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Conserved domains on  [gi|1540503894|ref|XP_027346078|]
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E3 ubiquitin-protein ligase UPL1-like isoform X3 [Abrus precatorius]

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 ...
3332-3692 2.98e-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: 477.06  E-value: 2.98e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3332 LRISVRRAYILEDSYNQLRMRPTQDLKGRLNVQFQGEEGIDAGGLTREWYQLLSRVLFD-KGALLFTTVGNNATFQPNPN 3410
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNpSYGLFRYTPDDSGLLYPNPS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3411 SVYQTEHLSYFKFVGRVVGKALFDGQLLDVYFTRSFYKHILGVKVTYHDIEAVDPDYYKNLKWMLENDVS-DVPDLTFSM 3489
Cdd:cd00078     81 SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDeDDLELTFTI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3490 DADEEkliLYERNQVtdyELKPGGRNIRVTEETKHEYVDLVAEHILTNAIRPQINSFLEGFNELVPRELISIFNDKELEL 3569
Cdd:cd00078    161 ELDSS---FGGAVTV---ELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELEL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3570 LISGLPEIDLDDLKANTEYT-GYTVASNVVQWFWEVVKTFNKEDMARLLQFVTGTSKVPLEGFKALQgisgpQRFQIHKA 3648
Cdd:cd00078    235 LICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRV 309
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1540503894 3649 YGAPDRLPSAHTCFNQLDLPEYTSKEQLQERLLLAIHEaSEGFG 3692
Cdd:cd00078    310 GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINE-GAGFG 352
DUF913 pfam06025
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ...
423-791 3.43e-105

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


:

Pssm-ID: 461803  Cd Length: 369  Bit Score: 342.67  E-value: 3.43e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  423 KAVRILEAFMDYSNPAAALFRDLGGLDDTISRLKFEVTLVENggkhpdensessarsvnMVRSSSTGLDDMQPLYSEPLV 502
Cdd:pfam06025    1 RAVQFLDTLIYNFQDAFQAFRNAGGLDAIIDRIVHEVDSALE-----------------LAEAGKGTPSEYKSSVVDYEI 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  503 SYHRRLLMKALLRAISLGTY--APGNTARIYGSEEN-VLPHCLCIIFRRAKDFGGGVFSLAATVMSDLIQKDPTCFPVLD 579
Cdd:pfam06025   64 PYYRQQLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSsQLLGSLRKIIENAKVFGSSVWSLAVNILSDFIHNEPTSFAVIQ 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  580 AAGLPSAFLDA-IMDDVLNSAEAITCIPQCLDALCLNSNGLQAVKDRNSLRCFVKVFTSRTYLRALA--GDTPASLSSGL 656
Cdd:pfam06025  144 EAGLSKAFLEAvLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNALESFFEIFESPDHVKAMEtdGELASNLGSSF 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  657 DELMRHASSLRGPGVDMLVEILETISKIGS-------------VVDSSSLCPDQSSSTSVPMETDGEDKNLILPNNEPSK 723
Cdd:pfam06025  224 DELVRHHPSLKPAIINAVIDMLARVVELGStkaepdgwgaklwVGCSSSSSFSPASSGSLPMETDGESGDESSSDEDVEM 303
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  724 PD--NTEQITEPSPDASIINIesflPDCVNNISRLLETILQNADTCRIFVEKKGIEAILQLFTLPLMPPS 791
Cdd:pfam06025  304 EDapDTDSTEETEPESHGNSL----TDYIDNVARFLEAFFSNNSHCSDFIEKGGIELLLDLATLPSLPYD 369
DUF908 pfam06012
Domain of Unknown Function (DUF908);
85-363 4.45e-34

Domain of Unknown Function (DUF908);


:

Pssm-ID: 428721  Cd Length: 351  Bit Score: 136.31  E-value: 4.45e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894   85 REAVLQILRVIRIILDNCTNKHFYSSYEqHLSALLASTDPDVVEATLDTLATFLKKTVGKYSIRDTSLNS---------- 154
Cdd:pfam06012    3 RELVEAILRFTRLLLENCGNRSIYNSSE-HLNDLLNTTSLDVLLAALRLLLRLAQRYSASNSRRGSAPRHiqqsllanhy 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  155 -----KLYALAQGWG------------------GKEEGLGLIASAAPNgcDPVAYELGCTLHFEFY------AVNELESD 205
Cdd:pfam06012   82 nidldRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKED--SKVLPSEWGSVKFTYYpssssdEAPTSSKS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  206 IKVAE----------------------------------PLVQGLQIIHLSDINKCMETDLELLHKLVTeyKVPASLRFS 251
Cdd:pfam06012  160 STSSNsspstptplrrsstlgtspdspsspststpssaaDSDEGLRTFEIPESKVASKSLEDILAKAIE--DLPKESRFE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  252 LLTRLRFARAF--GSLASRQQYTCIRLYAFIVLIQACADADDLVSFFNAEPGFINELVSLLSYEDAVLEKIRVLCLHSLA 329
Cdd:pfam06012  238 LLHRIRIAKALnsSSEESRQQLLAIRLLAIANLAYIHPESTFQTKLFEYDPDLVYQLAELIHPDTEVPLELQTAALYALE 317
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1540503894  330 ALCQDRSHQPSVLTAVTSGGHRGILSSLMQKAID 363
Cdd:pfam06012  318 ALARHRAKLSDVLSALGANVNHGILLYVLRKAVA 351
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
1301-1338 3.65e-17

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: 77.34  E-value: 3.65e-17
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1540503894 1301 ATIATIVEMGFSRARAEEALRRVETNSVEMAMEWLFSH 1338
Cdd:cd14327      1 EAVAQLVEMGFSRERAEEALRAVGTNSVELAMEWLFTN 38
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
2593-2621 2.78e-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: 46.34  E-value: 2.78e-06
                           10        20
                   ....*....|....*....|....*....
gi 1540503894 2593 ASGANTIDPTFLEALPEDLRAEVLASQQA 2621
Cdd:pfam14377    2 APPPEGIDPSFLAALPPDLRQEVLAQQDD 30
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
2630-2654 1.83e-05

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: 44.03  E-value: 1.83e-05
                           10        20
                   ....*....|....*....|....*
gi 1540503894 2630 APPSAEDIDPEFLAALPPDIQAEVL 2654
Cdd:pfam14377    1 AAPPPEGIDPSFLAALPPDLRQEVL 25
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
3332-3692 2.98e-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: 477.06  E-value: 2.98e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3332 LRISVRRAYILEDSYNQLRMRPTQDLKGRLNVQFQGEEGIDAGGLTREWYQLLSRVLFD-KGALLFTTVGNNATFQPNPN 3410
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNpSYGLFRYTPDDSGLLYPNPS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3411 SVYQTEHLSYFKFVGRVVGKALFDGQLLDVYFTRSFYKHILGVKVTYHDIEAVDPDYYKNLKWMLENDVS-DVPDLTFSM 3489
Cdd:cd00078     81 SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDeDDLELTFTI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3490 DADEEkliLYERNQVtdyELKPGGRNIRVTEETKHEYVDLVAEHILTNAIRPQINSFLEGFNELVPRELISIFNDKELEL 3569
Cdd:cd00078    161 ELDSS---FGGAVTV---ELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELEL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3570 LISGLPEIDLDDLKANTEYT-GYTVASNVVQWFWEVVKTFNKEDMARLLQFVTGTSKVPLEGFKALQgisgpQRFQIHKA 3648
Cdd:cd00078    235 LICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRV 309
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1540503894 3649 YGAPDRLPSAHTCFNQLDLPEYTSKEQLQERLLLAIHEaSEGFG 3692
Cdd:cd00078    310 GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINE-GAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
3356-3691 9.19e-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: 445.91  E-value: 9.19e-142
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  3356 DLKG-RLNVQFQGEEGIDAGGLTREWYQLLSRVLFDKGALLFTTVGNNATFQPNPNSVYQT-EHLSYFKFVGRVVGKALF 3433
Cdd:smart00119    1 DLKKrVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANeEHLSYFRFIGRVLGKALY 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  3434 DGQLLDVYFTRSFYKHILGVKVTYHDIEAVDPDYYKNLKWM-LENDVSDVPDLTFSMDADEEKLilyernQVTDYELKPG 3512
Cdd:smart00119   81 DNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEELDLTFSIVLTSEFG------QVKVVELKPG 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  3513 GRNIRVTEETKHEYVDLVAEHILTNAIRPQINSFLEGFNELVPRELISIFNDKELELLISGLPEIDLDDLKANTEYT-GY 3591
Cdd:smart00119  155 GSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKgGY 234
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  3592 TVASNVVQWFWEVVKTFNKEDMARLLQFVTGTSKVPLEGFKALQGisgpqRFQIHKAYGAPDRLPSAHTCFNQLDLPEYT 3671
Cdd:smart00119  235 SANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYS 309
                           330       340
                    ....*....|....*....|
gi 1540503894  3672 SKEQLQERLLLAIHEAsEGF 3691
Cdd:smart00119  310 SKEILREKLLLAINEG-KGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
3147-3693 7.36e-138

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 456.15  E-value: 7.36e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3147 HDDQTTIWNLNTALEPLWQEL---------STCISAAEMQLGQSSFCPNMSNINVAENLQGSSTspplPPGTQRLLPFIE 3217
Cdd:COG5021    318 HDRILTQYSRPLLEETLGESTsflvvnnddSSSIKDLPHQVGSNPFLEAHPEFSELLKNQSRGT----TRDFRNKPTGWS 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3218 AFFVLCEKLQVNETIMQQDHSNATAREVKESAgCSASMSFKTDSQR--------KIDGA-----ITFTRFAEKHRRLSNA 3284
Cdd:COG5021    394 SSIEDLGQFLFSDFLTSSSTYEDLRREQLGRE-SDESFYVASNVQQqrasregpLLSGWktrlnNLYRFYFVEHRKKTLT 472
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3285 FIrqNPSLLEKSLSMMLKAPRLidFDNKRAYFRsRIRQQHDQHLSGPLRISVRRAYILEDSYNQLRMRPTQDLKGRLNVQ 3364
Cdd:COG5021    473 KN--DSRLGSFISLNKLDIRRI--KEDKRRKLF-YSLKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESGDDLKKTLEIE 547
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3365 FQGEEGIDAGGLTREWYQLLSRVLFDKGALLF--TTVGNNaTFQPNPNSVYQTEHLSYFKFVGRVVGKALFDGQLLDVYF 3442
Cdd:COG5021    548 FVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFeyITEDLY-TLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQF 626
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3443 TRSFYKHILGVKVTYHDIEAVDPDYYKNLKWMLENDVSDVP-DLTFSMdadeEKLILYERNQVtdyELKPGGRNIRVTEE 3521
Cdd:COG5021    627 SKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETIlDLTFTV----EDDSFGESRTV---ELIPNGRNISVTNE 699
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3522 TKHEYVDLVAEHILTNAIRPQINSFLEGFNELVPRELISIFNDKELELLISGLPE-IDLDDLKANTEYTGYTVASNVVQW 3600
Cdd:COG5021    700 NKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPIIVW 779
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3601 FWEVVKTFNKEDMARLLQFVTGTSKVPLEGFKALQGISGPQRFQIHKAYGAPDRLPSAHTCFNQLDLPEYTSKEQLQERL 3680
Cdd:COG5021    780 FWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKL 859
                          570
                   ....*....|...
gi 1540503894 3681 LLAIHEaSEGFGF 3693
Cdd:COG5021    860 LTAINE-GAGFGL 871
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
3382-3693 1.83e-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: 375.02  E-value: 1.83e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3382 QLLSRVLFDKGALLF-TTVGNNATFQPNPNS--VYQTEHLSYFKFVGRVVGKALFDGQLLDVYFTRSFYKHILGVKVTYH 3458
Cdd:pfam00632    1 TLLSKELFDPNYGLFeYETEDDRTYWFNPSSseSPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3459 DIEAVDPDYYKNLKWMLENDVSDVPD--LTFSMDADEEKLIlyernqvtdYELKPGGRNIRVTEETKHEYVDLVAEHILT 3536
Cdd:pfam00632   81 DLESIDPELYKSLKSLLNMDNDDDEDlgLTFTIPVFGESKT---------IELIPNGRNIPVTNENKEEYIRLYVDYRLN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3537 NAIRPQINSFLEGFNELVPRELISIFNDKELELLISGLPEIDLDDLKANTEYT-GYTVASNVVQWFWEVVKTFNKEDMAR 3615
Cdd:pfam00632  152 KSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEFSPEQRRL 231
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540503894 3616 LLQFVTGTSKVPLEGFKALqgisgpQRFQIHK-AYGAPDRLPSAHTCFNQLDLPEYTSKEQLQERLLLAIHEaSEGFGF 3693
Cdd:pfam00632  232 FLKFVTGSSRLPVGGFKSL------PKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEE-GEGFGL 303
DUF913 pfam06025
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ...
423-791 3.43e-105

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


Pssm-ID: 461803  Cd Length: 369  Bit Score: 342.67  E-value: 3.43e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  423 KAVRILEAFMDYSNPAAALFRDLGGLDDTISRLKFEVTLVENggkhpdensessarsvnMVRSSSTGLDDMQPLYSEPLV 502
Cdd:pfam06025    1 RAVQFLDTLIYNFQDAFQAFRNAGGLDAIIDRIVHEVDSALE-----------------LAEAGKGTPSEYKSSVVDYEI 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  503 SYHRRLLMKALLRAISLGTY--APGNTARIYGSEEN-VLPHCLCIIFRRAKDFGGGVFSLAATVMSDLIQKDPTCFPVLD 579
Cdd:pfam06025   64 PYYRQQLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSsQLLGSLRKIIENAKVFGSSVWSLAVNILSDFIHNEPTSFAVIQ 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  580 AAGLPSAFLDA-IMDDVLNSAEAITCIPQCLDALCLNSNGLQAVKDRNSLRCFVKVFTSRTYLRALA--GDTPASLSSGL 656
Cdd:pfam06025  144 EAGLSKAFLEAvLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNALESFFEIFESPDHVKAMEtdGELASNLGSSF 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  657 DELMRHASSLRGPGVDMLVEILETISKIGS-------------VVDSSSLCPDQSSSTSVPMETDGEDKNLILPNNEPSK 723
Cdd:pfam06025  224 DELVRHHPSLKPAIINAVIDMLARVVELGStkaepdgwgaklwVGCSSSSSFSPASSGSLPMETDGESGDESSSDEDVEM 303
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  724 PD--NTEQITEPSPDASIINIesflPDCVNNISRLLETILQNADTCRIFVEKKGIEAILQLFTLPLMPPS 791
Cdd:pfam06025  304 EDapDTDSTEETEPESHGNSL----TDYIDNVARFLEAFFSNNSHCSDFIEKGGIELLLDLATLPSLPYD 369
DUF908 pfam06012
Domain of Unknown Function (DUF908);
85-363 4.45e-34

Domain of Unknown Function (DUF908);


Pssm-ID: 428721  Cd Length: 351  Bit Score: 136.31  E-value: 4.45e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894   85 REAVLQILRVIRIILDNCTNKHFYSSYEqHLSALLASTDPDVVEATLDTLATFLKKTVGKYSIRDTSLNS---------- 154
Cdd:pfam06012    3 RELVEAILRFTRLLLENCGNRSIYNSSE-HLNDLLNTTSLDVLLAALRLLLRLAQRYSASNSRRGSAPRHiqqsllanhy 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  155 -----KLYALAQGWG------------------GKEEGLGLIASAAPNgcDPVAYELGCTLHFEFY------AVNELESD 205
Cdd:pfam06012   82 nidldRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKED--SKVLPSEWGSVKFTYYpssssdEAPTSSKS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  206 IKVAE----------------------------------PLVQGLQIIHLSDINKCMETDLELLHKLVTeyKVPASLRFS 251
Cdd:pfam06012  160 STSSNsspstptplrrsstlgtspdspsspststpssaaDSDEGLRTFEIPESKVASKSLEDILAKAIE--DLPKESRFE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  252 LLTRLRFARAF--GSLASRQQYTCIRLYAFIVLIQACADADDLVSFFNAEPGFINELVSLLSYEDAVLEKIRVLCLHSLA 329
Cdd:pfam06012  238 LLHRIRIAKALnsSSEESRQQLLAIRLLAIANLAYIHPESTFQTKLFEYDPDLVYQLAELIHPDTEVPLELQTAALYALE 317
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1540503894  330 ALCQDRSHQPSVLTAVTSGGHRGILSSLMQKAID 363
Cdd:pfam06012  318 ALARHRAKLSDVLSALGANVNHGILLYVLRKAVA 351
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
1301-1338 3.65e-17

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: 77.34  E-value: 3.65e-17
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1540503894 1301 ATIATIVEMGFSRARAEEALRRVETNSVEMAMEWLFSH 1338
Cdd:cd14327      1 EAVAQLVEMGFSRERAEEALRAVGTNSVELAMEWLFTN 38
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
1298-1335 7.82e-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: 50.90  E-value: 7.82e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1540503894 1298 PDEATIATIVEMGFSRARAEEALRRVeTNSVEMAMEWL 1335
Cdd:pfam00627    1 EDEEAIQRLVEMGFDREQVREALRAT-GNNVERAAEYL 37
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
1299-1336 2.02e-06

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: 46.71  E-value: 2.02e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1540503894  1299 DEATIATIVEMGFSRARAEEALRRVETNsVEMAMEWLF 1336
Cdd:smart00165    1 DEEKIDQLLEMGFSREEALKALRAANGN-VERAAEYLL 37
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
2593-2621 2.78e-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: 46.34  E-value: 2.78e-06
                           10        20
                   ....*....|....*....|....*....
gi 1540503894 2593 ASGANTIDPTFLEALPEDLRAEVLASQQA 2621
Cdd:pfam14377    2 APPPEGIDPSFLAALPPDLRQEVLAQQDD 30
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
2630-2654 1.83e-05

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: 44.03  E-value: 1.83e-05
                           10        20
                   ....*....|....*....|....*
gi 1540503894 2630 APPSAEDIDPEFLAALPPDIQAEVL 2654
Cdd:pfam14377    1 AAPPPEGIDPSFLAALPPDLRQEVL 25
Rev1_UBM2 cd19318
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
2626-2653 7.23e-04

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: 39.51  E-value: 7.23e-04
                           10        20
                   ....*....|....*....|....*...
gi 1540503894 2626 PPAYAPPSAEDIDPEFLAALPPDIQAEV 2653
Cdd:cd19318      1 GPIIALPSFSQVDPSVLAALPPDLQEEL 28
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
3332-3692 2.98e-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: 477.06  E-value: 2.98e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3332 LRISVRRAYILEDSYNQLRMRPTQDLKGRLNVQFQGEEGIDAGGLTREWYQLLSRVLFD-KGALLFTTVGNNATFQPNPN 3410
Cdd:cd00078      1 LKITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNpSYGLFRYTPDDSGLLYPNPS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3411 SVYQTEHLSYFKFVGRVVGKALFDGQLLDVYFTRSFYKHILGVKVTYHDIEAVDPDYYKNLKWMLENDVS-DVPDLTFSM 3489
Cdd:cd00078     81 SFADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDeDDLELTFTI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3490 DADEEkliLYERNQVtdyELKPGGRNIRVTEETKHEYVDLVAEHILTNAIRPQINSFLEGFNELVPRELISIFNDKELEL 3569
Cdd:cd00078    161 ELDSS---FGGAVTV---ELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELEL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3570 LISGLPEIDLDDLKANTEYT-GYTVASNVVQWFWEVVKTFNKEDMARLLQFVTGTSKVPLEGFKALQgisgpQRFQIHKA 3648
Cdd:cd00078    235 LICGSEDIDLEDLKKNTEYKgGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRV 309
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1540503894 3649 YGAPDRLPSAHTCFNQLDLPEYTSKEQLQERLLLAIHEaSEGFG 3692
Cdd:cd00078    310 GSPDDRLPTAHTCFNLLKLPPYSSKEILREKLLYAINE-GAGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
3356-3691 9.19e-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: 445.91  E-value: 9.19e-142
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  3356 DLKG-RLNVQFQGEEGIDAGGLTREWYQLLSRVLFDKGALLFTTVGNNATFQPNPNSVYQT-EHLSYFKFVGRVVGKALF 3433
Cdd:smart00119    1 DLKKrVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANeEHLSYFRFIGRVLGKALY 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  3434 DGQLLDVYFTRSFYKHILGVKVTYHDIEAVDPDYYKNLKWM-LENDVSDVPDLTFSMDADEEKLilyernQVTDYELKPG 3512
Cdd:smart00119   81 DNRLLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEELDLTFSIVLTSEFG------QVKVVELKPG 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  3513 GRNIRVTEETKHEYVDLVAEHILTNAIRPQINSFLEGFNELVPRELISIFNDKELELLISGLPEIDLDDLKANTEYT-GY 3591
Cdd:smart00119  155 GSNIPVTEENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYKgGY 234
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  3592 TVASNVVQWFWEVVKTFNKEDMARLLQFVTGTSKVPLEGFKALQGisgpqRFQIHKAYGAPDRLPSAHTCFNQLDLPEYT 3671
Cdd:smart00119  235 SANSQTIKWFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYS 309
                           330       340
                    ....*....|....*....|
gi 1540503894  3672 SKEQLQERLLLAIHEAsEGF 3691
Cdd:smart00119  310 SKEILREKLLLAINEG-KGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
3147-3693 7.36e-138

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 456.15  E-value: 7.36e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3147 HDDQTTIWNLNTALEPLWQEL---------STCISAAEMQLGQSSFCPNMSNINVAENLQGSSTspplPPGTQRLLPFIE 3217
Cdd:COG5021    318 HDRILTQYSRPLLEETLGESTsflvvnnddSSSIKDLPHQVGSNPFLEAHPEFSELLKNQSRGT----TRDFRNKPTGWS 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3218 AFFVLCEKLQVNETIMQQDHSNATAREVKESAgCSASMSFKTDSQR--------KIDGA-----ITFTRFAEKHRRLSNA 3284
Cdd:COG5021    394 SSIEDLGQFLFSDFLTSSSTYEDLRREQLGRE-SDESFYVASNVQQqrasregpLLSGWktrlnNLYRFYFVEHRKKTLT 472
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3285 FIrqNPSLLEKSLSMMLKAPRLidFDNKRAYFRsRIRQQHDQHLSGPLRISVRRAYILEDSYNQLRMRPTQDLKGRLNVQ 3364
Cdd:COG5021    473 KN--DSRLGSFISLNKLDIRRI--KEDKRRKLF-YSLKQKAKIFDPYLHIKVRRDRVFEDSYREIMDESGDDLKKTLEIE 547
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3365 FQGEEGIDAGGLTREWYQLLSRVLFDKGALLF--TTVGNNaTFQPNPNSVYQTEHLSYFKFVGRVVGKALFDGQLLDVYF 3442
Cdd:COG5021    548 FVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFeyITEDLY-TLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQF 626
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3443 TRSFYKHILGVKVTYHDIEAVDPDYYKNLKWMLENDVSDVP-DLTFSMdadeEKLILYERNQVtdyELKPGGRNIRVTEE 3521
Cdd:COG5021    627 SKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETIlDLTFTV----EDDSFGESRTV---ELIPNGRNISVTNE 699
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3522 TKHEYVDLVAEHILTNAIRPQINSFLEGFNELVPRELISIFNDKELELLISGLPE-IDLDDLKANTEYTGYTVASNVVQW 3600
Cdd:COG5021    700 NKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPIIVW 779
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3601 FWEVVKTFNKEDMARLLQFVTGTSKVPLEGFKALQGISGPQRFQIHKAYGAPDRLPSAHTCFNQLDLPEYTSKEQLQERL 3680
Cdd:COG5021    780 FWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKL 859
                          570
                   ....*....|...
gi 1540503894 3681 LLAIHEaSEGFGF 3693
Cdd:COG5021    860 LTAINE-GAGFGL 871
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
3382-3693 1.83e-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: 375.02  E-value: 1.83e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3382 QLLSRVLFDKGALLF-TTVGNNATFQPNPNS--VYQTEHLSYFKFVGRVVGKALFDGQLLDVYFTRSFYKHILGVKVTYH 3458
Cdd:pfam00632    1 TLLSKELFDPNYGLFeYETEDDRTYWFNPSSseSPDLELLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3459 DIEAVDPDYYKNLKWMLENDVSDVPD--LTFSMDADEEKLIlyernqvtdYELKPGGRNIRVTEETKHEYVDLVAEHILT 3536
Cdd:pfam00632   81 DLESIDPELYKSLKSLLNMDNDDDEDlgLTFTIPVFGESKT---------IELIPNGRNIPVTNENKEEYIRLYVDYRLN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894 3537 NAIRPQINSFLEGFNELVPRELISIFNDKELELLISGLPEIDLDDLKANTEYT-GYTVASNVVQWFWEVVKTFNKEDMAR 3615
Cdd:pfam00632  152 KSIEPQLEAFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYDgGYTKNSPTIQWFWEILEEFSPEQRRL 231
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540503894 3616 LLQFVTGTSKVPLEGFKALqgisgpQRFQIHK-AYGAPDRLPSAHTCFNQLDLPEYTSKEQLQERLLLAIHEaSEGFGF 3693
Cdd:pfam00632  232 FLKFVTGSSRLPVGGFKSL------PKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEE-GEGFGL 303
DUF913 pfam06025
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ...
423-791 3.43e-105

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


Pssm-ID: 461803  Cd Length: 369  Bit Score: 342.67  E-value: 3.43e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  423 KAVRILEAFMDYSNPAAALFRDLGGLDDTISRLKFEVTLVENggkhpdensessarsvnMVRSSSTGLDDMQPLYSEPLV 502
Cdd:pfam06025    1 RAVQFLDTLIYNFQDAFQAFRNAGGLDAIIDRIVHEVDSALE-----------------LAEAGKGTPSEYKSSVVDYEI 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  503 SYHRRLLMKALLRAISLGTY--APGNTARIYGSEEN-VLPHCLCIIFRRAKDFGGGVFSLAATVMSDLIQKDPTCFPVLD 579
Cdd:pfam06025   64 PYYRQQLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSsQLLGSLRKIIENAKVFGSSVWSLAVNILSDFIHNEPTSFAVIQ 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  580 AAGLPSAFLDA-IMDDVLNSAEAITCIPQCLDALCLNSNGLQAVKDRNSLRCFVKVFTSRTYLRALA--GDTPASLSSGL 656
Cdd:pfam06025  144 EAGLSKAFLEAvLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNALESFFEIFESPDHVKAMEtdGELASNLGSSF 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  657 DELMRHASSLRGPGVDMLVEILETISKIGS-------------VVDSSSLCPDQSSSTSVPMETDGEDKNLILPNNEPSK 723
Cdd:pfam06025  224 DELVRHHPSLKPAIINAVIDMLARVVELGStkaepdgwgaklwVGCSSSSSFSPASSGSLPMETDGESGDESSSDEDVEM 303
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  724 PD--NTEQITEPSPDASIINIesflPDCVNNISRLLETILQNADTCRIFVEKKGIEAILQLFTLPLMPPS 791
Cdd:pfam06025  304 EDapDTDSTEETEPESHGNSL----TDYIDNVARFLEAFFSNNSHCSDFIEKGGIELLLDLATLPSLPYD 369
DUF908 pfam06012
Domain of Unknown Function (DUF908);
85-363 4.45e-34

Domain of Unknown Function (DUF908);


Pssm-ID: 428721  Cd Length: 351  Bit Score: 136.31  E-value: 4.45e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894   85 REAVLQILRVIRIILDNCTNKHFYSSYEqHLSALLASTDPDVVEATLDTLATFLKKTVGKYSIRDTSLNS---------- 154
Cdd:pfam06012    3 RELVEAILRFTRLLLENCGNRSIYNSSE-HLNDLLNTTSLDVLLAALRLLLRLAQRYSASNSRRGSAPRHiqqsllanhy 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  155 -----KLYALAQGWG------------------GKEEGLGLIASAAPNgcDPVAYELGCTLHFEFY------AVNELESD 205
Cdd:pfam06012   82 nidldRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKED--SKVLPSEWGSVKFTYYpssssdEAPTSSKS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  206 IKVAE----------------------------------PLVQGLQIIHLSDINKCMETDLELLHKLVTeyKVPASLRFS 251
Cdd:pfam06012  160 STSSNsspstptplrrsstlgtspdspsspststpssaaDSDEGLRTFEIPESKVASKSLEDILAKAIE--DLPKESRFE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540503894  252 LLTRLRFARAF--GSLASRQQYTCIRLYAFIVLIQACADADDLVSFFNAEPGFINELVSLLSYEDAVLEKIRVLCLHSLA 329
Cdd:pfam06012  238 LLHRIRIAKALnsSSEESRQQLLAIRLLAIANLAYIHPESTFQTKLFEYDPDLVYQLAELIHPDTEVPLELQTAALYALE 317
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1540503894  330 ALCQDRSHQPSVLTAVTSGGHRGILSSLMQKAID 363
Cdd:pfam06012  318 ALARHRAKLSDVLSALGANVNHGILLYVLRKAVA 351
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
1301-1338 3.65e-17

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: 77.34  E-value: 3.65e-17
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1540503894 1301 ATIATIVEMGFSRARAEEALRRVETNSVEMAMEWLFSH 1338
Cdd:cd14327      1 EAVAQLVEMGFSRERAEEALRAVGTNSVELAMEWLFTN 38
UBA_UBXN1 cd14302
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ...
1301-1341 9.05e-12

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: 61.92  E-value: 9.05e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1540503894 1301 ATIATIVEMGFSRARAEEALRRVETNSVEMAMEWLFSHADD 1341
Cdd:cd14302      1 SELQTLIEMGFSRNRAEKALAKTGNQGVEAAMEWLLAHEDD 41
UBA2_UBP5 cd14386
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
1298-1341 8.80e-11

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: 59.27  E-value: 8.80e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1540503894 1298 PDEATIATIVEMGFSRARAEEALRRVEtNSVEMAMEWLFSHADD 1341
Cdd:cd14386      1 VPEEAVAMLVSMGFTRDQAIKALKATD-NNVERAADWIFSHPDE 43
UBA1_atUBP14 cd14295
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
1299-1342 1.50e-09

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: 55.84  E-value: 1.50e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1540503894 1299 DEATIATIVEMGFSRARAEEALRRVETNSVEMAMEWLFSHADDP 1342
Cdd:cd14295      1 DQELVAQLMEMGFPKVRAEKALFFTQNKGLEEAMEWLEEHSEDA 44
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
1303-1339 6.23e-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: 54.02  E-value: 6.23e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1540503894 1303 IATIVEMGFSRARAEEALRRVEtNSVEMAMEWLFSHA 1339
Cdd:cd14297      4 VKQLVDMGFTEAQARKALRKTN-NNVERAVDWLFEGP 39
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
1300-1338 1.22e-08

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: 53.02  E-value: 1.22e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1540503894 1300 EATIATIVEMGFSRARAEEALRRVETNSVEMAMEWLFSH 1338
Cdd:cd14296      1 EEAVSQLMSMGFSENAAKRALYYTGNSSVEAAMNWLFEH 39
UBA1_spUBP14_like cd14385
UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
1299-1342 2.98e-08

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: 52.41  E-value: 2.98e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1540503894 1299 DEATIATIVEMGFSRARAEEALRRVETNSVEMAMEWLFSHADDP 1342
Cdd:cd14385      1 NAEALAQLLGMGFPEVRCKKALLATGNSDAEAAMNWLFEHMDDP 44
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
1298-1335 7.82e-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: 50.90  E-value: 7.82e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1540503894 1298 PDEATIATIVEMGFSRARAEEALRRVeTNSVEMAMEWL 1335
Cdd:pfam00627    1 EDEEAIQRLVEMGFDREQVREALRAT-GNNVERAAEYL 37
UBA1_KPC2 cd14303
UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
1298-1339 1.44e-06

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: 47.39  E-value: 1.44e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1540503894 1298 PDEATIATIVEMGFSRARAEEALrRVETNSVEMAMEWLFSHA 1339
Cdd:cd14303      1 VDPEALKQLTEMGFPEARATKAL-LLNRMSPTQAMEWLLEHE 41
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
1299-1336 2.02e-06

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: 46.71  E-value: 2.02e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1540503894  1299 DEATIATIVEMGFSRARAEEALRRVETNsVEMAMEWLF 1336
Cdd:smart00165    1 DEEKIDQLLEMGFSREEALKALRAANGN-VERAAEYLL 37
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
2593-2621 2.78e-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: 46.34  E-value: 2.78e-06
                           10        20
                   ....*....|....*....|....*....
gi 1540503894 2593 ASGANTIDPTFLEALPEDLRAEVLASQQA 2621
Cdd:pfam14377    2 APPPEGIDPSFLAALPPDLRQEVLAQQDD 30
UBA_RUP1p cd14307
UBA domain found in yeast UBA domain-containing protein RUP1p and similar proteins; RUP1p is a ...
1303-1338 4.53e-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: 45.75  E-value: 4.53e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1540503894 1303 IATIVEMGFSRARAEEALRRVETNsVEMAMEWLFSH 1338
Cdd:cd14307      4 VASLLEMGIPREVAIEALRETNGD-VEAAANYIFSN 38
UBA1_UBP5_like cd14294
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase UBP5, UBP13 and similar proteins; ...
1300-1342 6.76e-06

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: 45.38  E-value: 6.76e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1540503894 1300 EATIATIVEMGFSRARAEEALRRVETNSVEMAMEWLFSHADDP 1342
Cdd:cd14294      1 EAVVSQLAEMGFPLEACRKAVYHTNNSGLEAAMNWIMEHMDDP 43
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
2630-2654 1.83e-05

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: 44.03  E-value: 1.83e-05
                           10        20
                   ....*....|....*....|....*
gi 1540503894 2630 APPSAEDIDPEFLAALPPDIQAEVL 2654
Cdd:pfam14377    1 AAPPPEGIDPSFLAALPPDLRQEVL 25
UBA cd14270
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ...
1303-1333 2.06e-05

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: 43.88  E-value: 2.06e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1540503894 1303 IATIVEMGFSRARAEEALRRVEtNSVEMAME 1333
Cdd:cd14270      1 LAQLVEMGFSREQARRALRATN-GDVEAAVE 30
UBA_PUB_plant cd14290
UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family ...
1299-1342 3.02e-05

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: 43.97  E-value: 3.02e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1540503894 1299 DEATIATIVEMGFSRARAEEALRRVETNSVEMAMEWLFSHADDP 1342
Cdd:cd14290      3 NADLLKELEAMGFPRARAVRALHHTGNTSVEAAVNWIVEHENDP 46
UBA2_UBP13 cd14387
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ...
1300-1335 3.10e-05

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: 43.52  E-value: 3.10e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1540503894 1300 EATIATIVEMGFSRARAEEALRRVEtNSVEMAMEWL 1335
Cdd:cd14387      1 EESIAILMSMGFPRNRAIEALKRTN-NNLDRALDWL 35
UBA1_NUB1_like cd14291
UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called ...
1299-1335 3.35e-05

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: 43.21  E-value: 3.35e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1540503894 1299 DEATIATIVEMGFSRARAEEALRRVeTNSVEMAMEWL 1335
Cdd:cd14291      1 DEDKLQQLMEMGFSEAEARLALRAC-NGNVERAVDYI 36
UBA_UBS3B cd14301
UBA domain found in ubiquitin-associated and SH3 domain-containing protein B (UBS3B) and ...
1305-1338 4.76e-05

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: 42.81  E-value: 4.76e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1540503894 1305 TIVEMGFSRARAEEALRRVETNSVEMAMEWLFSH 1338
Cdd:cd14301      5 VLLSMGFPKHRAEKALAATGGRSVQLASDWLLSH 38
UBA_HUWE1 cd14288
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ...
1298-1338 2.64e-04

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: 40.85  E-value: 2.64e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1540503894 1298 PDEATIATIVEMGFSRARAEEALrrVETNSVEMAMEWLFSH 1338
Cdd:cd14288      1 VNEAHLQQLMDMGFTREHALEAL--LHTSTLEQATEYLLTH 39
UBA1_UBP5 cd14383
UBA1 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
1299-1342 3.51e-04

UBA1 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 UBA1 domain.


Pssm-ID: 270566 [Multi-domain]  Cd Length: 49  Bit Score: 40.81  E-value: 3.51e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1540503894 1299 DEATIATIVEMGFSRARAEEALRRVETNSVEMAMEWLFSHADDP 1342
Cdd:cd14383      3 DESVIIQLVEMGFPMDACRKAVYYTGNSGAEAAMNWVMSHMDDP 46
UBA2_KPC2 cd14304
UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
1298-1337 4.99e-04

UBA2 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 UBA2 domain.


Pssm-ID: 270489  Cd Length: 39  Bit Score: 39.93  E-value: 4.99e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1540503894 1298 PDEATIATIVEMGFSRARAEEALrRVETNSVEMAMEWLFS 1337
Cdd:cd14304      1 PNPRAVQSLMEMGFEEEDVLEAL-RVTRNNQNAACEWLLG 39
Rev1_UBM2 cd19318
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
2626-2653 7.23e-04

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: 39.51  E-value: 7.23e-04
                           10        20
                   ....*....|....*....|....*...
gi 1540503894 2626 PPAYAPPSAEDIDPEFLAALPPDIQAEV 2653
Cdd:cd19318      1 GPIIALPSFSQVDPSVLAALPPDLQEEL 28
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
1307-1339 1.08e-03

UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required.


Pssm-ID: 270491  Cd Length: 36  Bit Score: 38.96  E-value: 1.08e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1540503894 1307 VEMGFSRARAEEALRRVEtNSVEMAMEWLFSHA 1339
Cdd:cd14306      5 MELGFPEEDCIRALRACG-GNVEEAANWLLENA 36
UBA_At3g58460_like cd14287
UBA domain found in uncharacterized protein At3g58460 from Arabidopsis thaliana and its ...
1300-1335 2.69e-03

UBA domain found in uncharacterized protein At3g58460 from Arabidopsis thaliana and its homologs from other plants; The uncharacterized protein At3g58460 from Arabidopsis thaliana is also known as rhomboid-like protein 15 which is encoded by RBL15 gene. Although the biological function of the family members remains unclear, they all contain an N-terminal rhomboid-like domain and a C-terminal ubiquitin-associated (UBA) domain.


Pssm-ID: 270473 [Multi-domain]  Cd Length: 36  Bit Score: 38.14  E-value: 2.69e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1540503894 1300 EATIATIVEMGFSRARAEEALRRVETNsVEMAMEWL 1335
Cdd:cd14287      1 EALVQSLVAMGFEKHRARRALDAAGGD-INTAVEIL 35
UBA_scDdi1_like cd14309
UBA domain found in Saccharomyces cerevisiae DNA-damage response protein Ddi1 and similar ...
1300-1336 3.40e-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: 3.40e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1540503894 1300 EATIATIVEMGFSRARAEEALRRVETNsVEMAMEWLF 1336
Cdd:cd14309      1 EEKIAQLMDLGFSREEAIQALEATNGN-VELAASLLF 36
UBA_atDRM2_like cd14330
UBA domain found in Arabidopsis thaliana DNA (cytosine-5)-methyltransferase DRM2 (atDRM2) and ...
1300-1337 5.47e-03

UBA domain found in Arabidopsis thaliana DNA (cytosine-5)-methyltransferase DRM2 (atDRM2) and similar proteins; atDRM2, also called protein domains rearranged methylase 2, is a homolog of the mammalian de novo methyltransferase DNMT3. It is the major de novo methyltransferase targeted to DNA by small interfering RNAs (siRNAs) in the RNA-directed DNA methylation (RdDM) pathway in Arabidopsis thaliana. atDRM2 is a part of the RdDM effector complex and plays a catalytic role in RdDM. It contains an N-terminal UBA domains and a C-terminal methyltransferase domain, both of which are required for normal RdDM.


Pssm-ID: 270515  Cd Length: 37  Bit Score: 37.04  E-value: 5.47e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1540503894 1300 EATIATIVEMGFSRARAEEALRRVEtNSVEMAMEWLFS 1337
Cdd:cd14330      1 EEKIKTLVSMGFSESDARRALERCG-YDVAAAADFLFS 37
 
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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