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Conserved domains on  [gi|755515697|ref|XP_011239398|]
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ubiquitin-conjugating enzyme E2 Q2-like isoform X1 [Mus musculus]

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, ...
 204-358 6.45e-74

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: 226.36  E-value: 6.45e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 204 DRLMKELREIYRSQSYKSGtFSVELINDSLYDWHVKLRKVDPDSCLYRDLQRLKQKEGIDYILLNFSFKDNFPFDPPFVR 283
Cdd:cd23802    1 KRLMKELKDLMKSQSKKLG-FSVDPVDDNLYHWEVKLFGFDPDSPLAKDLKKLKKKHGYDYIELELRFPDLYPFYPPFVR 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755515697 284 VVLPVLSDGYVLDGGALCMELLTNQGWSSAYSIESVILQINATLVKGKARVRFG---VDNHYTEQVARRVYKSMVLKH 358
Cdd:cd23802   80 VVRPRLKGGTGHVGGAICMELLTLSGWSPAYSIESVLLQIRALLVKGGARDDFSaraNKSPYSEAEARAAFKRLARIH 157
RWD super family cl02687
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
 8-67 7.29e-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: 7.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697    8 ELEFLASIFHKDHERLRIVSWHLDDLQCQfLVPEATVGSPPSPPPLTLHCTITESYPSSP 67
Cdd:pfam05773   6 ELEALESIYPDEFEVISDSPYESLEIEIK-LSLDSDESDSSHLPPLVLKFTLPEDYPDEP 64
 
Name Accession Description Interval E-value
UBCc_UBE2Q cd23802
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Q1, ...
 204-358 6.45e-74

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: 226.36  E-value: 6.45e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 204 DRLMKELREIYRSQSYKSGtFSVELINDSLYDWHVKLRKVDPDSCLYRDLQRLKQKEGIDYILLNFSFKDNFPFDPPFVR 283
Cdd:cd23802    1 KRLMKELKDLMKSQSKKLG-FSVDPVDDNLYHWEVKLFGFDPDSPLAKDLKKLKKKHGYDYIELELRFPDLYPFYPPFVR 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755515697 284 VVLPVLSDGYVLDGGALCMELLTNQGWSSAYSIESVILQINATLVKGKARVRFG---VDNHYTEQVARRVYKSMVLKH 358
Cdd:cd23802   80 VVRPRLKGGTGHVGGAICMELLTLSGWSPAYSIESVLLQIRALLVKGGARDDFSaraNKSPYSEAEARAAFKRLARIH 157
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 205-329 1.08e-17

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: 78.88  E-value: 1.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697   205 RLMKELREIYRSQsyKSGTFSVELINDSLYDWHVKLrkVDPDSCLYRDLQrlkqkegidyILLNFSFKDNFPFDPPFVRV 284
Cdd:smart00212   1 RLLKELKELRKDP--PPGFTAYPVDDENLLEWTGTI--VGPPGTPYEGGV----------FKLTIEFPEDYPFKPPKVKF 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 755515697   285 VLPVLSdGYVLDGGALCMELLTNQGWSSAYSIESVILQINATLVK 329
Cdd:smart00212  67 ITKIYH-PNVDSSGEICLDILKQEKWSPALTLETVLLSLQSLLSE 110
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
 205-327 9.80e-12

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: 61.83  E-value: 9.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697  205 RLMKELREIyrsQSYKSGTFSVELINDSLYDWHVKLrkVDPDSCLYrdlqrlkqkEGIDYILlNFSFKDNFPFDPPFVRV 284
Cdd:pfam00179   1 RLQKELKEL---LKDPPPGISAGPVDDNLFEWKVTI--IGPDGTPY---------EGGVFKL-SVEFPEDYPFKPPKVKF 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 755515697  285 VLPVL-----SDGyvldggALCMELLTNQGWSSAYSIESVILQINATL 327
Cdd:pfam00179  66 TTKIYhpnvdSSG------EVCLDILKDERWSPALTLEQVLLSIQSLL 107
PLN00172 PLN00172
ubiquitin conjugating enzyme; Provisional
 202-362 2.07e-06

ubiquitin conjugating enzyme; Provisional


Pssm-ID: 177768 [Multi-domain]  Cd Length: 147  Bit Score: 47.05  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 202 ASDRLMKELREIYRSqsyKSGTFSVELINDSLYDWHVKLrkVDPDSCLYRDlqrlkqkeGIdyILLNFSFKDNFPFDPPF 281
Cdd:PLN00172   2 ATKRIQKEHKDLLKD---PPSNCSAGPSDENLFRWTASI--IGPSDSPYAG--------GV--FFLSILFPPDYPFKPPK 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 282 VRVVLPVLSDGyVLDGGALCMELLTNQgWSSAYSIESVILQINATLVKGKArvrfgvDNHYTEQVArRVYKSMVLKHEKS 361
Cdd:PLN00172  67 VQFTTKIYHPN-INSNGSICLDILRDQ-WSPALTVSKVLLSISSLLTDPNP------DDPLVPEIA-RVFKENRSRYEAT 137


                 .
gi 755515697 362 G 362
Cdd:PLN00172 138 A 138
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
 8-67 7.29e-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: 7.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697    8 ELEFLASIFHKDHERLRIVSWHLDDLQCQfLVPEATVGSPPSPPPLTLHCTITESYPSSP 67
Cdd:pfam05773   6 ELEALESIYPDEFEVISDSPYESLEIEIK-LSLDSDESDSSHLPPLVLKFTLPEDYPDEP 64
 
Name Accession Description Interval E-value
UBCc_UBE2Q cd23802
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Q1, ...
 204-358 6.45e-74

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: 226.36  E-value: 6.45e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 204 DRLMKELREIYRSQSYKSGtFSVELINDSLYDWHVKLRKVDPDSCLYRDLQRLKQKEGIDYILLNFSFKDNFPFDPPFVR 283
Cdd:cd23802    1 KRLMKELKDLMKSQSKKLG-FSVDPVDDNLYHWEVKLFGFDPDSPLAKDLKKLKKKHGYDYIELELRFPDLYPFYPPFVR 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755515697 284 VVLPVLSDGYVLDGGALCMELLTNQGWSSAYSIESVILQINATLVKGKARVRFG---VDNHYTEQVARRVYKSMVLKH 358
Cdd:cd23802   80 VVRPRLKGGTGHVGGAICMELLTLSGWSPAYSIESVLLQIRALLVKGGARDDFSaraNKSPYSEAEARAAFKRLARIH 157
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 205-329 1.08e-17

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: 78.88  E-value: 1.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697   205 RLMKELREIYRSQsyKSGTFSVELINDSLYDWHVKLrkVDPDSCLYRDLQrlkqkegidyILLNFSFKDNFPFDPPFVRV 284
Cdd:smart00212   1 RLLKELKELRKDP--PPGFTAYPVDDENLLEWTGTI--VGPPGTPYEGGV----------FKLTIEFPEDYPFKPPKVKF 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 755515697   285 VLPVLSdGYVLDGGALCMELLTNQGWSSAYSIESVILQINATLVK 329
Cdd:smart00212  67 ITKIYH-PNVDSSGEICLDILKQEKWSPALTLETVLLSLQSLLSE 110
UBCc_UEV cd00195
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain; ...
 205-327 1.61e-17

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: 77.34  E-value: 1.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 205 RLMKELREIyrsQSYKSGTFSVELINDSLYDWHVKLrKVDPDSCLyrdlqrlkqkEGiDYILLNFSFKDNFPFDPPFVRV 284
Cdd:cd00195    2 RLQKELKEL---QKNPPPGISVEPVDDDLFHWKATI-KGPEGTPY----------EG-GVFKLDIEFPDDYPFKPPKVRF 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 755515697 285 VLPVlsdgY---VLDGGALCMELLTNQGWSSAYSIESVILQINATL 327
Cdd:cd00195   67 LTPI----YhpnVDPDGEICLDILKSEGWSPALTLRSVLLSIQSLL 108
UBCc_invertebrate cd23955
ubiquitin-conjugating enzyme family protein; This subfamily includes ubiquitin-conjugating ...
 205-328 6.63e-15

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: 70.36  E-value: 6.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 205 RLMKELREIyrsQSYKSGTFSVELINDSLYDWHVKLRkvdPDSCLYRDlqrlkqkeGIDYILLNFSfkDNFPFDPPFVRV 284
Cdd:cd23955    2 RLLRDLKEL---QEEPLPGVSAEPLENDLFEWHVNIR---GPDGPYSG--------VILHLELTFP--EDYPNSPPSVRL 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755515697 285 vLPVLSDGYVLDGGALCMELLTN---------QGWSSAYSIESVILQINATLV 328
Cdd:cd23955   66 -LTPLPHPNVFTGNYICLDMLENfakhhskpySGWSPAYTVQSILLQLQAFLF 117
UBCc_ScCDC34-like cd23811
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae CDC34 and ...
 202-361 5.96e-14

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: 69.01  E-value: 5.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 202 ASDRLMKELREIyrSQSYKSGTFSVELINDSLYDWHVKLRKVDPDSCLYRDLQRLKQKegidyillnfsFKDNFPFDPPF 281
Cdd:cd23811    1 AAKILMKEYKEL--TKPKTGPWVHIELVNDNIFTWTVGLMVLNPDSIYNGGYFKAEMV-----------FPRDYPFSPPS 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 282 VRVVLPVLSDGyVLDGGALCMELL------------TNQGWSSAYSIESVILQINATL----VKGKARVRFGVDnhYTEQ 345
Cdd:cd23811   68 FRFLPPIFHPN-VYPDGRLCISILhspgddyqsgepAAERWSPAQTVESVLLSILSLLedpnINSPANVDAGVL--YRKN 144

                        170
                 ....*....|....*..
gi 755515697 346 vaRRVYKSMVLKH-EKS 361
Cdd:cd23811  145 --REEYKDKVKKTvEKS 159
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
 205-327 9.80e-12

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: 61.83  E-value: 9.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697  205 RLMKELREIyrsQSYKSGTFSVELINDSLYDWHVKLrkVDPDSCLYrdlqrlkqkEGIDYILlNFSFKDNFPFDPPFVRV 284
Cdd:pfam00179   1 RLQKELKEL---LKDPPPGISAGPVDDNLFEWKVTI--IGPDGTPY---------EGGVFKL-SVEFPEDYPFKPPKVKF 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 755515697  285 VLPVL-----SDGyvldggALCMELLTNQGWSSAYSIESVILQINATL 327
Cdd:pfam00179  66 TTKIYhpnvdSSG------EVCLDILKDERWSPALTLEQVLLSIQSLL 107
UBCc_TcUBE-like cd23828
Ubiquitin-conjugating enzyme E2, putative catalytic (UBCc) domain of Trypanosoma cruzi ...
 205-323 1.77e-09

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: 55.09  E-value: 1.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 205 RLMKELREIyrSQSYKSGT------FSVELIN-DSLYDWHVKLRKvDPDSCLYrdlqrlkqkEGIDYILLnFSFKDNFPF 277
Cdd:cd23828    2 RIGKDLRLL--LESIKTGTevdpagSLIASVDsDSLFHWRVVVKP-PANSIVY---------AGNTYELL-VIFSDDYPH 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 755515697 278 DPPFVRVVLPVLSDGyVLDGGALCmELLTNQGWSSAYSIESVILQI 323
Cdd:cd23828   69 EPPKVRFLTPIYSPL-VSPEGSVC-ERLLEDDWKPTQHAADAIELV 112
UBCc_UBE2W cd23808
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 W ...
 205-323 6.48e-09

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: 53.30  E-value: 6.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 205 RLMKELREIyrsQSYKSGTFSVELINDSLYDWHVKLRkVDPDScLYrdlqrlkqkEGIDYiLLNFSFKDNFPFDPP---F 281
Cdd:cd23808    3 RLQKELKEL---QKNPPPGITLDVADNNLTEWIVTIE-GAPGT-LY---------EGEKF-RLRFKFPPDYPIESPevvF 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 755515697 282 VRVVLP----VLSDGYVldggalCMELLTnQGWSSAYSIESVILQI 323
Cdd:cd23808   68 VGPPIPvhphVYSNGHI------CLSILY-DDWSPALTVSSVCLSI 106
UEV_Morgue-like cd23826
ubiquitin E2 variant (UEV) domain of Drosophila melanogaster Morgue and related proteins; ...
 205-327 1.01e-07

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: 50.70  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 205 RLMKELREIYrsQSYKSGTFSVELINDSLYDWHVKLRkvDPDSCLYrdlqrlkqKEGIDYilLNFSFKDNFPFDPPFVRV 284
Cdd:cd23826    5 RLRRELKALH--SDDPPEGISARPLDRSLLHLLATIE--GPPGSPY--------EGGIFF--LRIQIPESYPFRPPKVRF 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 755515697 285 VLPVLSDGyVLDGGALCMELLTNQgWSSAYSIESVILQINATL 327
Cdd:cd23826   71 LTKIYHPN-ISRHGDICLDILEHN-WSLALTIEKVLISIQSLL 111
UBCc_SpUBC14-like cd23815
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Schizosaccharomyces pombe UBC14 ...
 205-323 1.59e-07

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: 49.98  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 205 RLMKELREIyrsQSYKSGTFSVELINDSLYDWHVKLRkvDPDSCLYrdlqrlkqKEGIDYILLnfSFKDNFPFDPPFVRV 284
Cdd:cd23815    2 RIQKELADL---QKNPIAGISAGPVEDNLFEWKGTIL--GPVGSPY--------EGGIFKFKI--TFPEDYPFKPPTVKF 66

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 755515697 285 VLPVLSDGyVLDGGALCMELLTNQGWSSAYSIESVILQI 323
Cdd:cd23815   67 TTKIYHPN-VDDDGSICLGILKSDAWKPSIKLVSVLNAL 104
PLN00172 PLN00172
ubiquitin conjugating enzyme; Provisional
 202-362 2.07e-06

ubiquitin conjugating enzyme; Provisional


Pssm-ID: 177768 [Multi-domain]  Cd Length: 147  Bit Score: 47.05  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 202 ASDRLMKELREIYRSqsyKSGTFSVELINDSLYDWHVKLrkVDPDSCLYRDlqrlkqkeGIdyILLNFSFKDNFPFDPPF 281
Cdd:PLN00172   2 ATKRIQKEHKDLLKD---PPSNCSAGPSDENLFRWTASI--IGPSDSPYAG--------GV--FFLSILFPPDYPFKPPK 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 282 VRVVLPVLSDGyVLDGGALCMELLTNQgWSSAYSIESVILQINATLVKGKArvrfgvDNHYTEQVArRVYKSMVLKHEKS 361
Cdd:PLN00172  67 VQFTTKIYHPN-INSNGSICLDILRDQ-WSPALTVSKVLLSISSLLTDPNP------DDPLVPEIA-RVFKENRSRYEAT 137


                 .
gi 755515697 362 G 362
Cdd:PLN00172 138 A 138
UBCc_ScPEX4-like cd23812
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae Peroxin-4 ...
 205-327 4.00e-06

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae Peroxin-4 (PEX4) protein and related proteins; Saccharomyces cerevisiae PEX4 (EC 2.3.2.23), also called ubiquitin-conjugating enzyme E2-21 kDa, UBC10, or PAS2, acts as a ubiquitin-conjugating enzyme that catalyzes the covalent attachment of ubiquitin to other proteins. It is essential for peroxisome biogenesis and is required for UBC4-independent ubiquitination of PEX5. This subfamily also includes Arabidopsis thaliana PEX4 (also known as UBC21, EC 2.3.2.23) that is required for peroxisome biogenesis. It is necessary for the developmental elimination of obsolete peroxisome matrix proteins. It may be involved in the ubiquitination of PEX5, targeting it for recycling.


Pssm-ID: 467432 [Multi-domain]  Cd Length: 145  Bit Score: 46.00  E-value: 4.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 205 RLMKELREIyrSQSYKSGTFSVELIND-SLYDWHVKLRKvdPDSCLYrdlqrlkqkEGIDYiLLNFSFKDNFPFDPPFVR 283
Cdd:cd23812    2 RLLKELREL--QKEPNDPDIVLGPVEDdDLFRWEAVIKG--PKDTPY---------EGGRF-ELAIQVPSNYPISPPKVK 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 755515697 284 VVLPVLSDGYVLDGGALCMELLTNQgWSSAYSIESVILQINATL 327
Cdd:cd23812   68 FVTKIFHPNVHFKTGEICLDILKTA-WSPAWTLQSVCRAILALL 110
UBCc_UBE2F_UBE2M cd23794
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzymes E2 F, ...
 205-327 6.29e-06

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzymes E2 F, E2 M and related proteins; The E2F/E2M subfamily includes mammalian ubiquitin-conjugating enzymes E2 F (UBE2F/NCE2, EC 2.3.2.32) and E2 M (UBE2M/UBC12, EC 2.3.2.34), yeast NEDD8-conjugating enzyme UBC12 (EC 2.3.2.24), plant RUB1-conjugating enzyme 1-2 (RCE1/UBC12 and RCE2/UBC12L, EC 2.3.2.-), and similar proteins. UBE2F (also called EDD8-conjugating enzyme UBE2F, NEDD8 carrier protein UBE2F, NEDD8 protein ligase UBE2F, NEDD8-conjugating enzyme 2, or RING-type E3 NEDD8 transferase UBE2F) and UBE2M (also called NEDD8-conjugating enzyme UBC12, or NEDD8 carrier protein) accept the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The RBX2-UBE2F complex neddylates specific target proteins, such as CUL5. The RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. UBE2M is involved in cell proliferation. Saccharomyces cerevisiae UBC12 and Arabidopsis thaliana RCE1/RCE2 accept the ubiquitin-like protein NEDD8/RUB1 from the UBA3-ULA1 E1 complex and the ECR1-AXR1 E1 complex, respectively.


Pssm-ID: 467414  Cd Length: 138  Bit Score: 45.25  E-value: 6.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 205 RLMKELREIYrsqsyKSGTFSVELINDS-LYDWHVKLRkvdPDSCLYRDLQrlkqkegidyILLNFSFKDNFPFDPPFVR 283
Cdd:cd23794    5 RLQKDLEELD-----LPGQCKVEFPDPNdLLKFEVTIT---PDEGYYKGGT----------FVFEIDIPDNYPFEPPKVK 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 755515697 284 VVLPVlsdgY---VLDGGALCMELLtNQGWSSAYSIESVILQINATL 327
Cdd:cd23794   67 CLTKI----YhpnIDEEGNVCLNIL-REDWKPVLSLKDVILGLLFLF 108
UBCc_UBE2A_2B cd23790
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzymes E2A, ...
 202-323 1.71e-04

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzymes E2A, E2B and related proteins; The E2A/2B subfamily includes mammalian ubiquitin-conjugating enzymes UBE2A/RAD6A and UBE2B/RAD6B, yeast ubiquitin-conjugating enzyme E2 2 (UBC2/RAD6), plant ubiquitin-conjugating enzyme E2 1-3 (UBC1-3), 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. Both UBE2A/RAD6A and UBE2B/RAD6B are required for post-replication repair of UV-damaged DNA. In vitro, they catalyze 'Lys-11', as well as 'Lys-48'-linked polyubiquitination. UBE2B might also catalyze 'Lys-63'-linked polyubiquitination. Saccharomyces cerevisiae UBC2 is required for DNA repair, damage-induced mutagenesis, and sporulation.


Pssm-ID: 467410  Cd Length: 143  Bit Score: 41.34  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 202 ASDRLMKELREIyrsQSYKSGTFSVELINDSLYDWHVKLRkvDPDSCLYRDlqrlkqkeGIDYILLNFSfkDNFPFDPPF 281
Cdd:cd23790    3 ARRRLMRDFKRL---QKDPPEGISAAPVEDNIMVWNAVIF--GPEDTPWEG--------GTFKLRLEFS--EEYPNKPPK 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 755515697 282 VRVVLP-----VLSDgyvldgGALCMELLTNQgWSSAYSIESVILQI 323
Cdd:cd23790   68 VRFVSKmfhpnVYAD------GSICLDILQNR-WSPTYDVSAILTSI 107
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
 8-67 7.29e-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: 7.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697    8 ELEFLASIFHKDHERLRIVSWHLDDLQCQfLVPEATVGSPPSPPPLTLHCTITESYPSSP 67
Cdd:pfam05773   6 ELEALESIYPDEFEVISDSPYESLEIEIK-LSLDSDESDSSHLPPLVLKFTLPEDYPDEP 64
UBCc_UBE2C cd23791
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 C ...
 203-327 1.86e-03

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 C and related proteins; The E2C family includes mammalian ubiquitin-conjugating enzyme E2 C (UBE2C/UBCH10), yeast E2 ubiquitin-conjugating enzyme 11 (UBC11), plant ubiquitin-conjugating enzyme E2 19 (UBC19) and 20 (UBC20). 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. UBE2C, also known as (E3-independent) E2 ubiquitin-conjugating enzyme C (EC 2.3.2.24), E2 ubiquitin-conjugating enzyme C, ubiquitin carrier protein C, or ubiquitin-protein ligase C, catalyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitination in vitro. It is a ubiquitin carrier protein required for the destruction of mitotic cyclins and proteins that maintain sister chromatid cohesion in animal cells and in Schizosaccharomyces pombe. In Saccharomyces cerevisiae, UBC11 is not essential for mitotic cyclin destruction. Arabidopsis thaliana UBC19 is part of the anaphase-promoting complex (APC). It may have a key function during cell cycle and be involved in cyclin B1 degradation.


Pssm-ID: 467411  Cd Length: 140  Bit Score: 38.32  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 203 SDRLMKELREIYRSQSYKSGTFSVElinDSLYDWHVKLRkvDPDSCLYrdlqrlkqkEGIDYiLLNFSFKDNFPFDPPFV 282
Cdd:cd23791    1 TKRLQSELMTLMMSGDPGISAFPDG---DNLFKWIGTIT--GPEGTVY---------EGLKY-KLSLEFPSNYPYKAPTV 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 755515697 283 RVVLPVLS---DGYvldgGALCMELLTNQgWSSAYSIESVILQINATL 327
Cdd:cd23791   66 KFETPCFHpnvDQH----GNICLDILKEK-WSALYDVRTILLSIQSLL 108
UBCc_UBE2E cd23793
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 ...
 205-327 3.97e-03

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 E1-E3 and related proteins; The E2E subfamily includes mammalian ubiquitin-conjugating enzyme E2 E1-3 (UBE2E1/UBCH6, UBE2E2/UBCH8, UBE2E3/UBCH9) and similar proteins. UBE2E, also known as (E3-independent) E2 ubiquitin-conjugating enzyme E, or E2 ubiquitin-conjugating enzyme E, accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. UBE2E1 (EC 2.3.2.23 and EC 2.3.2.24) catalyzes the covalent attachment of ISG15 to other proteins. It mediates the selective degradation of short-lived and abnormal proteins. In vitro, it also catalyzes 'Lys-48'-linked polyubiquitination. In vitro, both UBE2E2 (EC 2.3.2.23) and UBE2E3 (EC 2.3.2.23) catalyze 'Lys-11'- and 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. UBE2E2 catalyzes the ISGylation of influenza A virus NS1 protein. UBE2E3 participates in the regulation of trans-epithelial sodium transport in renal cells. It may be involved in cell growth arrest.


Pssm-ID: 467413  Cd Length: 141  Bit Score: 37.36  E-value: 3.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755515697 205 RLMKELREIYRSQSYKSgtfSVELINDSLYDWHVKLrkVDPDSCLYRDlqrlkqkeGIdyILLNFSFKDNFPFDPPFVRV 284
Cdd:cd23793    2 RIQKELAEITLDPPPNC---SAGPKGDNLYEWVSTI--LGPPGSVYEG--------GV--FFLDIHFPPDYPFKPPKVTF 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 755515697 285 VLPVlsdgY---VLDGGALCMELLTNQgWSSAYSIESVILQINATL 327
Cdd:cd23793   67 RTRI----YhcnINSQGVICLDILKDN-WSPALTISKVLLSICSLL 107
UBCc_UBE2D cd23792
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 ...
 266-327 5.10e-03

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 D1-D3 and related proteins; The E2D family includes mammalian ubiquitin-conjugating enzyme E2 D1-4 (UBE2D1/SFT/UBC5A/UBCH5/UBCH5A, UBE2D2/PUBC1/UBC4/UBC5B/UBCH4/UBCH5B, UBE2D3/UBC5C/UBCH5C, UBE2D4/HBUCE1/UBCH5D), yeast E2 ubiquitin-conjugating enzyme 4 (UBC4) and 5 (UBC5), as well as plant counterpart ubiquitin-conjugating enzyme E2 8-12 (UBC8/UBCAT4A, UBC9/UBCAT4B, UBC10-12) and 28-30 (UBC28-30). 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. In vitro, UBE2D1-3 (EC 2.3.2.23 and EC 2.3.2.24) catalyze 'Lys-48'-linked polyubiquitination. UBE2D3 also catalyzes 'Lys-11'-linked polyubiquitination. In vitro, UBE2D4 can promote polyubiquitination using all 7 ubiquitin Lys residues but may prefer 'Lys-11' and 'Lys-48'-linked polyubiquitination. Saccharomyces cerevisiae UBC4-5 and Arabidopsis thaliana UBC8-11 mediates the selective degradation of short-lived and abnormal proteins.


Pssm-ID: 467412  Cd Length: 143  Bit Score: 36.86  E-value: 5.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755515697 266 LLNFSFKDNFPFDPPFV----RVVLPVLSdgyvlDGGALCMELLTNQgWSSAYSIESVILQINATL 327
Cdd:cd23792   49 FLNIHFPTDYPFKPPKVafttKIYHPNIN-----SNGSICLDILKDQ-WSPALTISKVLLSICSLL 108
 
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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