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Conserved domains on  [gi|1002296096|ref|XP_015611506|]
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E3 ubiquitin-protein ligase UPL1 isoform X1 [Oryza sativa Japonica Group]

Protein Classification

DUF913 and HECTc domain-containing protein( domain architecture ID 10532551)

protein containing domains DUF908, DUF913, DUF4414, and HECTc

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
3354-3714 3.82e-152

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


:

Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 476.67  E-value: 3.82e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3354 LRISVRRAYVLEDSYNQLRLRRSQDLKGRLTVQFQGEEGIDAGGLTREWYQLLSRVIFD-KGALLFTTVGNNATFQPNPN 3432
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNpSYGLFRYTPDDSGLLYPNPS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3433 SVYQTEHLSYFKFVGRVVAKALFDGQLLDVHFTRSFYKHILGVKVTYHDIEAVDPDYYKNLKWMLENDVS-DIPDLTFSM 3511
Cdd:cd00078     81 SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDeDDLELTFTI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3512 DPDEEkhiLYEkneVTDYELKPGGRNIRVTEETKHEYVDLVAEHILTTAIRPQINAFLEGFTELVPRELISLFHDKELEL 3591
Cdd:cd00078    161 ELDSS---FGG---AVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELEL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3592 LISGLPEIDFDDLKANAEYI-GYSPASPVILWFWEVVNGFSKEDMARFLQFVTGTSKVPLEGFKALQgisgpQRFQIHKA 3670
Cdd:cd00078    235 LICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRV 309
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1002296096 3671 YGAPERLPSAHTCFNQLDLPEYSSKEQLEERLLLAIHEaSEGFG 3714
Cdd:cd00078    310 GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINE-GAGFG 352
DUF913 pfam06025
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ...
422-786 9.45e-101

Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin protein ligases.


:

Pssm-ID: 461803  Cd Length: 369  Bit Score: 329.96  E-value: 9.45e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  422 TAVHVIEGFLDYHNPSSALFRDLGGLDDTIARLKIEVsqvdigsKKSEEPQSMSKGkevesslPPPDMQTVHSEALISYN 501
Cdd:pfam06025    1 RAVQFLDTLIYNFQDAFQAFRNAGGLDAIIDRIVHEV-------DSALELAEAGKG-------TPSEYKSSVVDYEIPYY 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  502 RRNLMKALLRTISLATYV--PGSSARVDGSEEN-VLPPCLCTIFRRAKEFGGGVFSLAATVMSDLIHKDPTCFTVLDAAG 578
Cdd:pfam06025   67 RQQLLKWLLKFIHHMMQHsgGGTDRLLRNLIDSsQLLGSLRKIIENAKVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAG 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  579 LPQAFIDA-IMGGILYNSDAITCIPQCLDALCLNSSGLQLVKDHNALRCFVKIFTSRSYLKALG--GDTAGALSLGLDEL 655
Cdd:pfam06025  147 LSKAFLEAvLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNALESFFEIFESPDHVKAMEtdGELASNLGSSFDEL 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  656 LRHQSSLRSSGVDMLIEILNTISKVGCG-------------GESSSCTESGNSSTPLPMETDVQGGTSRSEvgtsevGSS 722
Cdd:pfam06025  227 VRHHPSLKPAIINAVIDMLARVVELGSTkaepdgwgaklwvGCSSSSSFSPASSGSLPMETDGESGDESSS------DED 300
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002296096  723 EKMVDASLDATSSSIESY-----LPECICNVGRLIETILQNSDTCRLFSEKKGIEAVLQLFKLPLMPVS 786
Cdd:pfam06025  301 VEMEDAPDTDSTEETEPEshgnsLTDYIDNVARFLEAFFSNNSHCSDFIEKGGIELLLDLATLPSLPYD 369
DUF908 pfam06012
Domain of Unknown Function (DUF908);
85-362 6.64e-30

Domain of Unknown Function (DUF908);


:

Pssm-ID: 428721  Cd Length: 351  Bit Score: 123.98  E-value: 6.64e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096   85 REAVVQILRVSRLILENCTNRHFYSLFEqHLSSLLASTDADIVEGSLETL-------------RAFVNKSVGKSSIRSA- 150
Cdd:pfam06012    3 RELVEAILRFTRLLLENCGNRSIYNSSE-HLNDLLNTTSLDVLLAALRLLlrlaqrysasnsrRGSAPRHIQQSLLANHy 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  151 -----------------SLTSKLFAFSQGWGGKEGGLGLIACSLPSGCDPIATEIGSTLHFEFY---------------- 197
Cdd:pfam06012   82 nidldrllklaqpfpkpPPPDSTDPAPSTTKNSANEYANDLVSLAKEDSKVLPSEWGSVKFTYYpssssdeaptssksst 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  198 ------------RGADKSDKSQSI-------------DNCHRLEIIHLPSIISCKENDLEILEKLVKDysVPPSLRFSLL 252
Cdd:pfam06012  162 ssnsspstptplRRSSTLGTSPDSpsspststpssaaDSDEGLRTFEIPESKVASKSLEDILAKAIED--LPKESRFELL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  253 TRLRFARAFDSLAY--RRQYTCIRLSAFIVLVQASHDSESLALFLNNEPEFIDELLSLLSYEDEIPEKIRRLGILSLVAL 330
Cdd:pfam06012  240 HRIRIAKALNSSSEesRQQLLAIRLLAIANLAYIHPESTFQTKLFEYDPDLVYQLAELIHPDTEVPLELQTAALYALEAL 319
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1002296096  331 CQDRSHQPTVLSSVTSGGHRGILPSLMQKAVD 362
Cdd:pfam06012  320 ARHRAKLSDVLSALGANVNHGILLYVLRKAVA 351
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
1286-1323 1.32e-14

UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 (atUPL2) and similar proteins; The family includes two highly similar 405-kDa HECT E3 ubiquitin-protein ligases (UPLs), UPL1 and UPL2, from Arabidopsis thaliana. The HECT E3 UPL family plays a prominent role in the ubiquitination of plant proteins. The biological functions of UPL1 and UPL2 remain unclear. Both of them contain a ubiquitin-associated (UBA) domain and a C-terminal HECT domain. UBA domain may be involved in ubiquitin metabolism. HECT domain is necessary and sufficient for their E3 catalytic activity, but requires ATP, E1 and an E2 of the Arabidopsis UBC8 family to ubiquitinate proteins.


:

Pssm-ID: 270512 [Multi-domain]  Cd Length: 38  Bit Score: 70.02  E-value: 1.32e-14
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1002296096 1286 SSIATIVEMGFSRARAEEALRSVRTNSVEMATDWLFSH 1323
Cdd:cd14327      1 EAVAQLVEMGFSRERAEEALRAVGTNSVELAMEWLFTN 38
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
2664-2697 5.96e-08

Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).


:

Pssm-ID: 464159 [Multi-domain]  Cd Length: 34  Bit Score: 50.96  E-value: 5.96e-08
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1002296096 2664 TPPAAVEIDPEFLAALPPEIQAEVLAQQRAQRIA 2697
Cdd:pfam14377    1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
2631-2655 1.84e-06

Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).


:

Pssm-ID: 464159 [Multi-domain]  Cd Length: 34  Bit Score: 46.73  E-value: 1.84e-06
                           10        20
                   ....*....|....*....|....*
gi 1002296096 2631 NEIDPTFLEALPEDLRAEVLASQQN 2655
Cdd:pfam14377    6 EGIDPSFLAALPPDLRQEVLAQQDD 30
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
2701-2735 1.47e-03

Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).


:

Pssm-ID: 464159 [Multi-domain]  Cd Length: 34  Bit Score: 38.64  E-value: 1.47e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1002296096 2701 PIGQPVDMDNaSIIATFPPDLREEVLLTSSEAVLS 2735
Cdd:pfam14377    1 AAPPPEGIDP-SFLAALPPDLRQEVLAQQDDERLR 34
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
3354-3714 3.82e-152

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 476.67  E-value: 3.82e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3354 LRISVRRAYVLEDSYNQLRLRRSQDLKGRLTVQFQGEEGIDAGGLTREWYQLLSRVIFD-KGALLFTTVGNNATFQPNPN 3432
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNpSYGLFRYTPDDSGLLYPNPS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3433 SVYQTEHLSYFKFVGRVVAKALFDGQLLDVHFTRSFYKHILGVKVTYHDIEAVDPDYYKNLKWMLENDVS-DIPDLTFSM 3511
Cdd:cd00078     81 SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDeDDLELTFTI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3512 DPDEEkhiLYEkneVTDYELKPGGRNIRVTEETKHEYVDLVAEHILTTAIRPQINAFLEGFTELVPRELISLFHDKELEL 3591
Cdd:cd00078    161 ELDSS---FGG---AVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELEL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3592 LISGLPEIDFDDLKANAEYI-GYSPASPVILWFWEVVNGFSKEDMARFLQFVTGTSKVPLEGFKALQgisgpQRFQIHKA 3670
Cdd:cd00078    235 LICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRV 309
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1002296096 3671 YGAPERLPSAHTCFNQLDLPEYSSKEQLEERLLLAIHEaSEGFG 3714
Cdd:cd00078    310 GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINE-GAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
3378-3713 1.30e-142

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 448.22  E-value: 1.30e-142
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  3378 DLKG-RLTVQFQGEEGIDAGGLTREWYQLLSRVIFDKGALLFTTVGNNATFQPNPNSVYQT-EHLSYFKFVGRVVAKALF 3455
Cdd:smart00119    1 DLKKrVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANeEHLSYFRFIGRVLGKALY 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  3456 DGQLLDVHFTRSFYKHILGVKVTYHDIEAVDPDYYKNLKWM-LENDVSDIPDLTFSMDPDEEKhilyekNEVTDYELKPG 3534
Cdd:smart00119   81 DNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEELDLTFSIVLTSEF------GQVKVVELKPG 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  3535 GRNIRVTEETKHEYVDLVAEHILTTAIRPQINAFLEGFTELVPRELISLFHDKELELLISGLPEIDFDDLKANAEYI-GY 3613
Cdd:smart00119  155 GSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKgGY 234
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  3614 SPASPVILWFWEVVNGFSKEDMARFLQFVTGTSKVPLEGFKALQGisgpqRFQIHKAYGAPERLPSAHTCFNQLDLPEYS 3693
Cdd:smart00119  235 SANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYS 309
                           330       340
                    ....*....|....*....|
gi 1002296096  3694 SKEQLEERLLLAIHEAsEGF 3713
Cdd:smart00119  310 SKEILREKLLLAINEG-KGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
3300-3715 3.24e-138

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 457.31  E-value: 3.24e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3300 HRRLLNVFIrqNPSLLEKSLSMMLKVPRLidFDNKRAYFRsRIRQQHDQHLSAPLRISVRRAYVLEDSYNQLRLRRSQDL 3379
Cdd:COG5021    466 HRKKTLTKN--DSRLGSFISLNKLDIRRI--KEDKRRKLF-YSLKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESGDDL 540
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3380 KGRLTVQFQGEEGIDAGGLTREWYQLLSRVIFDKGALLF--TTVGNNaTFQPNPNSVYQTEHLSYFKFVGRVVAKALFDG 3457
Cdd:COG5021    541 KKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFeyITEDLY-TLPINPLSSINPEHLSYFKFLGRVIGKAIYDS 619
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3458 QLLDVHFTRSFYKHILGVKVTYHDIEAVDPDYYKNLKWMLENDVSD-IPDLTFSMDPDEEkhilyekNEVTDYELKPGGR 3536
Cdd:COG5021    620 RILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDEtILDLTFTVEDDSF-------GESRTVELIPNGR 692
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3537 NIRVTEETKHEYVDLVAEHILTTAIRPQINAFLEGFTELVPRELISLFHDKELELLISGLPE-IDFDDLKANAEYIGYSP 3615
Cdd:COG5021    693 NISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTE 772
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3616 ASPVILWFWEVVNGFSKEDMARFLQFVTGTSKVPLEGFKALQGISGPQRFQIHKAYGAPERLPSAHTCFNQLDLPEYSSK 3695
Cdd:COG5021    773 DSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSK 852
                          410       420
                   ....*....|....*....|
gi 1002296096 3696 EQLEERLLLAIHEaSEGFGF 3715
Cdd:COG5021    853 EKLRSKLLTAINE-GAGFGL 871
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
3404-3715 3.51e-117

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 374.25  E-value: 3.51e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3404 QLLSRVIFDKGALLF-TTVGNNATFQPNPNS--VYQTEHLSYFKFVGRVVAKALFDGQLLDVHFTRSFYKHILGVKVTYH 3480
Cdd:pfam00632    1 TLLSKELFDPNYGLFeYETEDDRTYWFNPSSseSPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3481 DIEAVDPDYYKNLKWMLENDVSDIPD--LTFSMDPDEEKHIlyeknevtdYELKPGGRNIRVTEETKHEYVDLVAEHILT 3558
Cdd:pfam00632   81 DLESIDPELYKSLKSLLNMDNDDDEDlgLTFTIPVFGESKT---------IELIPNGRNIPVTNENKEEYIRLYVDYRLN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3559 TAIRPQINAFLEGFTELVPRELISLFHDKELELLISGLPEIDFDDLKANAEYI-GYSPASPVILWFWEVVNGFSKEDMAR 3637
Cdd:pfam00632  152 KSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEFSPEQRRL 231
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002296096 3638 FLQFVTGTSKVPLEGFKALqgisgpQRFQIHKAYGAPE-RLPSAHTCFNQLDLPEYSSKEQLEERLLLAIHEaSEGFGF 3715
Cdd:pfam00632  232 FLKFVTGSSRLPVGGFKSL------PKFTIVRKGGDDDdRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEE-GEGFGL 303
DUF913 pfam06025
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ...
422-786 9.45e-101

Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin protein ligases.


Pssm-ID: 461803  Cd Length: 369  Bit Score: 329.96  E-value: 9.45e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  422 TAVHVIEGFLDYHNPSSALFRDLGGLDDTIARLKIEVsqvdigsKKSEEPQSMSKGkevesslPPPDMQTVHSEALISYN 501
Cdd:pfam06025    1 RAVQFLDTLIYNFQDAFQAFRNAGGLDAIIDRIVHEV-------DSALELAEAGKG-------TPSEYKSSVVDYEIPYY 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  502 RRNLMKALLRTISLATYV--PGSSARVDGSEEN-VLPPCLCTIFRRAKEFGGGVFSLAATVMSDLIHKDPTCFTVLDAAG 578
Cdd:pfam06025   67 RQQLLKWLLKFIHHMMQHsgGGTDRLLRNLIDSsQLLGSLRKIIENAKVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAG 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  579 LPQAFIDA-IMGGILYNSDAITCIPQCLDALCLNSSGLQLVKDHNALRCFVKIFTSRSYLKALG--GDTAGALSLGLDEL 655
Cdd:pfam06025  147 LSKAFLEAvLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNALESFFEIFESPDHVKAMEtdGELASNLGSSFDEL 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  656 LRHQSSLRSSGVDMLIEILNTISKVGCG-------------GESSSCTESGNSSTPLPMETDVQGGTSRSEvgtsevGSS 722
Cdd:pfam06025  227 VRHHPSLKPAIINAVIDMLARVVELGSTkaepdgwgaklwvGCSSSSSFSPASSGSLPMETDGESGDESSS------DED 300
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002296096  723 EKMVDASLDATSSSIESY-----LPECICNVGRLIETILQNSDTCRLFSEKKGIEAVLQLFKLPLMPVS 786
Cdd:pfam06025  301 VEMEDAPDTDSTEETEPEshgnsLTDYIDNVARFLEAFFSNNSHCSDFIEKGGIELLLDLATLPSLPYD 369
DUF908 pfam06012
Domain of Unknown Function (DUF908);
85-362 6.64e-30

Domain of Unknown Function (DUF908);


Pssm-ID: 428721  Cd Length: 351  Bit Score: 123.98  E-value: 6.64e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096   85 REAVVQILRVSRLILENCTNRHFYSLFEqHLSSLLASTDADIVEGSLETL-------------RAFVNKSVGKSSIRSA- 150
Cdd:pfam06012    3 RELVEAILRFTRLLLENCGNRSIYNSSE-HLNDLLNTTSLDVLLAALRLLlrlaqrysasnsrRGSAPRHIQQSLLANHy 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  151 -----------------SLTSKLFAFSQGWGGKEGGLGLIACSLPSGCDPIATEIGSTLHFEFY---------------- 197
Cdd:pfam06012   82 nidldrllklaqpfpkpPPPDSTDPAPSTTKNSANEYANDLVSLAKEDSKVLPSEWGSVKFTYYpssssdeaptssksst 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  198 ------------RGADKSDKSQSI-------------DNCHRLEIIHLPSIISCKENDLEILEKLVKDysVPPSLRFSLL 252
Cdd:pfam06012  162 ssnsspstptplRRSSTLGTSPDSpsspststpssaaDSDEGLRTFEIPESKVASKSLEDILAKAIED--LPKESRFELL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  253 TRLRFARAFDSLAY--RRQYTCIRLSAFIVLVQASHDSESLALFLNNEPEFIDELLSLLSYEDEIPEKIRRLGILSLVAL 330
Cdd:pfam06012  240 HRIRIAKALNSSSEesRQQLLAIRLLAIANLAYIHPESTFQTKLFEYDPDLVYQLAELIHPDTEVPLELQTAALYALEAL 319
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1002296096  331 CQDRSHQPTVLSSVTSGGHRGILPSLMQKAVD 362
Cdd:pfam06012  320 ARHRAKLSDVLSALGANVNHGILLYVLRKAVA 351
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
1286-1323 1.32e-14

UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 (atUPL2) and similar proteins; The family includes two highly similar 405-kDa HECT E3 ubiquitin-protein ligases (UPLs), UPL1 and UPL2, from Arabidopsis thaliana. The HECT E3 UPL family plays a prominent role in the ubiquitination of plant proteins. The biological functions of UPL1 and UPL2 remain unclear. Both of them contain a ubiquitin-associated (UBA) domain and a C-terminal HECT domain. UBA domain may be involved in ubiquitin metabolism. HECT domain is necessary and sufficient for their E3 catalytic activity, but requires ATP, E1 and an E2 of the Arabidopsis UBC8 family to ubiquitinate proteins.


Pssm-ID: 270512 [Multi-domain]  Cd Length: 38  Bit Score: 70.02  E-value: 1.32e-14
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1002296096 1286 SSIATIVEMGFSRARAEEALRSVRTNSVEMATDWLFSH 1323
Cdd:cd14327      1 EAVAQLVEMGFSRERAEEALRAVGTNSVELAMEWLFTN 38
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
1284-1320 1.42e-08

UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.


Pssm-ID: 395502 [Multi-domain]  Cd Length: 37  Bit Score: 52.83  E-value: 1.42e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1002296096 1284 DESSIATIVEMGFSRARAEEALRSvRTNSVEMATDWL 1320
Cdd:pfam00627    2 DEEAIQRLVEMGFDREQVREALRA-TGNNVERAAEYL 37
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
2664-2697 5.96e-08

Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).


Pssm-ID: 464159 [Multi-domain]  Cd Length: 34  Bit Score: 50.96  E-value: 5.96e-08
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1002296096 2664 TPPAAVEIDPEFLAALPPEIQAEVLAQQRAQRIA 2697
Cdd:pfam14377    1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
1284-1321 5.41e-07

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.


Pssm-ID: 197551 [Multi-domain]  Cd Length: 37  Bit Score: 48.25  E-value: 5.41e-07
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1002296096  1284 DESSIATIVEMGFSRARAEEALRSVRTNsVEMATDWLF 1321
Cdd:smart00165    1 DEEKIDQLLEMGFSREEALKALRAANGN-VERAAEYLL 37
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
2631-2655 1.84e-06

Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).


Pssm-ID: 464159 [Multi-domain]  Cd Length: 34  Bit Score: 46.73  E-value: 1.84e-06
                           10        20
                   ....*....|....*....|....*
gi 1002296096 2631 NEIDPTFLEALPEDLRAEVLASQQN 2655
Cdd:pfam14377    6 EGIDPSFLAALPPDLRQEVLAQQDD 30
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
2701-2735 1.47e-03

Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).


Pssm-ID: 464159 [Multi-domain]  Cd Length: 34  Bit Score: 38.64  E-value: 1.47e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1002296096 2701 PIGQPVDMDNaSIIATFPPDLREEVLLTSSEAVLS 2735
Cdd:pfam14377    1 AAPPPEGIDP-SFLAALPPDLRQEVLAQQDDERLR 34
Rev1_UBM2 cd19318
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
2666-2695 1.80e-03

Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen.


Pssm-ID: 412037  Cd Length: 36  Bit Score: 38.36  E-value: 1.80e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1002296096 2666 PAAVEIDPEFLAALPPEIQAEVLAQQRAQR 2695
Cdd:cd19318      7 PSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
3354-3714 3.82e-152

HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains.


Pssm-ID: 238033 [Multi-domain]  Cd Length: 352  Bit Score: 476.67  E-value: 3.82e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3354 LRISVRRAYVLEDSYNQLRLRRSQDLKGRLTVQFQGEEGIDAGGLTREWYQLLSRVIFD-KGALLFTTVGNNATFQPNPN 3432
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNpSYGLFRYTPDDSGLLYPNPS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3433 SVYQTEHLSYFKFVGRVVAKALFDGQLLDVHFTRSFYKHILGVKVTYHDIEAVDPDYYKNLKWMLENDVS-DIPDLTFSM 3511
Cdd:cd00078     81 SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDeDDLELTFTI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3512 DPDEEkhiLYEkneVTDYELKPGGRNIRVTEETKHEYVDLVAEHILTTAIRPQINAFLEGFTELVPRELISLFHDKELEL 3591
Cdd:cd00078    161 ELDSS---FGG---AVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELEL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3592 LISGLPEIDFDDLKANAEYI-GYSPASPVILWFWEVVNGFSKEDMARFLQFVTGTSKVPLEGFKALQgisgpQRFQIHKA 3670
Cdd:cd00078    235 LICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRV 309
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1002296096 3671 YGAPERLPSAHTCFNQLDLPEYSSKEQLEERLLLAIHEaSEGFG 3714
Cdd:cd00078    310 GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINE-GAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
3378-3713 1.30e-142

Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes.


Pssm-ID: 214523  Cd Length: 328  Bit Score: 448.22  E-value: 1.30e-142
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  3378 DLKG-RLTVQFQGEEGIDAGGLTREWYQLLSRVIFDKGALLFTTVGNNATFQPNPNSVYQT-EHLSYFKFVGRVVAKALF 3455
Cdd:smart00119    1 DLKKrVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANeEHLSYFRFIGRVLGKALY 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  3456 DGQLLDVHFTRSFYKHILGVKVTYHDIEAVDPDYYKNLKWM-LENDVSDIPDLTFSMDPDEEKhilyekNEVTDYELKPG 3534
Cdd:smart00119   81 DNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEELDLTFSIVLTSEF------GQVKVVELKPG 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  3535 GRNIRVTEETKHEYVDLVAEHILTTAIRPQINAFLEGFTELVPRELISLFHDKELELLISGLPEIDFDDLKANAEYI-GY 3613
Cdd:smart00119  155 GSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKgGY 234
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  3614 SPASPVILWFWEVVNGFSKEDMARFLQFVTGTSKVPLEGFKALQGisgpqRFQIHKAYGAPERLPSAHTCFNQLDLPEYS 3693
Cdd:smart00119  235 SANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYS 309
                           330       340
                    ....*....|....*....|
gi 1002296096  3694 SKEQLEERLLLAIHEAsEGF 3713
Cdd:smart00119  310 SKEILREKLLLAINEG-KGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
3300-3715 3.24e-138

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 457.31  E-value: 3.24e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3300 HRRLLNVFIrqNPSLLEKSLSMMLKVPRLidFDNKRAYFRsRIRQQHDQHLSAPLRISVRRAYVLEDSYNQLRLRRSQDL 3379
Cdd:COG5021    466 HRKKTLTKN--DSRLGSFISLNKLDIRRI--KEDKRRKLF-YSLKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESGDDL 540
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3380 KGRLTVQFQGEEGIDAGGLTREWYQLLSRVIFDKGALLF--TTVGNNaTFQPNPNSVYQTEHLSYFKFVGRVVAKALFDG 3457
Cdd:COG5021    541 KKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFeyITEDLY-TLPINPLSSINPEHLSYFKFLGRVIGKAIYDS 619
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3458 QLLDVHFTRSFYKHILGVKVTYHDIEAVDPDYYKNLKWMLENDVSD-IPDLTFSMDPDEEkhilyekNEVTDYELKPGGR 3536
Cdd:COG5021    620 RILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDEtILDLTFTVEDDSF-------GESRTVELIPNGR 692
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3537 NIRVTEETKHEYVDLVAEHILTTAIRPQINAFLEGFTELVPRELISLFHDKELELLISGLPE-IDFDDLKANAEYIGYSP 3615
Cdd:COG5021    693 NISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTE 772
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3616 ASPVILWFWEVVNGFSKEDMARFLQFVTGTSKVPLEGFKALQGISGPQRFQIHKAYGAPERLPSAHTCFNQLDLPEYSSK 3695
Cdd:COG5021    773 DSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSK 852
                          410       420
                   ....*....|....*....|
gi 1002296096 3696 EQLEERLLLAIHEaSEGFGF 3715
Cdd:COG5021    853 EKLRSKLLTAINE-GAGFGL 871
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
3404-3715 3.51e-117

HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.


Pssm-ID: 459880  Cd Length: 304  Bit Score: 374.25  E-value: 3.51e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3404 QLLSRVIFDKGALLF-TTVGNNATFQPNPNS--VYQTEHLSYFKFVGRVVAKALFDGQLLDVHFTRSFYKHILGVKVTYH 3480
Cdd:pfam00632    1 TLLSKELFDPNYGLFeYETEDDRTYWFNPSSseSPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3481 DIEAVDPDYYKNLKWMLENDVSDIPD--LTFSMDPDEEKHIlyeknevtdYELKPGGRNIRVTEETKHEYVDLVAEHILT 3558
Cdd:pfam00632   81 DLESIDPELYKSLKSLLNMDNDDDEDlgLTFTIPVFGESKT---------IELIPNGRNIPVTNENKEEYIRLYVDYRLN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096 3559 TAIRPQINAFLEGFTELVPRELISLFHDKELELLISGLPEIDFDDLKANAEYI-GYSPASPVILWFWEVVNGFSKEDMAR 3637
Cdd:pfam00632  152 KSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEFSPEQRRL 231
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002296096 3638 FLQFVTGTSKVPLEGFKALqgisgpQRFQIHKAYGAPE-RLPSAHTCFNQLDLPEYSSKEQLEERLLLAIHEaSEGFGF 3715
Cdd:pfam00632  232 FLKFVTGSSRLPVGGFKSL------PKFTIVRKGGDDDdRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEE-GEGFGL 303
DUF913 pfam06025
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ...
422-786 9.45e-101

Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin protein ligases.


Pssm-ID: 461803  Cd Length: 369  Bit Score: 329.96  E-value: 9.45e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  422 TAVHVIEGFLDYHNPSSALFRDLGGLDDTIARLKIEVsqvdigsKKSEEPQSMSKGkevesslPPPDMQTVHSEALISYN 501
Cdd:pfam06025    1 RAVQFLDTLIYNFQDAFQAFRNAGGLDAIIDRIVHEV-------DSALELAEAGKG-------TPSEYKSSVVDYEIPYY 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  502 RRNLMKALLRTISLATYV--PGSSARVDGSEEN-VLPPCLCTIFRRAKEFGGGVFSLAATVMSDLIHKDPTCFTVLDAAG 578
Cdd:pfam06025   67 RQQLLKWLLKFIHHMMQHsgGGTDRLLRNLIDSsQLLGSLRKIIENAKVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAG 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  579 LPQAFIDA-IMGGILYNSDAITCIPQCLDALCLNSSGLQLVKDHNALRCFVKIFTSRSYLKALG--GDTAGALSLGLDEL 655
Cdd:pfam06025  147 LSKAFLEAvLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNALESFFEIFESPDHVKAMEtdGELASNLGSSFDEL 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  656 LRHQSSLRSSGVDMLIEILNTISKVGCG-------------GESSSCTESGNSSTPLPMETDVQGGTSRSEvgtsevGSS 722
Cdd:pfam06025  227 VRHHPSLKPAIINAVIDMLARVVELGSTkaepdgwgaklwvGCSSSSSFSPASSGSLPMETDGESGDESSS------DED 300
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002296096  723 EKMVDASLDATSSSIESY-----LPECICNVGRLIETILQNSDTCRLFSEKKGIEAVLQLFKLPLMPVS 786
Cdd:pfam06025  301 VEMEDAPDTDSTEETEPEshgnsLTDYIDNVARFLEAFFSNNSHCSDFIEKGGIELLLDLATLPSLPYD 369
DUF908 pfam06012
Domain of Unknown Function (DUF908);
85-362 6.64e-30

Domain of Unknown Function (DUF908);


Pssm-ID: 428721  Cd Length: 351  Bit Score: 123.98  E-value: 6.64e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096   85 REAVVQILRVSRLILENCTNRHFYSLFEqHLSSLLASTDADIVEGSLETL-------------RAFVNKSVGKSSIRSA- 150
Cdd:pfam06012    3 RELVEAILRFTRLLLENCGNRSIYNSSE-HLNDLLNTTSLDVLLAALRLLlrlaqrysasnsrRGSAPRHIQQSLLANHy 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  151 -----------------SLTSKLFAFSQGWGGKEGGLGLIACSLPSGCDPIATEIGSTLHFEFY---------------- 197
Cdd:pfam06012   82 nidldrllklaqpfpkpPPPDSTDPAPSTTKNSANEYANDLVSLAKEDSKVLPSEWGSVKFTYYpssssdeaptssksst 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  198 ------------RGADKSDKSQSI-------------DNCHRLEIIHLPSIISCKENDLEILEKLVKDysVPPSLRFSLL 252
Cdd:pfam06012  162 ssnsspstptplRRSSTLGTSPDSpsspststpssaaDSDEGLRTFEIPESKVASKSLEDILAKAIED--LPKESRFELL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002296096  253 TRLRFARAFDSLAY--RRQYTCIRLSAFIVLVQASHDSESLALFLNNEPEFIDELLSLLSYEDEIPEKIRRLGILSLVAL 330
Cdd:pfam06012  240 HRIRIAKALNSSSEesRQQLLAIRLLAIANLAYIHPESTFQTKLFEYDPDLVYQLAELIHPDTEVPLELQTAALYALEAL 319
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1002296096  331 CQDRSHQPTVLSSVTSGGHRGILPSLMQKAVD 362
Cdd:pfam06012  320 ARHRAKLSDVLSALGANVNHGILLYVLRKAVA 351
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
1286-1323 1.32e-14

UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 (atUPL2) and similar proteins; The family includes two highly similar 405-kDa HECT E3 ubiquitin-protein ligases (UPLs), UPL1 and UPL2, from Arabidopsis thaliana. The HECT E3 UPL family plays a prominent role in the ubiquitination of plant proteins. The biological functions of UPL1 and UPL2 remain unclear. Both of them contain a ubiquitin-associated (UBA) domain and a C-terminal HECT domain. UBA domain may be involved in ubiquitin metabolism. HECT domain is necessary and sufficient for their E3 catalytic activity, but requires ATP, E1 and an E2 of the Arabidopsis UBC8 family to ubiquitinate proteins.


Pssm-ID: 270512 [Multi-domain]  Cd Length: 38  Bit Score: 70.02  E-value: 1.32e-14
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1002296096 1286 SSIATIVEMGFSRARAEEALRSVRTNSVEMATDWLFSH 1323
Cdd:cd14327      1 EAVAQLVEMGFSRERAEEALRAVGTNSVELAMEWLFTN 38
UBA2_UBP5 cd14386
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
1284-1326 1.27e-10

UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. This model corresponds to the UBA2 domain.


Pssm-ID: 270569 [Multi-domain]  Cd Length: 43  Bit Score: 58.88  E-value: 1.27e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1002296096 1284 DESSIATIVEMGFSRARAEEALRSVrTNSVEMATDWLFSHPEE 1326
Cdd:cd14386      2 PEEAVAMLVSMGFTRDQAIKALKAT-DNNVERAADWIFSHPDE 43
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
1288-1324 2.20e-09

UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270483 [Multi-domain]  Cd Length: 39  Bit Score: 55.18  E-value: 2.20e-09
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1002296096 1288 IATIVEMGFSRARAEEALRsvRT-NSVEMATDWLFSHP 1324
Cdd:cd14297      4 VKQLVDMGFTEAQARKALR--KTnNNVERAVDWLFEGP 39
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
1284-1320 1.42e-08

UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.


Pssm-ID: 395502 [Multi-domain]  Cd Length: 37  Bit Score: 52.83  E-value: 1.42e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1002296096 1284 DESSIATIVEMGFSRARAEEALRSvRTNSVEMATDWL 1320
Cdd:pfam00627    2 DEEAIQRLVEMGFDREQVREALRA-TGNNVERAAEYL 37
UBA_UBXN1 cd14302
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ...
1286-1326 2.34e-08

UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also called SAPK substrate protein 1 (SAKS1) or UBA/UBX 33.3 kDa protein, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (UBX) domain. It binds polyubiquitin and valosin-containing protein (VCP), and has been identified as a substrate for stress-activated protein kinases (SAPKs). Moreover, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and may be involved in the Ub-proteasome proteolytic pathways. In addition, UBXN1 can associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domain.


Pssm-ID: 270487 [Multi-domain]  Cd Length: 41  Bit Score: 52.29  E-value: 2.34e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1002296096 1286 SSIATIVEMGFSRARAEEALRSVRTNSVEMATDWLFSHPEE 1326
Cdd:cd14302      1 SELQTLIEMGFSRNRAEKALAKTGNQGVEAAMEWLLAHEDD 41
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
2664-2697 5.96e-08

Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).


Pssm-ID: 464159 [Multi-domain]  Cd Length: 34  Bit Score: 50.96  E-value: 5.96e-08
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1002296096 2664 TPPAAVEIDPEFLAALPPEIQAEVLAQQRAQRIA 2697
Cdd:pfam14377    1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
UBA_UBS3B cd14301
UBA domain found in ubiquitin-associated and SH3 domain-containing protein B (UBS3B) and ...
1286-1323 7.27e-08

UBA domain found in ubiquitin-associated and SH3 domain-containing protein B (UBS3B) and similar proteins; UBS3B, or Cbl-interacting protein p70, suppressor of T-cell receptor signaling 1 (Sts-1), T-cell ubiquitin ligand 2 (TULA-2), or tyrosine-protein phosphatase STS1/TULA2, is ubiquitously expressed in mammalian tissues in a variety of cell types. It exhibits high phosphatase activity, but demonstrates no proapoptotic activity. It negatively regulates the tyrosine kinase Zap-70 activation and T cell receptor (TCR) signaling pathways that modulate T cell activation. Moreover, UBS3B acts as a Cbl- and ubiquitin-interacting protein that inhibits endocytosis of epidermal growth factor receptor (EGFR) and platelet-derived growth factor receptor.


Pssm-ID: 270486 [Multi-domain]  Cd Length: 38  Bit Score: 50.90  E-value: 7.27e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1002296096 1286 SSIATIVEMGFSRARAEEALRSVRTNSVEMATDWLFSH 1323
Cdd:cd14301      1 SALEVLLSMGFPKHRAEKALAATGGRSVQLASDWLLSH 38
UBA1_NUB1_like cd14291
UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called ...
1284-1320 3.75e-07

UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called negative regulator of ubiquitin-like proteins 1, renal carcinoma antigen NY-REN-18, or protein BS4, is a NEDD8-interacting protein that can be induced by interferon. It functions as a strong post-transcriptional down-regulator of the NEDD8 expression and plays critical roles in regulating many biological events, such as cell growth, NF-kappaB signaling, and biological responses to hypoxia. NUB1 can also interact with aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) which may function in the regulation of cell cycle progression. NUB1 contains three ubiquitin-associated domains (UBA), a bipartite nuclear localization signal (NLS) and a PEST motif. This model corresponds to UBA1 domain.


Pssm-ID: 270477 [Multi-domain]  Cd Length: 36  Bit Score: 48.98  E-value: 3.75e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1002296096 1284 DESSIATIVEMGFSRARAEEALRSVRtNSVEMATDWL 1320
Cdd:cd14291      1 DEDKLQQLMEMGFSEAEARLALRACN-GNVERAVDYI 36
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
1284-1321 5.41e-07

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.


Pssm-ID: 197551 [Multi-domain]  Cd Length: 37  Bit Score: 48.25  E-value: 5.41e-07
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1002296096  1284 DESSIATIVEMGFSRARAEEALRSVRTNsVEMATDWLF 1321
Cdd:smart00165    1 DEEKIDQLLEMGFSREEALKALRAANGN-VERAAEYLL 37
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
1285-1323 6.52e-07

UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270482 [Multi-domain]  Cd Length: 39  Bit Score: 48.40  E-value: 6.52e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1002296096 1285 ESSIATIVEMGFSRARAEEALRSVRTNSVEMATDWLFSH 1323
Cdd:cd14296      1 EEAVSQLMSMGFSENAAKRALYYTGNSSVEAAMNWLFEH 39
UBA1_atUBP14 cd14295
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
1284-1325 8.52e-07

UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and similar proteins; atUBP14, also called deubiquitinating enzyme 14, TITAN-6 protein, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is related to the isopeptidase T class of deubiquitinating enzymes that recycle polyubiquitin chains following protein degradation. atUBP14 is essential for early plant development. It can disassemble multi-ubiquitin chains linked internally via epsilon-amino isopeptide bonds using Lys48 and can process some, but not all, translational fusions of ubiquitin linked via alpha-amino peptide bonds. atUBP14 contains two ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270481 [Multi-domain]  Cd Length: 45  Bit Score: 48.14  E-value: 8.52e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1002296096 1284 DESSIATIVEMGFSRARAEEALRSVRTNSVEMATDWLFSHPE 1325
Cdd:cd14295      1 DQELVAQLMEMGFPKVRAEKALFFTQNKGLEEAMEWLEEHSE 42
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
2631-2655 1.84e-06

Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).


Pssm-ID: 464159 [Multi-domain]  Cd Length: 34  Bit Score: 46.73  E-value: 1.84e-06
                           10        20
                   ....*....|....*....|....*
gi 1002296096 2631 NEIDPTFLEALPEDLRAEVLASQQN 2655
Cdd:pfam14377    6 EGIDPSFLAALPPDLRQEVLAQQDD 30
UBA_RUP1p cd14307
UBA domain found in yeast UBA domain-containing protein RUP1p and similar proteins; RUP1p is a ...
1285-1323 2.39e-06

UBA domain found in yeast UBA domain-containing protein RUP1p and similar proteins; RUP1p is a ubiquitin-associated (UBA) domain-containing protein encoded by a nonessential yeast gene RUP1. It can mediate the association of Rsp5 and Ubp2. The N-terminal UBA domain is responsible for antagonizing Rsp5 function, as well as bridging the Rsp5-Ubp2 interaction. No other characterized functional domains or motifs are found in RUP1p.


Pssm-ID: 270492  Cd Length: 38  Bit Score: 46.52  E-value: 2.39e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1002296096 1285 ESSIATIVEMGFSRARAEEALRsvRTN-SVEMATDWLFSH 1323
Cdd:cd14307      1 EEAVASLLEMGIPREVAIEALR--ETNgDVEAAANYIFSN 38
UBA_HUWE1 cd14288
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ...
1283-1324 9.16e-06

UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, also called ARF-binding protein 1 (ARF-BP1), HECT, UBA and WWE domain-containing protein 1, homologous to E6AP carboxyl terminus homologs protein 9 (HectH9), large structure of UREB1 (LASU1), Mcl-1 ubiquitin ligase E3 (Mule), upstream regulatory element-binding protein 1 (URE-B1), or URE-binding protein 1, may function as a ubiquitin-protein ligase that involves in the ubiquitination cascade that targets specific substrate proteins in proteolysis. It can ubiquitylate DNA polymerase beta (Pol beta), the major BER DNA polymerase and modulates base excision repair (BER). HUWE1 also acts as a critical mediator of both the p53-independent and p53-dependent tumor suppressor functions of ARF tumor suppressor in p53 regulation. Moreover, HUWE1 is both required and sufficient for the polyubiquitination of Mcl-1, an anti-apoptotic Bcl-2 family member involving in DNA damage-induced apoptosis. Furthermore, HUWE1 plays an important role in the regulation of Cdc6 stability after DNA damage. In addition, HUWE1 works as a partner of N-Myc oncoprotein in neural cells. It ubiquitinates N-Myc and primes it for proteasomal-mediated degradation. HUWE1 contains a ubiquitin-associated (UBA) domain, a WWE domain, and a Bcl-2 homology region 3 (BH3) domain at the N-terminus and a HECT domain at the C-terminus. WWE domain plays a role in the regulation of specific protein-protein interactions in a ubiquitin conjugation system. BH3 domain is responsible for the specific binding to Mcl-1. HECT domain involves in the inhibition of the transcriptional activity of p53 via a ubiquitin-dependent degradation pathway. It also controls neural differentiation and proliferation by destabilizing the N-Myc oncoprotein.


Pssm-ID: 270474  Cd Length: 40  Bit Score: 45.08  E-value: 9.16e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1002296096 1283 LDESSIATIVEMGFSRARAEEALrsVRTNSVEMATDWLFSHP 1324
Cdd:cd14288      1 VNEAHLQQLMDMGFTREHALEAL--LHTSTLEQATEYLLTHP 40
UBA2_UBP13 cd14387
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ...
1285-1320 9.70e-06

UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13 is an ortholog of UBP5 implicated in catalyzing hydrolysis of various ubiquitin (Ub)-chains. It contains a zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. Due to the non-activating catalysis for K63-polyubiquitin chains, UBP13 may function differently from USP5 in cellular deubiquitination processes. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270570  Cd Length: 35  Bit Score: 44.67  E-value: 9.70e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1002296096 1285 ESSIATIVEMGFSRARAEEALRsvRT-NSVEMATDWL 1320
Cdd:cd14387      1 EESIAILMSMGFPRNRAIEALK--RTnNNLDRALDWL 35
UBA cd14270
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ...
1288-1318 1.23e-04

UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ubiquitin-associated (UBA) domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only the bind UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains.


Pssm-ID: 270456 [Multi-domain]  Cd Length: 30  Bit Score: 41.57  E-value: 1.23e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1002296096 1288 IATIVEMGFSRARAEEALRSVRtNSVEMATD 1318
Cdd:cd14270      1 LAQLVEMGFSREQARRALRATN-GDVEAAVE 30
UBA1_spUBP14_like cd14385
UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
1284-1326 2.11e-04

UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270568 [Multi-domain]  Cd Length: 47  Bit Score: 41.24  E-value: 2.11e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1002296096 1284 DESSIATIVEMGFSRARAEEALRSVRTNSVEMATDWLFSHPEE 1326
Cdd:cd14385      1 NAEALAQLLGMGFPEVRCKKALLATGNSDAEAAMNWLFEHMDD 43
UBA_PUB_plant cd14290
UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family ...
1284-1326 3.03e-04

UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family includes some uncharacterized hypothetical proteins found in plants. Although their biological function remain unclear, all family members contain an N-terminal ubiquitin-associated (UBA) domain and a C-terminal PUB domain. UBA domain, along with UBL (ubiquitin-like) domain, has been implicated in proteasomal degradation by associating with substrates destined for degradation as well as with subunits of the proteasome, thus regulating protein turnover. PUB domain functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins.


Pssm-ID: 270476 [Multi-domain]  Cd Length: 49  Bit Score: 40.89  E-value: 3.03e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1002296096 1284 DESSIATIVEMGFSRARAEEALRSVRTNSVEMATDWLFSHPEE 1326
Cdd:cd14290      3 NADLLKELEAMGFPRARAVRALHHTGNTSVEAAVNWIVEHEND 45
UBA1_KPC2 cd14303
UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
1284-1323 4.70e-04

UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar proteins; KPC2, also called ubiquitin-associated domain-containing protein 1 (UBAC1), or glialblastoma cell differentiation-related protein 1, is one of two subunits of Kip1 ubiquitination-promoting complex (KPC), a novel E3 ubiquitin-protein ligase that also contains KPC1 subunit and regulates the ubiquitin-dependent degradation of the cyclin-dependent kinase (CDK) inhibitor p27 at G1 phase. KPC2 contains a ubiquitin-like (UBL) domain and two ubiquitin-associated (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270488 [Multi-domain]  Cd Length: 41  Bit Score: 40.07  E-value: 4.70e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1002296096 1284 DESSIATIVEMGFSRARAEEALRSVRtNSVEMATDWLFSH 1323
Cdd:cd14303      2 DPEALKQLTEMGFPEARATKALLLNR-MSPTQAMEWLLEH 40
UBA_UBS3A_like cd14300
UBA domain found in ubiquitin-associated and SH3 domain-containing protein A (UBS3A) and ...
1290-1323 6.33e-04

UBA domain found in ubiquitin-associated and SH3 domain-containing protein A (UBS3A) and similar proteins; UBS3A, also called Cbl-interacting protein 4 (CLIP4), suppressor of T-cell receptor signaling 2 (Sts-2), or T-cell ubiquitin ligand 1 (TULA-1), is a lymphoid protein only detected in thymus, spleen, and bone marrow. UBS3A exhibits extremely low phosphatase activity, but is capable of promoting T-cell apoptosis independent of either T cell receptor (TCR)/CD3-mediated signaling or caspase activity. It functions as a negative regulator of TCR signaling. UBS3A can also inhibit HIV-1 biogenesis through the binding of ATP-binding cassette protein family E member 1 (ABCE-1), a host factor of HIV-1 assembly. Moreover, UBS3A acts as the Cbl- and ubiquitin-interacting protein that can inhibit endocytosis and downregulation of ligand-activated epidermal growth factor receptor (EGFR) by impairing Cbl-induced ubiquitination, as well as inhibit clathrin-dependent endocytosis in general. This family also includes Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and some uncharacterized AAA-type ATPase-like proteins found in plants.


Pssm-ID: 270485  Cd Length: 37  Bit Score: 39.83  E-value: 6.33e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1002296096 1290 TIVEMGFSRARAEEALRSVRTNSVEMATDWLFSH 1323
Cdd:cd14300      3 TLLAMGFPEDVARKALKATGGKSIEKATDWLLSH 36
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
2701-2735 1.47e-03

Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).


Pssm-ID: 464159 [Multi-domain]  Cd Length: 34  Bit Score: 38.64  E-value: 1.47e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1002296096 2701 PIGQPVDMDNaSIIATFPPDLREEVLLTSSEAVLS 2735
Cdd:pfam14377    1 AAPPPEGIDP-SFLAALPPDLRQEVLAQQDDERLR 34
Rev1_UBM2 cd19318
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
2666-2695 1.80e-03

Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen.


Pssm-ID: 412037  Cd Length: 36  Bit Score: 38.36  E-value: 1.80e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1002296096 2666 PAAVEIDPEFLAALPPEIQAEVLAQQRAQR 2695
Cdd:cd19318      7 PSFSQVDPSVLAALPPDLQEELEAAYAQRQ 36
UBA_scDdi1_like cd14309
UBA domain found in Saccharomyces cerevisiae DNA-damage response protein Ddi1 and similar ...
1285-1321 3.60e-03

UBA domain found in Saccharomyces cerevisiae DNA-damage response protein Ddi1 and similar proteins; Ddi1, also called v-SNARE-master 1 (Vsm1), is a ubiquitin receptor involved in regulation of the cell cycle and late secretory pathway in Saccharomyces cerevisiae. It functions as a ubiquitin association domain (UBA)- ubiquitin-like-domain (UBL) shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. For instance, Ddi1 plays an essential role in the final stages of proteasomal degradation of Ho endonuclease and of its cognate FBP, Ufo1. Moreover, Ddi1 and its associated protein Rad23p play a cooperative role as negative regulators in yeast PHO pathway. Ddi1 contains an N-terminal UBL domain and a C-terminal UBA domain. It also harbors a central retroviral aspartyl-protease-like domain (RVP) which may be important in cell-cycle control. At this point, Ddi1 may function proteolytically during regulated protein turnover in the cell. This family also includes mammalian regulatory solute carrier protein family 1 member 1 (RSC1A1), also called transporter regulator RS1 (RS1) which mediates transcriptional and post-transcriptional regulation of Na(+)-D-glucose cotransporter SGLT1.


Pssm-ID: 270494  Cd Length: 36  Bit Score: 37.51  E-value: 3.60e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1002296096 1285 ESSIATIVEMGFSRARAEEALRSVRTNsVEMATDWLF 1321
Cdd:cd14309      1 EEKIAQLMDLGFSREEAIQALEATNGN-VELAASLLF 36
UBA_UBAC2 cd14305
UBA domain found in ubiquitin-associated domain-containing protein 2 (UBAC2) and similar ...
1285-1320 5.00e-03

UBA domain found in ubiquitin-associated domain-containing protein 2 (UBAC2) and similar proteins; UBAC2, also called phosphoglycerate dehydrogenase-like protein 1, is a ubiquitin-associated domain (UBA)-domain containing protein encoded by gene UBAC2 (or PHGDHL1), a risk gene for Behcet's disease (BD). It may play an important role in the development of BD through its transcriptional modulation. Members in this family contain an N-terminal rhomboid-like domain and a C-terminal UBA domain.


Pssm-ID: 270490  Cd Length: 38  Bit Score: 37.33  E-value: 5.00e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1002296096 1285 ESSIATIVEMGFSRARAEEALRsVRTNSVEMATDWL 1320
Cdd:cd14305      3 EEQVQQLVDMGFSREDVLEALR-QSNNDVNAATNLL 37
UBA_HERC1_2 cd14331
UBA domain found in probable E3 ubiquitin-protein ligase HERC1, HERC2 and similar proteins; ...
1288-1323 7.03e-03

UBA domain found in probable E3 ubiquitin-protein ligase HERC1, HERC2 and similar proteins; HERC1, also called HECT domain and RCC1-like domain-containing protein 1, p532, or p619, is an ubiquitously expressed giant protein involved in ubiquitin-dependent intracellular membrane trafficking through its interaction with vesicle coat proteins such as clathrin and ARF. Moreover, it has been identified as a tuberous sclerosis complex TSC2-interacting protein that may play a role in TSC-mTOR (mammalian target of rapamycin) pathway. HERC2, also called HECT domain and RCC1-like domain-containing protein 2, is a SUMO-regulated E3 ubiquitin ligase that plays an important role in the SUMO-dependent pathway which orchestrates the DNA double-strand break (DSB) response. Moreover, HERC2 functions as a RNF8 auxiliary factor that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. HERC1 and HERC2 are multi-domain proteins with different domain organizations. Both of them contain a ubiquitin-association (UBA) domain, more than one RCC1-like domains (RLDs) and a C-terminal HECT E3 ubiquitin ligase domain.


Pssm-ID: 270516  Cd Length: 40  Bit Score: 37.01  E-value: 7.03e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1002296096 1288 IATIVEMGFSRARAEEALRSV----RTNSVEMATDWLFSH 1323
Cdd:cd14331      1 IVQLMEMGFSRRQIEMAMQALgsesDAPNIENLVNWLLEH 40
UBA1_UBP5_like cd14294
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase UBP5, UBP13 and similar proteins; ...
1285-1323 8.08e-03

UBA1 domain found in ubiquitin carboxyl-terminal hydrolase UBP5, UBP13 and similar proteins; UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13, is an ortholog of UBP5. It has similar domain architecture, but functions differently from USP5 in cellular deubiquitination processes. It exhibits a weak deubiquitinating activity preferring to Lys63-linked polyubiquitin in a non-activation manner. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270480 [Multi-domain]  Cd Length: 44  Bit Score: 36.91  E-value: 8.08e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1002296096 1285 ESSIATIVEMGFSRARAEEALRSVRTNSVEMATDWLFSH 1323
Cdd:cd14294      1 EAVVSQLAEMGFPLEACRKAVYHTNNSGLEAAMNWIMEH 39
 
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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