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Conserved domains on  [gi|19920682|ref|NP_608833|]
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modifier of rpr and grim, ubiquitously expressed [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UEV_Morgue-like cd23826
ubiquitin E2 variant (UEV) domain of Drosophila melanogaster Morgue and related proteins; ...
 337-483 8.01e-80

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: 244.84  E-value: 8.01e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 337 MRNNFLRGEA-NLLNSYESEGISAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVS 415
Cdd:cd23826   1 WRSRRLRRELkALHSDDPPEGISARPLDRSLLHLLATIEGPPGSPYEGGIFFLRIQIPESYPFRPPKVRFLTKIYHPNIS 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19920682 416 RHGDVGIDIFqQHNWSLALNVAKVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRAWTWKYA 483
Cdd:cd23826  81 RHGDICLDIL-EHNWSLALTIEKVLISIQSLLTDPYLEDPLVPEIAELYVNDREEFEQTAREWTWKYA 147
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 234-265 9.14e-08

F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures.


:

Pssm-ID: 438852  Cd Length: 35  Bit Score: 48.21  E-value: 9.14e-08
                        10        20        30
                ....*....|....*....|....*....|..
gi 19920682 234 IPVEVMLKIFAYLDDMSLWMASEVCKQWHDIV 265
Cdd:cd09917   3 LPDEILLKILSYLDPRDLLRLSLVCKRWRELA 34
PLN03029 super family cl33622
type-a response regulator protein; Provisional
 104-170 4.30e-05

type-a response regulator protein; Provisional


The actual alignment was detected with superfamily member PLN03029:

Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 44.64  E-value: 4.30e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19920682  104 DKQEDEETENDVDIMGFEDLEDPQPaavPQHPNPQPpmePQDQQPAQPVIDLPQPVPEAAAPRRESP 170
Cdd:PLN03029 153 QKQENQEKQEKLEESEIQSEKQEQP---SQQPQSQP---QPQQQPQQPNNNKRKAMEEGLSPDRTRP 213
 
Name Accession Description Interval E-value
UEV_Morgue-like cd23826
ubiquitin E2 variant (UEV) domain of Drosophila melanogaster Morgue and related proteins; ...
 337-483 8.01e-80

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: 244.84  E-value: 8.01e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 337 MRNNFLRGEA-NLLNSYESEGISAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVS 415
Cdd:cd23826   1 WRSRRLRRELkALHSDDPPEGISARPLDRSLLHLLATIEGPPGSPYEGGIFFLRIQIPESYPFRPPKVRFLTKIYHPNIS 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19920682 416 RHGDVGIDIFqQHNWSLALNVAKVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRAWTWKYA 483
Cdd:cd23826  81 RHGDICLDIL-EHNWSLALTIEKVLISIQSLLTDPYLEDPLVPEIAELYVNDREEFEQTAREWTWKYA 147
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
 342-479 1.85e-55

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: 181.62  E-value: 1.85e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682   342 LRGEANLLNSYESEGISAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVG 421
Cdd:pfam00179   2 LQKELKELLKDPPPGISAGPVDDNLFEWKVTIIGPDGTPYEGGVFKLSVEFPEDYPFKPPKVKFTTKIYHPNVDSSGEVC 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19920682   422 IDIFQQHNWSLALNVAKVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRAWT 479
Cdd:pfam00179  82 LDILKDERWSPALTLEQVLLSIQSLLSEPNPEDPLNAEAAKLYRKNREEFEKKVREYV 139
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 355-484 1.28e-40

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: 142.82  E-value: 1.28e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682    355 EGISAIPLDRQN-NYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIFQQHNWSLA 433
Cdd:smart00212  15 PGFTAYPVDDENlLEWTGTIVGPPGTPYEGGVFKLTIEFPEDYPFKPPKVKFITKIYHPNVDSSGEICLDILKQEKWSPA 94

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 19920682    434 LNVAKVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRAWTWKYAM 484
Cdd:smart00212  95 LTLETVLLSLQSLLSEPNPDSPLNADAAELYKKNREEFKKKAREWTKKYAE 145
PLN00172 PLN00172
ubiquitin conjugating enzyme; Provisional
 358-483 5.29e-34

ubiquitin conjugating enzyme; Provisional


Pssm-ID: 177768 [Multi-domain]  Cd Length: 147  Bit Score: 125.25  E-value: 5.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682  358 SAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIFQQHnWSLALNVA 437
Cdd:PLN00172  22 SAGPSDENLFRWTASIIGPSDSPYAGGVFFLSILFPPDYPFKPPKVQFTTKIYHPNINSNGSICLDILRDQ-WSPALTVS 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 19920682  438 KVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRAWTWKYA 483
Cdd:PLN00172 101 KVLLSISSLLTDPNPDDPLVPEIARVFKENRSRYEATAREWTQRYA 146
COG5078 COG5078
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
338-448 2.17e-09

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444052 [Multi-domain]  Cd Length: 146  Bit Score: 55.88  E-value: 2.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 338 RNNFLRGEANLLNSYESEG--ISAIPLDRQNNYWQATILGP---PGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHP 412
Cdd:COG5078   7 RSRRLANDYEELENILARGswIHFKATRGNPPKYEVTFNIRgiiRGGPTYGDTHRIEITLPESYPQAPPQVRWLTPIFHP 86

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 19920682 413 NVSR-HGDVGIDifQQHNWSLALNVAKVLLSVQSLLT 448
Cdd:COG5078  87 NIYEaGGSVCIG--RADHWTPSLTLDDLIISLARLLQ 121
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 234-265 9.14e-08

F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures.


Pssm-ID: 438852  Cd Length: 35  Bit Score: 48.21  E-value: 9.14e-08
                        10        20        30
                ....*....|....*....|....*....|..
gi 19920682 234 IPVEVMLKIFAYLDDMSLWMASEVCKQWHDIV 265
Cdd:cd09917   3 LPDEILLKILSYLDPRDLLRLSLVCKRWRELA 34
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 234-265 3.10e-07

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 46.71  E-value: 3.10e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 19920682   234 IPVEVMLKIFAYLDDMSLWMASEVCKQWHDIV 265
Cdd:pfam12937   4 LPDEILLQIFSYLDPKDLLRLALVCRRWRELA 35
PLN03029 PLN03029
type-a response regulator protein; Provisional
 104-170 4.30e-05

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 44.64  E-value: 4.30e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19920682  104 DKQEDEETENDVDIMGFEDLEDPQPaavPQHPNPQPpmePQDQQPAQPVIDLPQPVPEAAAPRRESP 170
Cdd:PLN03029 153 QKQENQEKQEKLEESEIQSEKQEQP---SQQPQSQP---QPQQQPQQPNNNKRKAMEEGLSPDRTRP 213
FBOX smart00256
A Receptor for Ubiquitination Targets;
234-265 6.99e-04

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 37.03  E-value: 6.99e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 19920682    234 IPVEVMLKIFAYLDDMSLWMASEVCKQWHDIV 265
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLI 32
 
Name Accession Description Interval E-value
UEV_Morgue-like cd23826
ubiquitin E2 variant (UEV) domain of Drosophila melanogaster Morgue and related proteins; ...
 337-483 8.01e-80

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: 244.84  E-value: 8.01e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 337 MRNNFLRGEA-NLLNSYESEGISAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVS 415
Cdd:cd23826   1 WRSRRLRRELkALHSDDPPEGISARPLDRSLLHLLATIEGPPGSPYEGGIFFLRIQIPESYPFRPPKVRFLTKIYHPNIS 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19920682 416 RHGDVGIDIFqQHNWSLALNVAKVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRAWTWKYA 483
Cdd:cd23826  81 RHGDICLDIL-EHNWSLALTIEKVLISIQSLLTDPYLEDPLVPEIAELYVNDREEFEQTAREWTWKYA 147
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
 342-479 1.85e-55

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: 181.62  E-value: 1.85e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682   342 LRGEANLLNSYESEGISAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVG 421
Cdd:pfam00179   2 LQKELKELLKDPPPGISAGPVDDNLFEWKVTIIGPDGTPYEGGVFKLSVEFPEDYPFKPPKVKFTTKIYHPNVDSSGEVC 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19920682   422 IDIFQQHNWSLALNVAKVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRAWT 479
Cdd:pfam00179  82 LDILKDERWSPALTLEQVLLSIQSLLSEPNPEDPLNAEAAKLYRKNREEFEKKVREYV 139
UBCc_UBE2D cd23792
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 ...
 358-482 6.26e-43

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: 148.95  E-value: 6.26e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 358 SAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIFQQHnWSLALNVA 437
Cdd:cd23792  20 SAGPVGDDLFHWQATIMGPPDSPYQGGVFFLNIHFPTDYPFKPPKVAFTTKIYHPNINSNGSICLDILKDQ-WSPALTIS 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 19920682 438 KVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRAWTWKY 482
Cdd:cd23792  99 KVLLSICSLLTDPNPDDPLVPEIAHLYKTDREKYEATAREWTRKY 143
UBCc_UEV cd00195
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain; ...
 342-450 6.30e-42

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: 145.13  E-value: 6.30e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 342 LRGEANLLNSYESEGISAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVG 421
Cdd:cd00195   3 LQKELKELQKNPPPGISVEPVDDDLFHWKATIKGPEGTPYEGGVFKLDIEFPDDYPFKPPKVRFLTPIYHPNVDPDGEIC 82

                        90       100
                ....*....|....*....|....*....
gi 19920682 422 IDIFQQHNWSLALNVAKVLLSVQSLLTDP 450
Cdd:cd00195  83 LDILKSEGWSPALTLRSVLLSIQSLLSDP 111
UBCc smart00212
Ubiquitin-conjugating enzyme E2, catalytic domain homologues; Proteins destined for ...
 355-484 1.28e-40

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: 142.82  E-value: 1.28e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682    355 EGISAIPLDRQN-NYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIFQQHNWSLA 433
Cdd:smart00212  15 PGFTAYPVDDENlLEWTGTIVGPPGTPYEGGVFKLTIEFPEDYPFKPPKVKFITKIYHPNVDSSGEICLDILKQEKWSPA 94

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 19920682    434 LNVAKVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRAWTWKYAM 484
Cdd:smart00212  95 LTLETVLLSLQSLLSEPNPDSPLNADAAELYKKNREEFKKKAREWTKKYAE 145
UBCc_UBE2A_2B cd23790
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzymes E2A, ...
 355-477 4.81e-36

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: 130.32  E-value: 4.81e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 355 EGISAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIFqQHNWSLAL 434
Cdd:cd23790  20 EGISAAPVEDNIMVWNAVIFGPEDTPWEGGTFKLRLEFSEEYPNKPPKVRFVSKMFHPNVYADGSICLDIL-QNRWSPTY 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 19920682 435 NVAKVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRA 477
Cdd:cd23790  99 DVSAILTSIQSLLTDPNPNSPANSEAAQLYQENRREYNRRVRE 141
UBCc_UBE2N cd23813
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 N ...
 345-482 1.33e-35

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 N and related proteins; The E2N subfamily includes mammalian ubiquitin-conjugating enzymes E2 N (UBE2N/UBCH13/UBC13/BLU), yeast ubiquitin-conjugating enzyme E2 13 (UBC13), and plant ubiquitin-conjugating enzyme E2 35-36 (UBC35/UBC13A/UBG13A, UBC36/UBC13B/UBG13B), which function as ubiquitin-conjugating enzymes (EC 2.3.2.23). UBE2N, also called Bendless-like ubiquitin-conjugating enzyme, forms heterodimers with UBE2V1 and UBE2V2, respectively. The UBE2V1/UBE2N and UBE2V2/UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. UBE2N also plays a role in the control of progress through the cell cycle and differentiation, as well as in the error-free DNA repair pathway, and contributes to the survival of cells after DNA damage. Saccharomyces cerevisiae UBC13 has a role in the DNA error-free post-replication repair (PRR) pathway. The UBC13/MMS2 heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. Arabidopsis thaliana UBC35 and UBC36 catalyze the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. They mediate transcriptional activation of target genes. They are required for post-replication repair of UV-damaged DNA and for adapting root developmental programs to suboptimal availability of iron.


Pssm-ID: 467433  Cd Length: 144  Bit Score: 129.24  E-value: 1.33e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 345 EANLLNSYESEGISAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDI 424
Cdd:cd23813   8 ETQRLLAEPVPGISATPDEDNLRYFDVVIDGPPDSPYEGGVFKLELFLPEEYPMAPPKVRFLTKIYHPNIDKLGRICLDI 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 19920682 425 FQQhNWSLALNVAKVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRAWTWKY 482
Cdd:cd23813  88 LKD-KWSPALQIRTVLLSIQALLSAPNPDDPLANDVAEHWKTNEAGAIATAREWTRLY 144
UBCc_UBE2E cd23793
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 ...
 369-479 6.68e-35

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: 127.49  E-value: 6.68e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 369 WQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIFQQhNWSLALNVAKVLLSVQSLLT 448
Cdd:cd23793  30 WVSTILGPPGSVYEGGVFFLDIHFPPDYPFKPPKVTFRTRIYHCNINSQGVICLDILKD-NWSPALTISKVLLSICSLLT 108

                        90       100       110
                ....*....|....*....|....*....|.
gi 19920682 449 DPYTEVCMEPELGYIYEHERERFEQLVRAWT 479
Cdd:cd23793 109 DCNPADPLVGSIATQYLTDREEHDRIAREWT 139
UBCc_SpUBC14-like cd23815
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Schizosaccharomyces pombe UBC14 ...
 349-482 9.63e-35

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: 127.02  E-value: 9.63e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 349 LNSYESEGISAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIFQQH 428
Cdd:cd23815  10 LQKNPIAGISAGPVEDNLFEWKGTILGPVGSPYEGGIFKFKITFPEDYPFKPPTVKFTTKIYHPNVDDDGSICLGILKSD 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 19920682 429 NWSLALNVAKVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRAWTWKY 482
Cdd:cd23815  90 AWKPSIKLVSVLNALLDLLEEPNPDDALVPSIAEQYKTDRAKFNKTAREWVKKY 143
UBCc_UBE2T cd23805
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 T ...
 342-482 1.03e-34

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: 126.87  E-value: 1.03e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 342 LRGEANLLNSYESEGISAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVG 421
Cdd:cd23805   3 LKRELQLLQKDPPPGISCWPKDDSLDELEAQIQGPEGTPYEGGVFKLEITIPERYPFEPPKVRFLTPIYHPNIDSAGRIC 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19920682 422 IDIFQ---QHNWSLALNVAKVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRAWTWKY 482
Cdd:cd23805  83 LDILKmppKGSWKPSLNISTVLTSIRLLLAEPNPDDPLMADIAAEYKYNRALFDAKAKEWTKKH 146
PLN00172 PLN00172
ubiquitin conjugating enzyme; Provisional
 358-483 5.29e-34

ubiquitin conjugating enzyme; Provisional


Pssm-ID: 177768 [Multi-domain]  Cd Length: 147  Bit Score: 125.25  E-value: 5.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682  358 SAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIFQQHnWSLALNVA 437
Cdd:PLN00172  22 SAGPSDENLFRWTASIIGPSDSPYAGGVFFLSILFPPDYPFKPPKVQFTTKIYHPNINSNGSICLDILRDQ-WSPALTVS 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 19920682  438 KVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRAWTWKYA 483
Cdd:PLN00172 101 KVLLSISSLLTDPNPDDPLVPEIARVFKENRSRYEATAREWTQRYA 146
UBCc_UBE2K cd23800
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 K ...
 356-479 1.37e-31

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: 118.43  E-value: 1.37e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 356 GISAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRH-GDVGIDIFqQHNWSLAL 434
Cdd:cd23800  20 GIKVELVGDDLTHLKGEIAGPPDTPYEGGTFVLDIKIPDTYPFEPPKMKFITKIWHPNISSQtGAICLDIL-KDQWSPAL 98

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 19920682 435 NVAKVLLSVQSLLTDPytevcmEP------ELGYIYEHERERFEQLVRAWT 479
Cdd:cd23800  99 TLRTALLSIQALLSAP------EPddpqdaVVAKQYKSNREEFEKTARHWT 143
UBCc_UBE2C cd23791
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 C ...
 354-450 1.55e-31

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: 118.06  E-value: 1.55e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 354 SEGISAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIFQQhNWSLA 433
Cdd:cd23791  16 DPGISAFPDGDNLFKWIGTITGPEGTVYEGLKYKLSLEFPSNYPYKAPTVKFETPCFHPNVDQHGNICLDILKE-KWSAL 94

                        90
                ....*....|....*..
gi 19920682 434 LNVAKVLLSVQSLLTDP 450
Cdd:cd23791  95 YDVRTILLSIQSLLGEP 111
PTZ00390 PTZ00390
ubiquitin-conjugating enzyme; Provisional
 356-488 4.21e-30

ubiquitin-conjugating enzyme; Provisional


Pssm-ID: 240397  Cd Length: 152  Bit Score: 114.52  E-value: 4.21e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682  356 GISAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIFQQhNWSLALN 435
Cdd:PTZ00390  21 GIKAEPDPGNYRHFKILMEGPDGTPYEGGYYKLELFLPEQYPMEPPKVRFLTKIYHPNIDKLGRICLDILKD-KWSPALQ 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19920682  436 VAKVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRAWTWKYAMYELI 488
Cdd:PTZ00390 100 IRTVLLSIQALLSAPEPDDPLDTSVADHFKNNRADAEKVAREWNQKYAKHNKL 152
UBCc_ScPEX4-like cd23812
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae Peroxin-4 ...
 347-450 1.12e-25

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: 102.24  E-value: 1.12e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 347 NLLNSYESEGISAIPLDRQNNY-WQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVS-RHGDVGIDI 424
Cdd:cd23812   9 ELQKEPNDPDIVLGPVEDDDLFrWEAVIKGPKDTPYEGGRFELAIQVPSNYPISPPKVKFVTKIFHPNVHfKTGEICLDI 88

                        90       100
                ....*....|....*....|....*.
gi 19920682 425 FQQhNWSLALNVAKVLLSVQSLLTDP 450
Cdd:cd23812  89 LKT-AWSPAWTLQSVCRAILALLSDP 113
UBCc_UBE2G1 cd23795
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 G1 ...
 349-453 7.56e-25

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 G1 and related proteins; The subfamily includes mammalian ubiquitin-conjugating enzymes E2 G1 (UBE2G1/UBC7/E217K), fission yeast ubiquitin-conjugating enzyme E2 15 (UBC15), plant ubiquitin-conjugating enzymes E2 7 (UBC7), E2 13 (UBC13) and E2 14 (UBC14). 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, UBE2G1 catalyzes 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. It may be involved in the degradation of muscle-specific proteins and may mediate polyubiquitination of CYP3A4. Schizosaccharomyces pombe UBC15 has a role in the formation of chromatin structures that influence the localization of transcriptional silencing factors. Arabidopsis thaliana UBC7, UBC13 and UBC14 are involved in the formation of multiubiquitin chains. They signal the protein for selective degradation.


Pssm-ID: 467415  Cd Length: 155  Bit Score: 100.32  E-value: 7.56e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 349 LNSYESEGISAIPLDRQNNY-WQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIFqq 427
Cdd:cd23795  13 LQKNPVEGFSAGLVDDSNIYeWEVMIIGPPDTLYEGGFFKAELTFPDDYPNSPPKMKFITEMWHPNVYPDGDVCISIL-- 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 19920682 428 HN--------------WSLALNVAKVLLSVQSLLTDPYTE 453
Cdd:cd23795  91 HPpgedkngyekaserWLPIHTVETILISVISMLSDPNDE 130
UBCc_UBE2G2 cd23796
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 G2 ...
 355-477 2.01e-24

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 G2 and related proteins; The subfamily includes mammalian ubiquitin-conjugating enzymes E2 G2 (UBE2G2/UBC7), yeast E2 ubiquitin-conjugating enzyme 7 (UBC7) 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. In vitro, UBE2G2 catalyzes 'Lys-48'-linked polyubiquitination. It is involved in endoplasmic reticulum-associated degradation (ERAD) and is required for sterol-induced ubiquitination of 3-hydroxy-3-methylglutaryl coenzyme A reductase and its subsequent proteasomal degradation. UBC7, also called ubiquitin-conjugating enzyme E2-18 kDa, functions in the degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system.


Pssm-ID: 467416 [Multi-domain]  Cd Length: 158  Bit Score: 99.27  E-value: 2.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 355 EGISAIPLDRQNNY-WQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIFQQ------ 427
Cdd:cd23796  17 EGIVAGPVSEDNFFeWEALIQGPEGTPFEGGVFPARLTFPKDYPLSPPKMKFTCEMFHPNIYPDGRVCISILHApgddpm 96

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19920682 428 ------HNWSLALNVAKVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRA 477
Cdd:cd23796  97 gyesssERWSPVQSVEKILLSVVSMLAEPNDESGANVDAAKMWREDREEFNKIAKA 152
UBCc_UBE2R cd23803
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 ...
 342-452 6.88e-23

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 R1-R2 and related proteins; The E2R subfamily includes mammalian ubiquitin-conjugating enzymes E2 R1 (UBE2R1/UBCH3/CDC34, EC 2.3.2.23 and EC 2.3.2.24), and E2 R2 (UBE2R2/UBC3B/CDC34B, EC 2.3.2.23), which accept ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, UBE2R1 catalyzes 'Lys-48'-linked polyubiquitination. It also involved in the degradation of beta-catenin. In vitro, UBE2R2 catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. It may be involved in the degradation of katenin.


Pssm-ID: 467423 [Multi-domain]  Cd Length: 170  Bit Score: 95.12  E-value: 6.88e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 342 LRGEANLLNSYESEGISAIPLDRQNNY-WQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDV 420
Cdd:cd23803   3 LQLELKSLQEEPVEGFRVTLVDEDNLFeWEVAIFGPPNTLYEGGYFKAHMKFPPDYPYSPPSFRFLTKMWHPNVYENGDV 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 19920682 421 GIDIFQ------------QHNWSLALNVAKVLLSVQSLLTDPYT 452
Cdd:cd23803  83 CISILHppvddpqsgelpSERWNPTQNVRTILLSVISLLNEPNT 126
UBCc_ApmR795-like cd23833
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Acanthamoeba polyphaga mimivirus ...
 349-450 1.62e-22

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Acanthamoeba polyphaga mimivirus bifunctional E2/E3 enzyme R795 and related proteins; R795 (EC 2.3.2.23/EC 2.3.2.27) is a bifunctional enzyme which acts as an E2 ubiquitin-conjugating enzyme that catalyzes the covalent attachment of ubiquitin to other proteins. It also acts as a RING-type E3 ubiquitin-protein transferase.


Pssm-ID: 467438 [Multi-domain]  Cd Length: 117  Bit Score: 92.29  E-value: 1.62e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 349 LNSYESEGISAI---PLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIF 425
Cdd:cd23833   7 LRSLLKNPHPNIdvyPSEEDIGFWKVLMEGPEGTPYEGGVFLLYVEFPEEYPVKPPEVRFITPIYHCNINSDGRICHSIL 86

                        90       100
                ....*....|....*....|....*
gi 19920682 426 QQhNWSLALNVAKVLLSVQSLLTDP 450
Cdd:cd23833  87 DR-NYTPDTTMREILDAVYGLLLTP 110
UBCc_UBE2S cd23804
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 S ...
 349-479 1.33e-19

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 S and related domains; The E2S subfamily includes mammalian ubiquitin-conjugating enzymes E2 S (UBE2S/E2EPF), plant ubiquitin-conjugating enzyme E2 22 (UBC22), and similar proteins. They are ubiquitin-conjugating enzymes (EC2.3.2.23) that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins. UBE2S catalyzes 'Lys-11'-linked polyubiquitination. It acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. UBE2S acts by specifically elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit. It also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is however unclear whether UBE2D1/UBCH5 acts as an E2 enzyme for the APC/C in vivo. UBE2S is also involved in ubiquitination and subsequent degradation of VHL, resulting in an accumulation of HIF1A. In vitro, it can promote polyubiquitination using all 7 ubiquitin Lys residues, except 'Lys-48'-linked polyubiquitination.


Pssm-ID: 467424  Cd Length: 146  Bit Score: 85.22  E-value: 1.33e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 349 LNSYESEGISAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIFQQh 428
Cdd:cd23804  14 LQSNPPEGIRVIPNEEDLTDIQAEIEGPEGTPYEGGVFRVKLVLGPDFPASPPKGYFLTKIFHPNVSPTGEICVNTLKK- 92

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 19920682 429 NWSLALNVAKVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRAWT 479
Cdd:cd23804  93 DWKPELGLRHILLTIRCLLIEPNPESALNEEAGKLLLEDYDEYAKRARLMT 143
UBCc_UBE2U cd23806
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 U ...
 342-476 2.25e-19

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 U and related proteins; The E2U subfamily includes mammalian ubiquitin-conjugating enzymes E2 U (UBE2U/, EC 2.3.2.23) and similar proteins. They are ubiquitin-conjugating enzymes that accept ubiquitin from the E1 complex and catalyze the covalent attachment to other proteins.


Pssm-ID: 467426  Cd Length: 141  Bit Score: 84.21  E-value: 2.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 342 LRGEANLLNSYESEGISAIPLDRQNNY-WQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRH-GD 419
Cdd:cd23806   3 LERELLELQENPLWGIEAKPVSDDNLFeWTAKIKGLKDTIWEGGIFRLTLKFSENYNYVPPEVQFHTIPFHPNVDPItGR 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 19920682 420 VGIDIFQQHN-WSLALNVAKVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVR 476
Cdd:cd23806  83 PCIDFLDDPEkWNPSYSLKSILLSIQVLLSNPVLENPVNPEAAEMLKTSPHLYRQMVL 140
UBCc_UBE2Z cd23809
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Z ...
 370-473 5.43e-19

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Z and related proteins; The E2Z subfamily includes mammalian ubiquitin-conjugating enzymes E2 Z (UBE2Z/HOYS7) 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. UBE2Z, also called Uba6-specific E2 conjugating enzyme 1 (Use1), acts as a ubiquitin-conjugating enzyme that accept ubiquitin from the E1 complex and catalyzes the covalent attachment to other proteins. It is a specific substrate for UBA6, not charged with ubiquitin by UBE1. It may be involved in apoptosis regulation.


Pssm-ID: 467429  Cd Length: 151  Bit Score: 83.44  E-value: 5.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 370 QATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTK-----ILHPNVSRHGDVGIDIFQQ---HNWSLALNVAKVLL 441
Cdd:cd23809  32 HALIIGPPDTPYEGGFFYFLLRFPPDYPISPPKVRLMTTgggrvRFNPNLYANGKVCLSILGTwtgPAWSPAQGLSSVLL 111

                        90       100       110
                ....*....|....*....|....*....|...
gi 19920682 442 SVQSLL-TDPYtevcmEPELGyiYEHERERFEQ 473
Cdd:cd23809 112 SIQSLMsENPY-----HNEPG--FEQERDPEDS 137
UBCc_UBE2I cd23798
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 I ...
 369-482 1.14e-18

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 I and related proteins; The E2I subfamily includes mammalian ubiquitin-conjugating enzymes E2 I (UBE2I/UBC9/UBCE9, EC 2.3.2.-), yeast ubiquitin-conjugating enzyme E2-18 kDa (UBC9, EC2.3.2.-), and plant SUMO-conjugating enzyme 1 (SCE1/AHUS5, EC2.3.2.-). UBE2I, also called SUMO-conjugating enzyme UBC9, RING-type E3 SUMO transferase UBC9, SUMO-protein ligase, ubiquitin carrier protein 9, ubiquitin carrier protein I, or ubiquitin-protein ligase I, accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3, SUMO4 and SUMO1P1/SUMO5 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. It can catalyze the formation of poly-SUMO chains. It is necessary for sumoylation of FOXL2 and KAT5 and essential for nuclear architecture and chromosome segregation. UBE2I also sumoylates p53/TP53 at 'Lys-386' and mediates sumoylation of ERCC6 which is essential for its transcription-coupled nucleotide excision repair activity. Saccharomyces cerevisiae UBC9, also called SUMO-conjugating enzyme UBC9, RING-type E3 SUMO transferase UBC9, ubiquitin carrier protein 9, ubiquitin-conjugating enzyme E2-18 kDa, acts as an E2 ubiquitin-like--protein ligase that mediates SUMO/Smt3 attachment to septins and PCNA. It may be involved in degradation of S- (CLB5) and M-phase cyclins (CLB2). Arabidopsis thaliana SCE1, also called SUMO-conjugating enzyme SCE1, protein EMBRYO DEFECTIVE 1637, or protein hus5 homolog, is a SUMO-conjugating enzyme that accepts the SUMO proteins from the E1 SUMO-activating heterodimer SAE1/SAE2 and catalyzes its covalent attachment to other proteins with the E3 SUMO ligases SIZ1 and MMS21. It associates with SIZ1 for sumoylation of the transcription factor GTE3.


Pssm-ID: 467418 [Multi-domain]  Cd Length: 152  Bit Score: 82.58  E-value: 1.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 369 WQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIF-QQHNWSLALNVAKVLLSVQSLL 447
Cdd:cd23798  38 WECGIPGKKGTPWEGGLYKLTMEFPEDYPSKPPKCKFDPPLFHPNVYPSGTVCLSILnEDKDWKPSITIKQILLGIQDLL 117

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 19920682 448 TDP------YTEVCMepelgyIYEHERERFEQLVRAWTWKY 482
Cdd:cd23798 118 DEPnlddpaQAEAYT------LYKNNREEYERRVRAQAKKY 152
UBCc_UBE2W cd23808
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzyme E2 W ...
 345-447 3.27e-18

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: 80.26  E-value: 3.27e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 345 EANLLNSYESEGISAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFL-TKI-LHPNVSRHGDVGI 422
Cdd:cd23808   7 ELKELQKNPPPGITLDVADNNLTEWIVTIEGAPGTLYEGEKFRLRFKFPPDYPIESPEVVFVgPPIpVHPHVYSNGHICL 86

                        90       100
                ....*....|....*....|....*
gi 19920682 423 DIFQQHnWSLALNVAKVLLSVQSLL 447
Cdd:cd23808  87 SILYDD-WSPALTVSSVCLSILSML 110
UBCc_UBE2L3 cd23801
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 L3, ...
 360-483 4.56e-18

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 L3, L5, L6 and related proteins; The E2L3-like subfamily includes mammalian ubiquitin-conjugating enzymes E2 L3 (UBE2L3/UBCH7/UBCE7), L5 (UBE2L5), L6 (UBE2L6/UBCH8), 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. UBE2L3 specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. It does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PRKN and ARIH1, that function like RING-HECT hybrids. In vitro, UBE2L3 catalyzes 'Lys-11'-linked polyubiquitination. It is involved in the selective degradation of short-lived and abnormal proteins. In addition to ubiquitin, UBE2L6 also catalyzes the covalent attachment of ISG15 to other proteins. It functions in the E6/E6-AP-induced ubiquitination of p53/TP53. It promotes ubiquitination and subsequent proteasomal degradation of FLT3.


Pssm-ID: 467421  Cd Length: 147  Bit Score: 80.77  E-value: 4.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 360 IPLDRQNNYWQATILgPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIFQQHNWSLALNVAKV 439
Cdd:cd23801  24 SVDESNVLKWTGLLV-PDNPPYNKGAFRIEITFPAEYPFKPPKITFKTKIYHPNVDEKGQVCLPIISPENWKPATKIDQV 102

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 19920682 440 LLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRAWTWKYA 483
Cdd:cd23801 103 LQALLALINDPEPEHPLRADLAEEYSKDKKKFLKNAEEFTKKHA 146
UBCc_invertebrate cd23955
ubiquitin-conjugating enzyme family protein; This subfamily includes ubiquitin-conjugating ...
 352-451 3.20e-17

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: 77.68  E-value: 3.20e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 352 YESEGISAIPLDrqNNY--WQATILGPPGsPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIFQQHN 429
Cdd:cd23955  13 EPLPGVSAEPLE--NDLfeWHVNIRGPDG-PYSGVILHLELTFPEDYPNSPPSVRLLTPLPHPNVFTGNYICLDMLENFA 89

                        90       100       110
                ....*....|....*....|....*....|.
gi 19920682 430 ---------WSLALNVAKVLLSVQSLLTDPY 451
Cdd:cd23955  90 khhskpysgWSPAYTVQSILLQLQAFLFDED 120
UBCc_UBE2F_UBE2M cd23794
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin conjugating enzymes E2 F, ...
 376-476 4.84e-17

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: 77.60  E-value: 4.84e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 376 PPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIFQQhNWSLALNVAKVLLSVQSLLTDPYTEVC 455
Cdd:cd23794  38 PDEGYYKGGTFVFEIDIPDNYPFEPPKVKCLTKIYHPNIDEEGNVCLNILRE-DWKPVLSLKDVILGLLFLFLEPNPDDP 116

                        90       100
                ....*....|....*....|.
gi 19920682 456 MEPELGYIYEHERERFEQLVR 476
Cdd:cd23794 117 LNKEAAELLLRDPEEFERNVR 137
UBCc_ScCDC34-like cd23811
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of Saccharomyces cerevisiae CDC34 and ...
 377-477 3.43e-16

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: 76.32  E-value: 3.43e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 377 PGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIFQQ------------HNWSLALNVAKVLLSVQ 444
Cdd:cd23811  42 PDSIYNGGYFKAEMVFPRDYPFSPPSFRFLPPIFHPNVYPDGRLCISILHSpgddyqsgepaaERWSPAQTVESVLLSIL 121

                        90       100       110
                ....*....|....*....|....*....|...
gi 19920682 445 SLLTDPYTEVCMEPELGYIYEHERERFEQLVRA 477
Cdd:cd23811 122 SLLEDPNINSPANVDAGVLYRKNREEYKDKVKK 154
UBCc_UBE2H cd23797
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 H ...
 375-477 1.41e-15

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 H and related proteins; The E2H subfamily includes mammalian ubiquitin-conjugating enzymes E2 H (UBE2H), yeast E2 ubiquitin-conjugating enzyme 8 (UBC8/GID3), and plant ubiquitin-conjugating enzyme E2 4-6 (UBC4-6). 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. UBE2H (also E3-independent, EC 2.3.2.24) transfers ubiquitin to MAEA, a core component of the CTLH E3 ubiquitin-protein ligase complex. In vitro, UBE2H catalyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitination. It might also ubiquitinate histone H2A. Saccharomyces cerevisiae UBC8 is required for the adaptation to the presence of glucose in the growth medium; it mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium. It is also required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1).


Pssm-ID: 467417  Cd Length: 138  Bit Score: 73.38  E-value: 1.41e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 375 GPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVS-RHGDVGIDIFQQhNWS----LaLNVAKVLLSvqSLLT- 448
Cdd:cd23797  33 GPKDTPYEGGVWKVRVELPDDYPYKSPSIGFVNKIFHPNIDeASGSVCLDVINQ-TWSpmydL-VNIFEVFLP--QLLTy 108

                        90       100       110
                ....*....|....*....|....*....|...
gi 19920682 449 ----DPYTevcmePELGYIYEHERERFEQLVRA 477
Cdd:cd23797 109 pnpsDPLN-----GEAAALMLHDPEAYKEKVKE 136
UEV_UBE2V cd23807
ubiquitin E2 variant (UEV) domain of ubiquitin-conjugating enzyme E2 variant 1, 2 and related ...
 363-450 4.95e-14

ubiquitin E2 variant (UEV) domain of ubiquitin-conjugating enzyme E2 variant 1, 2 and related proteins; The E2V subfamily includes mammalian ubiquitin-conjugating enzyme E2 variant 1 (UBE2V1/CROC1/UBE2V/UEV1) and variant 2 (UBE2V2/MMS2/UEV2), yeast ubiquitin-conjugating enzyme variant MMS2, plant ubiquitin-conjugating enzyme E2 variant 1A (UEV1A/MMZ1) and variant 1B (UEV1B/MMZ2), and similar proteins. They have no ubiquitin ligase activity on their own. UBE2V1 (also called UEV-1, CROC-1, or TRAF6-regulated IKK activator 1 beta Uev1A) and UBE2V2 (also called DDVit 1, enterocyte differentiation-associated factor 1 (EDAF-1), enterocyte differentiation-promoting factor 1 (EDPF-1), MMS2 homolog, or vitamin D3-inducible protein) form heterodimers with UBE2N, respectively. Saccharomyces cerevisiae UEV MMS2 has a role in the DNA error-free postreplication repair (PRR) pathway. It forms a heterodimer with UBC13. Arabidopsis thaliana UEV1A and UEV1A form heterodimers with UBC35 or UBC36. The heterodimers possess ubiquitin-conjugating enzyme (EC 2.3.2.23) activity, catalyzing the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination does not lead to protein degradation by the proteasome. Members of this subfamily may mediate transcriptional activation of target genes and plays a role in the control of progress through the cell cycle and differentiation. UEVs are homologous to E2 ubiquitin ligases but lack the conserved cysteine residue required for catalytic activity.


Pssm-ID: 467427  Cd Length: 134  Bit Score: 69.05  E-value: 4.95e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 363 DRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRH-GDVGIDIFQQ-HNWSLALNVAKVL 440
Cdd:cd23807  34 DMTLTHWNGTIIGPPGTVFENRIYSLKIECGENYPDEPPTVRFVTKINLPCVDQSnGVVDPRKFPVlKNWQRNYTIETVL 113

                        90
                ....*....|
gi 19920682 441 LSVQSLLTDP 450
Cdd:cd23807 114 TELRREMTSK 123
UBCc_UBE2J cd23799
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 J1, ...
 342-450 2.16e-13

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 J1, J2 and related proteins; The E2J subfamily includes mammalian ubiquitin-conjugating enzymes E2 J1 (UBE2J1/HSPC153/HSPC205/NCUBE1) and J2 (UBE2J2/NCUBE1), yeast ubiquitin-conjugating enzyme E2 6 (UBC6/DOA2), and plant ubiquitin-conjugating enzyme E2 32-34 (UBC32-34). 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. UBE2J1 and UBE2J2 are non-canonical ubiquitin-conjugating enzyme (NCUBE), which function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD). Saccharomyces cerevisiae UBC6 functions in 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 DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains.


Pssm-ID: 467419  Cd Length: 134  Bit Score: 67.11  E-value: 2.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 342 LRGEANLLNSYESEGISAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTkilhPNvsrhG--D 419
Cdd:cd23799   3 LLKELRELQKDPPPYIVAAPLEDNILEWHFTIRGPPDTPYEGGIYHGKIVFPPDYPFKPPSIYMLT----PN----GrfE 74

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 19920682 420 VGIDI------FQQHNWSLALNVAKVLLSVQSLLTDP 450
Cdd:cd23799  75 TNTKIclsissFHPESWNPAWSIRTILIGLLSFMPED 111
UBCc_TcUBE-like cd23828
Ubiquitin-conjugating enzyme E2, putative catalytic (UBCc) domain of Trypanosoma cruzi ...
 369-420 1.55e-10

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: 58.55  E-value: 1.55e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 19920682 369 WQATILGPPGS-PYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDV 420
Cdd:cd23828  38 WRVVVKPPANSiVYAGNTYELLVIFSDDYPHEPPKVRFLTPIYSPLVSPEGSV 90
UBCc_BIRC6 cd23810
Ubiquitin-conjugating enzyme E2, catalytic (UBCc)-like domain of baculoviral IAP ...
 363-488 2.23e-10

Ubiquitin-conjugating enzyme E2, catalytic (UBCc)-like domain of baculoviral IAP repeat-containing protein 6 (BIRC6) and related proteins; BIRC6, also BIR repeat-containing ubiquitin-conjugating enzyme (BRUCE), RING-type E3 ubiquitin transferase (EC 2.3.2.27) BIRC6, or ubiquitin-conjugating BIR domain enzyme apollon (APOLLON), is an anti-apoptotic protein which can regulate cell death by controlling caspases and by acting as an E3 ubiquitin-protein ligase. It has an unusual ubiquitin conjugation system in that it could combine in a single polypeptide, ubiquitin conjugating (E2) with ubiquitin ligase (E3) activity, forming a chimeric E2/E3 ubiquitin ligase. Its targets include CASP9 and DIABLO/SMAC. BIRC6 acts as an inhibitor of CASP3, CASP7, and CASP9. BIRC6 is an important regulator for the final stages of cytokinesis. It is crucial for normal vesicle targeting to the site of abscission, but also for the integrity of the midbody and the midbody ring, and its striking ubiquitin modification.


Pssm-ID: 467430 [Multi-domain]  Cd Length: 205  Bit Score: 60.25  E-value: 2.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 363 DRQN-NYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLT----KI-LHPNVSRHGDVGIDIF------QQHNW 430
Cdd:cd23810  31 DEERmDVMKALITGPEDTPYANGCFLFDIFFPPDYPQSPPKVNLLTtgggSVrFNPNLYNDGKVCLSLLgtwsgpPGEKW 110

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 431 SLAL-NVAKVLLSVQSLL--TDPYTEvcmEPelGyiYEHER---------ERFEQLVRAWTWKYAMYELI 488
Cdd:cd23810 111 NPGTsTLLQVLVSIQSLIlvPEPYFN---EP--G--YERSRgtpegdaasREYNANIRYNTVRWAMLEQL 173
UBCc_UBE2O cd23837
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 O ...
 371-451 7.51e-10

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 O and related proteins; The E2O subfamily includes mammalian ubiquitin-conjugating enzymes E2 O (UBE2O, EC 2.3.2.24), plant ubiquitin-conjugating enzyme E2 23-26 (UBC23-26, EC2.3.2.23) and E2 38-39 (UBC38-39, EC2.3.2.23), and similar proteins. UBE2O is an E2/E3 hybrid ubiquitin-protein ligase that displays both E2 and E3 ligase activities and mediates monoubiquitination of target proteins. Arabidopsis thaliana UBC proteins accept the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. UBC24, also called PHO2, mediates PHO1 degradation through multivesicular body-mediated vacuolar proteolysis in response to inorganic phosphate (Pi) availability. It negatively regulates the protein abundance of PHF1 and PHT1s under Pi-sufficient conditions by facilitating the degradation of PHT1 proteins at the endomembrane.


Pssm-ID: 467439 [Multi-domain]  Cd Length: 198  Bit Score: 58.33  E-value: 7.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 371 ATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKI---LHPNVSRHGDVGIDIF------QQHNWSLAL-NVAKVL 440
Cdd:cd23837  36 ALIVGPEGTPYEDGLFFFDIQLPPDYPNVPPKVHYHSWTggrLNPNLYEDGKVCLSLLgtwsgkGTEKWTPKSsNLLQVL 115

                        90
                ....*....|...
gi 19920682 441 LSVQSLL--TDPY 451
Cdd:cd23837 116 VSIQGLVlvKEPY 128
COG5078 COG5078
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
338-448 2.17e-09

Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444052 [Multi-domain]  Cd Length: 146  Bit Score: 55.88  E-value: 2.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682 338 RNNFLRGEANLLNSYESEG--ISAIPLDRQNNYWQATILGP---PGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHP 412
Cdd:COG5078   7 RSRRLANDYEELENILARGswIHFKATRGNPPKYEVTFNIRgiiRGGPTYGDTHRIEITLPESYPQAPPQVRWLTPIFHP 86

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 19920682 413 NVSR-HGDVGIDifQQHNWSLALNVAKVLLSVQSLLT 448
Cdd:COG5078  87 NIYEaGGSVCIG--RADHWTPSLTLDDLIISLARLLQ 121
UEV_AKTIP cd23814
ubiquitin E2 variant (UEV) domain of AKT-interacting protein and related proteins; AKTIP, ...
 342-417 2.36e-09

ubiquitin E2 variant (UEV) domain of AKT-interacting protein and related proteins; AKTIP, also called Ft1, or fused toes protein homolog, is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). AKTIP regulates apoptosis by enhancing phosphorylation and activation of AKT1. It increases release of TNFSF6 via the AKT1/GSK3B/NFATC1 signaling cascade. AKTIP contains a UEV domain that is homologous to E2 ubiquitin ligases but lacks the conserved cysteine residue required for catalytic activity.


Pssm-ID: 467434  Cd Length: 112  Bit Score: 54.86  E-value: 2.36e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19920682 342 LRGEANLLNSYESEGISAIPLDRQNNYWQATILGPPGsPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRH 417
Cdd:cd23814   3 LLAEYKLLREQPPPGVYVLPSAENPLLWHGVIFVRSG-LYKGGIFRFTISIPDNYPDGPPRVTFLSPVFHPLVDPQ 77
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 234-265 9.14e-08

F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures.


Pssm-ID: 438852  Cd Length: 35  Bit Score: 48.21  E-value: 9.14e-08
                        10        20        30
                ....*....|....*....|....*....|..
gi 19920682 234 IPVEVMLKIFAYLDDMSLWMASEVCKQWHDIV 265
Cdd:cd09917   3 LPDEILLKILSYLDPRDLLRLSLVCKRWRELA 34
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 234-265 3.10e-07

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 46.71  E-value: 3.10e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 19920682   234 IPVEVMLKIFAYLDDMSLWMASEVCKQWHDIV 265
Cdd:pfam12937   4 LPDEILLQIFSYLDPKDLLRLALVCRRWRELA 35
F-box_FBXO48 cd22113
F-box domain found in F-box only protein 48 (FBXO48) and similar proteins; FBXO48, also called ...
 231-275 1.41e-06

F-box domain found in F-box only protein 48 (FBXO48) and similar proteins; FBXO48, also called FBX48, is one of the paralogs of the F-box only protein 7 (FBXO7), which is the causative gene for PARK15 (also known as Parkinsonian-pyramidal disease, PPD). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438885  Cd Length: 46  Bit Score: 45.00  E-value: 1.41e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 19920682 231 VNIIPVEVMLKIFAYLDDMSLWMASEVCKQWHDIVgKNTAQsMWK 275
Cdd:cd22113   1 IELLPPEMSLRIFSQLDVQSLCRASQTCKTWNDLI-ENSDY-LWR 43
F-box_SpPof1-like cd22147
F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar ...
 233-275 2.14e-06

F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar proteins; SpPof1, also called F-box/WD repeat-containing protein pof1, probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It is required for the inactivation of zip1 via ubiquitination. This subfamily also includes Saccharomyces cerevisiae methionine-requiring protein 30 (ScMET30, also called E3 ubiquitin ligase complex SCF(Met30) subunit MET30), Aspergillus niger sulfur controller B (AnSCONB, also called sulfur metabolite repression control protein B) and Neurospora crassa sulfur controller 2 (NcSCON2, also called sulfur metabolite repression control protein 2). ScMET30 acts as a transcriptional inhibitor that negatively regulates the expression of sulfur amino acid biosynthesis genes. It controls cell cycle function (being required for the G1/S transition and M-phase but not the S-phase), sulfur metabolism, and methionine biosynthesis as part of the E3 ubiquitin ligase complex SCF(Met30). AnSCONB and NcSCON2 are components of the SCF (sconB/scon-2) E3 ubiquitin ligase complexes involved in the regulation of sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438918  Cd Length: 46  Bit Score: 44.61  E-value: 2.14e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 19920682 233 IIPVEVMLKIFAYLDDMSLWMASEVCKQWHDIVgknTAQSMWK 275
Cdd:cd22147   4 ALPVELSLKILSYLDAKSLCRAAQVSKKWRNLA---DDDELWK 43
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 234-265 1.69e-05

F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 425796  Cd Length: 43  Bit Score: 41.76  E-value: 1.69e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 19920682   234 IPVEVMLKIFAYLDDMSLWMASEVCKQWHDIV 265
Cdd:pfam00646   4 LPDDLLLEILSRLDPKDLLRLSLVSKRWRSLV 35
PLN03029 PLN03029
type-a response regulator protein; Provisional
 104-170 4.30e-05

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 44.64  E-value: 4.30e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19920682  104 DKQEDEETENDVDIMGFEDLEDPQPaavPQHPNPQPpmePQDQQPAQPVIDLPQPVPEAAAPRRESP 170
Cdd:PLN03029 153 QKQENQEKQEKLEESEIQSEKQEQP---SQQPQSQP---QPQQQPQQPNNNKRKAMEEGLSPDRTRP 213
F-box_FBXL2-like cd22115
F-box domain found in F-box/LRR-repeat protein 2 (FBXL2), F-box/LRR-repeat protein 20 (FBXL20) ...
 229-262 4.46e-05

F-box domain found in F-box/LRR-repeat protein 2 (FBXL2), F-box/LRR-repeat protein 20 (FBXL20) and similar proteins; The family includes FBXL2 and FBXL30. FBXL2, also called F-box and leucine-rich repeat protein 2, or F-box protein FBL2/FBL3, is a calcium-activated substrate-recognition component of an SCF (SKP1-cullin-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Unlike many F-box proteins, FBXL2 does not seem to target phosphodegron within its substrates but rather calmodulin-binding motifs and is thereby antagonized by calmodulin. FBXL20, also called SCRAPPER, F-box and leucine-rich repeat protein 20, or F-box/LRR-repeat protein 2-like, is a component of a synapse-localized SCF-type E3 ubiquitin ligase which regulates neural transmission. It is widely expressed in the central nervous system and plays an important role in the ubiquitin-dependent degradation of regulating synaptic membrane exocytosis 1 (RIM1), which is an important factor in the release of synaptic vesicles. It may also mediate the ubiquitin degradation of E-cadherin resulting in an increased invasive ability of malignant cells. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438887  Cd Length: 45  Bit Score: 40.86  E-value: 4.46e-05
                        10        20        30
                ....*....|....*....|....*....|....
gi 19920682 229 NIVNIIPVEVMLKIFAYLDDMSLWMASEVCKQWH 262
Cdd:cd22115   2 LINKKLPKELLLRIFSFLDVVTLCRCAQVSKYWN 35
F-box_FBXW12 cd22137
F-box domain found in F-box/WD repeat-containing protein 12 (FBXW12) and similar proteins; ...
 234-275 5.51e-05

F-box domain found in F-box/WD repeat-containing protein 12 (FBXW12) and similar proteins; FBXW12, also called F-box and WD-40 domain-containing protein 12, or F-box only protein 35 (FBXO35), is the substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It functions as an epithelial growth suppressor. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438909  Cd Length: 44  Bit Score: 40.44  E-value: 5.51e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 19920682 234 IPVEVMLKIFAYLDDMSLWMASEVCKQWHDIVGKNtaqSMWK 275
Cdd:cd22137   3 LPDLPMLRIFSFLDAFSLLQAAQVNKQWNKVADSD---YLWR 41
F-box_FBXO11 cd22091
F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called ...
 234-275 1.08e-04

F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called FBX11, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1), is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438863  Cd Length: 45  Bit Score: 39.71  E-value: 1.08e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 19920682 234 IPVEVMLKIFAYLDDMSLWMASEVCKQWHDIVGKntaQSMWK 275
Cdd:cd22091   4 LPDEVLLKIFSYLLEQDLCRAAQVCKRFNTLAND---PELWK 42
F-box_FBXL5 cd22118
F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also ...
 234-264 1.10e-04

F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also called F-box and leucine-rich repeat protein 5, F-box protein FBL4/FBL5, or p45SKP2-like protein, is the substrate-recognition component of an SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438890  Cd Length: 41  Bit Score: 39.63  E-value: 1.10e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 19920682 234 IPVEVMLKIFAYLDDMSLWMASEVCKQWHDI 264
Cdd:cd22118   4 LPPEIMLKIFSYLNPQDLCRCAQVCTKWSQL 34
F-box_FBXO15 cd22093
F-box domain found in F-box only protein 15 (FBXO15) and similar proteins; FBXO15, also called ...
 234-275 1.29e-04

F-box domain found in F-box only protein 15 (FBXO15) and similar proteins; FBXO15, also called FBX15, has a novel dual molecular function by controlling transcriptional repression and being part of SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligases, which is essential for stress response, gliotoxin production and virulence in the opportunistic human pathogen Aspergillus fumigatus. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438865  Cd Length: 46  Bit Score: 39.54  E-value: 1.29e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 19920682 234 IPVEVMLKIFAYLDDMSLWMASEVCKQWHDIVGKNtaqSMWK 275
Cdd:cd22093   4 LPSEILLKILSYLDASSLLCISCVNKLFYQLANDN---ALWR 42
F-box_unchar cd22138
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 ...
 232-275 2.60e-04

F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 (FBXO13); The family corresponds to a group of uncharacterized F-box proteins which show sequence similarity to F-box only protein 13 (FBXO13). FBXO13, also called FBX13, or F-box/LRR-repeat protein 17 (FBL17), or F-box and leucine-rich repeat protein 17 (FBXL17), is the substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438910  Cd Length: 45  Bit Score: 38.46  E-value: 2.60e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 19920682 232 NIIPVEVMLKIFAYLDDMSLWMASEVCKQWHDIVgknTAQSMWK 275
Cdd:cd22138   2 QSLPVECQLKIFSFLSEVDKCLAATVCRSWSELI---RSPRLWR 42
F-box_DdgacFF-like cd22148
F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) ...
 230-276 2.96e-04

F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) and similar proteins; DdgacFF, also called GTPase activating factor for raC protein FF, is a Rho GTPase-activating protein involved in the signal transduction pathway. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438919  Cd Length: 44  Bit Score: 38.42  E-value: 2.96e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 19920682 230 IVNIIPVEVMLKIFAYLDDMSLWMASEVCKQWHDIVGKNtaqSMWKA 276
Cdd:cd22148   1 FISLLPEHLALKILSYLSPKELLIASQVSKTWRRLASSN---ELWKA 44
F-box_FBXL1 cd22114
F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also ...
 234-262 3.86e-04

F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also called S-phase kinase-associated protein 2, cyclin-A/CDK2-associated protein p45, F-box protein Skp2, or p45skp2, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. It specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438886  Cd Length: 41  Bit Score: 38.16  E-value: 3.86e-04
                        10        20
                ....*....|....*....|....*....
gi 19920682 234 IPVEVMLKIFAYLDDMSLWMASEVCKQWH 262
Cdd:cd22114   4 LPDELLLGIFSCLCLPDLLKVSQVCKRWY 32
FBOX smart00256
A Receptor for Ubiquitination Targets;
234-265 6.99e-04

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 37.03  E-value: 6.99e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 19920682    234 IPVEVMLKIFAYLDDMSLWMASEVCKQWHDIV 265
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLI 32
F-box_FBXL8 cd22121
F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also ...
 232-265 8.88e-04

F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also called F-box and leucine-rich repeat protein 8, or F-box protein FBL8, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438893  Cd Length: 35  Bit Score: 36.95  E-value: 8.88e-04
                        10        20        30
                ....*....|....*....|....*....|....
gi 19920682 232 NIIPVEVMLKIFAYLDDMSLWMASEVCKQWHDIV 265
Cdd:cd22121   1 NALPEEILVHIFRHLSLRDRYAAAQVCKHWREAA 34
UBCc_UBE2Q cd23802
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-conjugating enzyme E2 Q1, ...
 390-447 1.22e-03

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: 39.54  E-value: 1.22e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19920682 390 IYFPERYPMTPPTVRFLT-KILHPNVSRHGDVGIDIFQQHNWSLALNVAKVLLSVQSLL 447
Cdd:cd23802  65 LRFPDLYPFYPPFVRVVRpRLKGGTGHVGGAICMELLTLSGWSPAYSIESVLLQIRALL 123
F-box_FBXO42 cd22110
F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called ...
 231-265 1.41e-03

F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called FBX42, or just one F-box and Kelch domain-containing protein (JFK), is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It specifically recognizes p53/TP53, promoting its ubiquitination and degradation. FBXO42 is also involved in the ubiquitin-proteasome system that may play a role in the pathogenesis of Parkinson's disease (PD). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438882  Cd Length: 38  Bit Score: 36.16  E-value: 1.41e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 19920682 231 VNIIPVEVMLKIFAYL---DDMSlwMASEVCKQWHDIV 265
Cdd:cd22110   1 INDLPEEILEYILSYLspyGDLK--SAALVCKRWHRII 36
F-box_AtGID2-like cd22151
F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, ...
 234-262 1.63e-03

F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, also called protein SLEEPY 1, is an essential component of the SCF-type E3 ligase complex, SCF(GID2), a complex that positively regulates the gibberellin signaling pathway. Upon gibberellin treatment, the SCF(GID2) complex mediates the ubiquitination and subsequent degradation of DELLA proteins (GAI, RGA and RGL2), some repressors of the gibberellin pathway, leading to the activation of the pathway. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438922  Cd Length: 44  Bit Score: 36.14  E-value: 1.63e-03
                        10        20
                ....*....|....*....|....*....
gi 19920682 234 IPVEVMLKIFAYLDDMSLWMASEVCKQWH 262
Cdd:cd22151   3 LPDDLLQEIFKRLDPKSLARAACVCRRWR 31
F-box_FBXW5 cd22132
F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, ...
 234-262 1.80e-03

F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, also called F-box and WD-40 domain-containing protein 5, is the substrate-recognition component of both SCF (SKP1-CUL1-F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438904 [Multi-domain]  Cd Length: 46  Bit Score: 36.05  E-value: 1.80e-03
                        10        20
                ....*....|....*....|....*....
gi 19920682 234 IPVEVMLKIFAYLDDMSLWMASEVCKQWH 262
Cdd:cd22132   4 LPDSLLLHIFSYLSPKDLLAAGQVCKQWY 32
F-box_ScCDC4-like cd22141
F-box domain found in Saccharomyces cerevisiae cell division control protein 4 (ScCDC4) and ...
 234-279 2.00e-03

F-box domain found in Saccharomyces cerevisiae cell division control protein 4 (ScCDC4) and similar proteins; ScCDC4 is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It is essential for initiation of DNA replication and separation of the spindle pole bodies to form the poles of the mitotic spindle. It also plays a role in bud development, fusion of zygotic nuclei after conjugation and various aspects of sporulation. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438913  Cd Length: 47  Bit Score: 36.00  E-value: 2.00e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 19920682 234 IPVEVMLKIFAYLDDMSLWMASEVCKQWHDIVgKNTAqsMWKAYIK 279
Cdd:cd22141   4 LPFEISLKIFNYLQFEDLLNSLGVSKKWNKII-RNTA--LWKKLLI 46
F-box_FBXO41 cd22109
F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called ...
 242-265 2.05e-03

F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called FBX41, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a novel central nervous system (CNS)-specific F-box protein that localizes to the centrosome and the cytoplasm of neurons and promotes neuronal migration. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438881  Cd Length: 47  Bit Score: 36.15  E-value: 2.05e-03
                        10        20
                ....*....|....*....|....
gi 19920682 242 IFAYLDDMSLWMASEVCKQWHDIV 265
Cdd:cd22109  14 VFSYLDTKSLLRCAEVCREWRDVS 37
PHA03247 PHA03247
large tegument protein UL36; Provisional
 126-209 2.12e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920682   126 PQPAAVPQHPNPQPPMEPQDQQPAQPVIDlPQPVPEaaaPRRESPERDFEH----ERAINPFLLPIKRPRATAPLALPHY 201
Cdd:PHA03247 2920 QPQPPPPPQPQPPPPPPPRPQPPLAPTTD-PAGAGE---PSGAVPQPWLGAlvpgRVAVPRFRVPQPAPSREAPASSTPP 2995


                  ....*...
gi 19920682   202 MHELADGR 209
Cdd:PHA03247 2996 LTGHSLSR 3003
F-box_FBXO3 cd22084
F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called ...
 234-282 2.15e-03

F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called FBX3, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. It also promotes ubiquitylation and transcriptional activity of AIRE (autoimmune regulator). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438856  Cd Length: 49  Bit Score: 36.08  E-value: 2.15e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 19920682 234 IPVEVMLKIFAYLDDMSLWMASEVCKQWHDIVGKNtaqSMWKAYIKQRW 282
Cdd:cd22084   4 LPSDPLLNILSFLDYRDLISCSQVCRRLNQLCSHD---PLWKRLCKKYW 49
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
 121-165 2.24e-03

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 39.82  E-value: 2.24e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 19920682  121 EDLEDPQPAA--VPQHPNPQPPMEPQDQQPAQPVIDLPQPVPEAAAP 165
Cdd:PLN02983 139 EALPQPPPPApvVMMQPPPPHAMPPASPPAAQPAPSAPASSPPPTPA 185
F-box_FBXO18 cd22095
F-box domain found in F-box only protein 18 (FBXO18) and similar proteins; FBXO18, also called ...
 231-265 2.69e-03

F-box domain found in F-box only protein 18 (FBXO18) and similar proteins; FBXO18, also called FBX18, or F-box DNA helicase 1 (FBH1), is a 3'-5' DNA helicase and the substrate-recognition component of the SCF(FBH1) E3 ubiquitin ligase complex that plays a key role in response to stalled/damaged replication forks. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438867  Cd Length: 48  Bit Score: 35.71  E-value: 2.69e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 19920682 231 VNIIPVEVMLKIFAYLDDMSLWM-ASEVCKQWHDIV 265
Cdd:cd22095   2 IQQLPEELLRNIFAFLPAEDLYQnISLVCRHWRDIV 37
F-box_AtTIR1-like cd22159
F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), ...
 232-267 2.94e-03

F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), coronatine-insensitive protein 1 (COI1) and similar proteins; TIR1, also called F-box/LRR-repeat protein 1 (FBL1), is part of an SCF (SKP1-cullin-F-box) protein ligase complex that promotes the ubiquitin-dependent proteolysis of a family of transcriptional regulators known as Aux/IAAs in an auxin-dependent manner. TIR1 is an auxin receptor that plays a potential role in plant hormone signaling. COI1, also called F-box/LRR-repeat protein 2 (FBL2), is the substrate-recruiting module of an SCF ubiquitin E3 ligase complex. It mediates jasmonate signalling by promoting hormone-dependent ubiquitylation and degradation of transcriptional repressor JASMONATE ZIM-domain (JAZ) family proteins. This subfamily also includes Arabidopsis thaliana EIN3-binding F-box protein 1 (EBF1). EBF1, also called F-box/LRR-repeat protein 6 (FBL6), is a component of the SCF(EBF1) E3 ubiquitin ligase complex, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (probably including EIN3 and EIL1). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438930  Cd Length: 40  Bit Score: 35.52  E-value: 2.94e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 19920682 232 NIIPVEVMLKIFAYLDD------MSLwmaseVCKQWHDIVGK 267
Cdd:cd22159   2 DLLPDEILELIFSYLSDpwdrnsCSL-----VCKRWYRLERA 38
F-box_FBXO10 cd22090
F-box domain found in F-box only protein 10 (FBXO10) and similar proteins; FBXO10, also called ...
 231-265 7.22e-03

F-box domain found in F-box only protein 10 (FBXO10) and similar proteins; FBXO10, also called FBX10, or PRMT11, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The SCF(FBXO10) complex mediates ubiquitination and degradation of BCL2, an anti-apoptotic protein, thereby playing a role in apoptosis by controlling the stability of BCL2. It also associates with the receptor for advanced glycation end products (RAGE) to mediate its ubiquitination and degradation. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438862  Cd Length: 50  Bit Score: 34.64  E-value: 7.22e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 19920682 231 VNIIPVEVMLKIFAYLDDMSLWMASEVCKQWHDIV 265
Cdd:cd22090   2 VTGLPLELWRLILAYLPVRDLCRCCQVCRAWYELI 36
F-box_FBXO45 cd22111
F-box domain found in F-box only protein 45 (FBXO45) and similar proteins; FBXO45, also called ...
 235-262 7.27e-03

F-box domain found in F-box only protein 45 (FBXO45) and similar proteins; FBXO45, also called FBX45, or F-box/SPRY domain-containing protein 1, functions as the substrate-recognition component of E3 ubiquitin ligase complexes. It is critical for synaptogenesis, neuronal migration, and synaptic transmission. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438883  Cd Length: 36  Bit Score: 34.18  E-value: 7.27e-03
                        10        20
                ....*....|....*....|....*...
gi 19920682 235 PVEVMLKIFAYLDDMSLWMASEVCKQWH 262
Cdd:cd22111   5 PSRVLEVIFSYLDLPDLRNCSLVCKSWY 32
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 231-274 8.07e-03

F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also called F-box and leucine-rich repeat protein 13, or dynein regulatory complex subunit 6, is a component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. It is also the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438896  Cd Length: 42  Bit Score: 34.23  E-value: 8.07e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 19920682 231 VNIIPVEVMLKIFAYLDDMSLWMASEVCKQWHDIVGKNtaqSMW 274
Cdd:cd22124   1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSS---SLW 41
 
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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