conjugating enzyme E2-24 kDa, functions in the degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. It is a cognate E2 conjugating enzyme for the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M).


Pssm-ID: 467420  Cd Length: 145  Bit Score: 37.92  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691 208 RLMKELRDIYRSQSYKTGIYsVELINDSLYDWHVKLqKVDPDSP-----LHSDLQIlkekegieyillnfsfKDNFPFDP 282
Cdd:cd23800    3 RIKKELKEVQKDSEAESGIK-VELVGDDLTHLKGEI-AGPPDTPyeggtFVLDIKI----------------PDTYPFEP 64

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 530406691 283 PFVRVVLPVLsgglvHPskgrwlNVLTV---VCLD 314
Cdd:cd23800   65 PKMKFITKIW-----HP------NISSQtgaICLD 88
UBCc_SpUBC14-like cd23815
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Schizosaccharomyces pombe UBC14 ...
 208-291 7.36e-03

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Schizosaccharomyces pombe UBC14 and related proteins; Schizosaccharomyces pombe UBC14 (EC 2.3.2.23), also called ubiquitin-conjugating enzyme E2 14, E2 ubiquitin-conjugating enzyme 14, ubiquitin carrier protein 14, or ubiquitin-protein ligase 14, acts as a ubiquitin-conjugating enzyme that catalyzes the covalent attachment of ubiquitin to other proteins. It mediates the selective degradation of short-lived and abnormal proteins.


Pssm-ID: 467435  Cd Length: 143  Bit Score: 36.11  E-value: 7.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530406691 208 RLMKELRDIyrsQSYKTGIYSVELINDSLYDWHVKLQKVdPDSPLhsdlqilkeKEGIEYILLnfSFKDNFPFDPPFVRV 287
Cdd:cd23815    2 RIQKELADL---QKNPIAGISAGPVEDNLFEWKGTILGP-VGSPY---------EGGIFKFKI--TFPEDYPFKPPTVKF 66


                 ....
gi 530406691 288 VLPV 291
Cdd:cd23815   67 TTKI 70
 
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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