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Conserved domains on  [gi|2062392405|ref|XP_042083789|]
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E3 ubiquitin-protein ligase HUWE1 isoform X1 [Haplochromis burtoni]

Protein Classification

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 ...
 4225-4578 7.73e-160

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: 499.01  E-value: 7.73e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4225 VHVRRDHVFEDSYRELHRKSPEDMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSH 4304
Cdd:cd00078      3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4305 CNPNHLSYFKFVGRVVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYPFFQGLVYLLENDVSTLGYELTFSTEV 4384
Cdd:cd00078     83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4385 QE-FGVCEVRDLKPNGANILVTEENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPAI 4463
Cdd:cd00078    163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4464 DIDDLKANTEY-HKYQSSSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEgmngiQKFQIHRDDRSTDRLP 4542
Cdd:cd00078    243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2062392405 4543 SAHTCFNQLDLPAYESYEKLRHMLLLAIQECsEGFG 4578
Cdd:cd00078    318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
DUF913 pfam06025
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ...
 431-853 3.72e-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: 331.12  E-value: 3.72e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  431 RAVRVVD-LITNLD--MAAFQSHSGLSIFICRLEHEVDLSRKECPFVIKPKIQRPSAAVESEdmdtdmemsevamesspr 507
Cdd:pfam06025    1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALELAEAGKGTPSEYKSSVVDYE------------------ 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  508 pstssssraegdhraqssttntpragmqcIP-QRAALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGS-LPTSLKHIISNA 583
Cdd:pfam06025   63 -----------------------------IPyYRQQLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENA 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  584 EYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLTDVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLHSFVQCQPF 663
Cdd:pfam06025  114 KVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAGLSKAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNAL 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  664 ERLFKVLLSPDYLPAMRrrrssdPLGDTASNLGSAVDELMRHQPTLKTDATTAIIKLLEEICNLGRAPEY---ICQKPSI 740
Cdd:pfam06025  194 ESFFEIFESPDHVKAME------TDGELASNLGSSFDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEpdgWGAKLWV 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  741 QKADGTVAVPPARSSHAAEEASsedeeeeealhtfsqQQGEAESSRQSVPLELVVGTEERIP-------IPLMDYILNVM 813
Cdd:pfam06025  268 GCSSSSSFSPASSGSLPMETDG---------------ESGDESSSDEDVEMEDAPDTDSTEEtepeshgNSLTDYIDNVA 332

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 2062392405  814 KFVESILSNNTtddHCQEFVNQKGLLPLVSILGLPNLPID 853
Cdd:pfam06025  333 RFLEAFFSNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
DUF908 super family cl20318
Domain of Unknown Function (DUF908);
90-367 1.68e-23

Domain of Unknown Function (DUF908);


The actual alignment was detected with superfamily member pfam06012:

Pssm-ID: 428721  Cd Length: 351  Bit Score: 105.49  E-value: 1.68e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405   90 KALLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASCDMQVVLSVLNLLYVFSKR-SNYITRLGSEKRT---PLLA---- 161
Cdd:pfam06012    3 RELVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLLRLAQRySASNSRRGSAPRHiqqSLLAnhyn 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  162 ----RLQHLAESWG------------------GKENGFGLAECCRDLPmTKYPPSATTLHFEFYAEPGPEVKVERKTSSN 219
Cdd:pfam06012   83 idldRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKEDS-KVLPSEWGSVKFTYYPSSSSDEAPTSSKSST 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  220 T-----------------------------------------LHYIHIEQLDKISESPSEIMESLtmMYNIPKDKQTLLF 258
Cdd:pfam06012  162 SsnsspstptplrrsstlgtspdspsspststpssaadsdegLRTFEIPESKVASKSLEDILAKA--IEDLPKESRFELL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  259 THIRLAHGFSNHK--KRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQITDKQLVDIKAASLRTLTSI 334
Cdd:pfam06012  240 HRIRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEAL 319

                          330       340       350
                   ....*....|....*....|....*....|...
gi 2062392405  335 VHleRTPKLSNIIDCTGTASYHGFLPVLVRNCI 367
Cdd:pfam06012  320 AR--HRAKLSDVLSALGANVNHGILLYVLRKAV 350
UBA_HUWE1 cd14288
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ...
 1398-1437 3.89e-19

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: 83.22  E-value: 3.89e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2062392405 1398 VNQAQLTQLMDMGFSREHAMEALLNTSTMEQATEYLLTHP 1437
Cdd:cd14288      1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP 40
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 1698-1759 6.76e-14

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


:

Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 69.25  E-value: 6.76e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2062392405 1698 WRWFDDRsGRWCSYSASNNSTIDSAWRAGESSV--RFTAGRRRYTVQFNTMVQVNEETGNRRPV 1759
Cdd:pfam02825    2 WEWEDDN-GGWHPYDPEVSSLIEEAYQKGKPSVdlSITTAGFPYTIDFKSMTQTNKDTGTTRPV 64
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
 3110-3143 1.59e-07

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: 50.19  E-value: 1.59e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2062392405 3110 GGPGVTEVSPEFLAALPPAIQEEVLAQQRAEQQR 3143
Cdd:pfam14377    1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
 3063-3090 1.03e-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: 47.88  E-value: 1.03e-06
                           10        20
                   ....*....|....*....|....*...
gi 2062392405 3063 PEGVDPSFLAALPEDIRREVLQNQLGIR 3090
Cdd:pfam14377    5 PEGIDPSFLAALPPDLRQEVLAQQDDER 32
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 2838-3167 1.81e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 1.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 2838 DPPRVSEGFLTAPPSG---EVTPTTPAPHEQALVSLETAISQQVHQPIADLLLAESHASSLAALAGAGLPPLSTAERPN- 2913
Cdd:PHA03247  2606 GDPRGPAPPSPLPPDThapDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRr 2685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 2914 -----------SEAEASQMEMSPAPAIGERVGGGGGGTLDEGREASLSPDIVENSEPAAAGVSQLEGS------PMDTSS 2976
Cdd:PHA03247  2686 raarptvgsltSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGparparPPTTAG 2765

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 2977 PASATQEE---AAPNPAQPTQLSQELSGSGESGLTDRQTDAETGSTSVSSPGETM---PRSDSADSQSQAIQEEPLPSTS 3050
Cdd:PHA03247  2766 PPAPAPPAapaAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPaasPAGPLPPPTSAQPTAPPPPPGP 2845

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 3051 NEEEDPLAGISLPEGvdpsflaalpeDIRREVLQNQLGI------RPPSRPPAATSLPSSTAPVLGGPGVTEVSPeflaa 3124
Cdd:PHA03247  2846 PPPSLPLGGSVAPGG-----------DVRRRPPSRSPAAkpaapaRPPVRRLARPAVSRSTESFALPPDQPERPP----- 2909

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2062392405 3125 lPPAIQEEVLAQQRAEQQRRELAQQPPQG--DTPLDPVTFIQTLP 3167
Cdd:PHA03247  2910 -QPQAPPPPQPQPQPPPPPQPQPPPPPPPrpQPPLAPTTDPAGAG 2953
PHA03255 super family cl31530
BDLF3; Provisional
 3636-3743 3.65e-03

BDLF3; Provisional


The actual alignment was detected with superfamily member PHA03255:

Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 42.20  E-value: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 3636 NKATEVPAGHPTPQAPNPNT---ATSSGATASVTTqgTAAVGAMQSTVAGPGASVGAVAQgTSSGTSIATSQTSSTTISI 3712
Cdd:PHA03255    36 NVTGTTAVTTPSPSASGPSTnqsTTLTTTSAPITT--TAILSTNTTTVTSTGTTVTPVPT-TSNASTINVTTKVTAQNIT 112

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2062392405 3713 PTSTGTiSTgrkQRGAVSNTESEKLASTGLT 3743
Cdd:PHA03255   113 ATEAGT-GT---STGVTSNVTTRSSSTTSAT 139
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 4225-4578 7.73e-160

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: 499.01  E-value: 7.73e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4225 VHVRRDHVFEDSYRELHRKSPEDMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSH 4304
Cdd:cd00078      3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4305 CNPNHLSYFKFVGRVVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYPFFQGLVYLLENDVSTLGYELTFSTEV 4384
Cdd:cd00078     83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4385 QE-FGVCEVRDLKPNGANILVTEENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPAI 4463
Cdd:cd00078    163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4464 DIDDLKANTEY-HKYQSSSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEgmngiQKFQIHRDDRSTDRLP 4542
Cdd:cd00078    243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2062392405 4543 SAHTCFNQLDLPAYESYEKLRHMLLLAIQECsEGFG 4578
Cdd:cd00078    318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 4249-4577 9.55e-156

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: 486.36  E-value: 9.55e-156
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  4249 KNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGRVVAKAVYDNR 4328
Cdd:smart00119    4 KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHLSYFRFIGRVLGKALYDNR 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  4329 LLECYFTRSFYKHILGKSVRYTDMESEDYPFFQGLVYL-LENDVSTLgYELTFSTEVQE-FGVCEVRDLKPNGANILVTE 4406
Cdd:smart00119   84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSIVLTSeFGQVKVVELKPGGSNIPVTE 162

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  4407 ENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPAIDIDDLKANTEY-HKYQSSSIQIQ 4485
Cdd:smart00119  163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYkGGYSANSQTIK 242

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  4486 WFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGmngiqKFQIHRDDRSTDRLPSAHTCFNQLDLPAYESYEKLRHM 4565
Cdd:smart00119  243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317

                           330
                    ....*....|..
gi 2062392405  4566 LLLAIQECsEGF 4577
Cdd:smart00119  318 LLLAINEG-KGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
4163-4580 4.62e-147

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 483.11  E-value: 4.62e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4163 RFAETHRTVLNQILRQSTTHL--ADGPFAVLVDYIRILDFDVKRKYFRQeleRLDEGLRKEDMAVH--VRRDHVFEDSYR 4238
Cdd:COG5021    454 RLNNLYRFYFVEHRKKTLTKNdsRLGSFISLNKLDIRRIKEDKRRKLFY---SLKQKAKIFDPYLHikVRRDRVFEDSYR 530

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4239 ELHRKSPEDMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGR 4318
Cdd:COG5021    531 EIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGR 610

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4319 VVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYPFFQGLVYLLENDVSTLGYELTFSTEVQEFGVCEVRDLKPN 4398
Cdd:COG5021    611 VIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPN 690

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4399 GANILVTEENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLP-AIDIDDLKANTEYHKY 4477
Cdd:COG5021    691 GRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPeDIDIDDWKSNTAYHGY 770

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4478 QSSSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGMNGIQKFQIHRDDRSTDRLPSAHTCFNQLDLPAYE 4557
Cdd:COG5021    771 TEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYS 850

                          410       420
                   ....*....|....*....|...
gi 2062392405 4558 SYEKLRHMLLLAIQECSeGFGLA 4580
Cdd:COG5021    851 SKEKLRSKLLTAINEGA-GFGLL 872
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 4274-4580 7.40e-118

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 376.57  E-value: 7.40e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4274 IISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNH--LSYFKFVGRVVAKAVYDNRLLECYFTRSFYKHILGKSVRYTD 4351
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4352 MESEDYPFFQGLVYLLENDVSTLG-YELTFSteVQEFGVCEVRDLKPNGANILVTEENKKEYVHLVCQMKMTGAIRKQLA 4430
Cdd:pfam00632   82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4431 AFLEGFYEIIPKRLISIFTEQELELLISGLPAIDIDDLKANTEY-HKYQSSSIQIQWFWRALRSFDQADRAKFLQFVTGT 4509
Cdd:pfam00632  160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYdGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2062392405 4510 SKVPLQGFAALegmngiQKFQIHR-DDRSTDRLPSAHTCFNQLDLPAYESYEKLRHMLLLAIQECsEGFGLA 4580
Cdd:pfam00632  240 SRLPVGGFKSL------PKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
DUF913 pfam06025
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ...
 431-853 3.72e-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: 331.12  E-value: 3.72e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  431 RAVRVVD-LITNLD--MAAFQSHSGLSIFICRLEHEVDLSRKECPFVIKPKIQRPSAAVESEdmdtdmemsevamesspr 507
Cdd:pfam06025    1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALELAEAGKGTPSEYKSSVVDYE------------------ 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  508 pstssssraegdhraqssttntpragmqcIP-QRAALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGS-LPTSLKHIISNA 583
Cdd:pfam06025   63 -----------------------------IPyYRQQLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENA 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  584 EYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLTDVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLHSFVQCQPF 663
Cdd:pfam06025  114 KVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAGLSKAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNAL 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  664 ERLFKVLLSPDYLPAMRrrrssdPLGDTASNLGSAVDELMRHQPTLKTDATTAIIKLLEEICNLGRAPEY---ICQKPSI 740
Cdd:pfam06025  194 ESFFEIFESPDHVKAME------TDGELASNLGSSFDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEpdgWGAKLWV 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  741 QKADGTVAVPPARSSHAAEEASsedeeeeealhtfsqQQGEAESSRQSVPLELVVGTEERIP-------IPLMDYILNVM 813
Cdd:pfam06025  268 GCSSSSSFSPASSGSLPMETDG---------------ESGDESSSDEDVEMEDAPDTDSTEEtepeshgNSLTDYIDNVA 332

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 2062392405  814 KFVESILSNNTtddHCQEFVNQKGLLPLVSILGLPNLPID 853
Cdd:pfam06025  333 RFLEAFFSNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
DUF908 pfam06012
Domain of Unknown Function (DUF908);
90-367 1.68e-23

Domain of Unknown Function (DUF908);


Pssm-ID: 428721  Cd Length: 351  Bit Score: 105.49  E-value: 1.68e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405   90 KALLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASCDMQVVLSVLNLLYVFSKR-SNYITRLGSEKRT---PLLA---- 161
Cdd:pfam06012    3 RELVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLLRLAQRySASNSRRGSAPRHiqqSLLAnhyn 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  162 ----RLQHLAESWG------------------GKENGFGLAECCRDLPmTKYPPSATTLHFEFYAEPGPEVKVERKTSSN 219
Cdd:pfam06012   83 idldRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKEDS-KVLPSEWGSVKFTYYPSSSSDEAPTSSKSST 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  220 T-----------------------------------------LHYIHIEQLDKISESPSEIMESLtmMYNIPKDKQTLLF 258
Cdd:pfam06012  162 SsnsspstptplrrsstlgtspdspsspststpssaadsdegLRTFEIPESKVASKSLEDILAKA--IEDLPKESRFELL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  259 THIRLAHGFSNHK--KRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQITDKQLVDIKAASLRTLTSI 334
Cdd:pfam06012  240 HRIRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEAL 319

                          330       340       350
                   ....*....|....*....|....*....|...
gi 2062392405  335 VHleRTPKLSNIIDCTGTASYHGFLPVLVRNCI 367
Cdd:pfam06012  320 AR--HRAKLSDVLSALGANVNHGILLYVLRKAV 350
UBA_HUWE1 cd14288
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ...
 1398-1437 3.89e-19

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: 83.22  E-value: 3.89e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2062392405 1398 VNQAQLTQLMDMGFSREHAMEALLNTSTMEQATEYLLTHP 1437
Cdd:cd14288      1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP 40
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 1698-1759 6.76e-14

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 69.25  E-value: 6.76e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2062392405 1698 WRWFDDRsGRWCSYSASNNSTIDSAWRAGESSV--RFTAGRRRYTVQFNTMVQVNEETGNRRPV 1759
Cdd:pfam02825    2 WEWEDDN-GGWHPYDPEVSSLIEEAYQKGKPSVdlSITTAGFPYTIDFKSMTQTNKDTGTTRPV 64
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 1698-1759 1.06e-12

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 65.82  E-value: 1.06e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2062392405  1698 WRW-FDDRSGRWCSYSASNNSTIDSAWRAGESSVRFTAGRRRYTVQFNTMVQVNEETGNRRPV 1759
Cdd:smart00678    1 YVWeYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKV 63
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
 3110-3143 1.59e-07

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: 50.19  E-value: 1.59e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2062392405 3110 GGPGVTEVSPEFLAALPPAIQEEVLAQQRAEQQR 3143
Cdd:pfam14377    1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
 3063-3090 1.03e-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: 47.88  E-value: 1.03e-06
                           10        20
                   ....*....|....*....|....*...
gi 2062392405 3063 PEGVDPSFLAALPEDIRREVLQNQLGIR 3090
Cdd:pfam14377    5 PEGIDPSFLAALPPDLRQEVLAQQDDER 32
PHA03247 PHA03247
large tegument protein UL36; Provisional
 2838-3167 1.81e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 1.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 2838 DPPRVSEGFLTAPPSG---EVTPTTPAPHEQALVSLETAISQQVHQPIADLLLAESHASSLAALAGAGLPPLSTAERPN- 2913
Cdd:PHA03247  2606 GDPRGPAPPSPLPPDThapDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRr 2685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 2914 -----------SEAEASQMEMSPAPAIGERVGGGGGGTLDEGREASLSPDIVENSEPAAAGVSQLEGS------PMDTSS 2976
Cdd:PHA03247  2686 raarptvgsltSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGparparPPTTAG 2765

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 2977 PASATQEE---AAPNPAQPTQLSQELSGSGESGLTDRQTDAETGSTSVSSPGETM---PRSDSADSQSQAIQEEPLPSTS 3050
Cdd:PHA03247  2766 PPAPAPPAapaAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPaasPAGPLPPPTSAQPTAPPPPPGP 2845

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 3051 NEEEDPLAGISLPEGvdpsflaalpeDIRREVLQNQLGI------RPPSRPPAATSLPSSTAPVLGGPGVTEVSPeflaa 3124
Cdd:PHA03247  2846 PPPSLPLGGSVAPGG-----------DVRRRPPSRSPAAkpaapaRPPVRRLARPAVSRSTESFALPPDQPERPP----- 2909

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2062392405 3125 lPPAIQEEVLAQQRAEQQRRELAQQPPQG--DTPLDPVTFIQTLP 3167
Cdd:PHA03247  2910 -QPQAPPPPQPQPQPPPPPQPQPPPPPPPrpQPPLAPTTDPAGAG 2953
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
 1398-1433 3.58e-05

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: 43.58  E-value: 3.58e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2062392405 1398 VNQAQLTQLMDMGFSREHAMEALLNTST-MEQATEYL 1433
Cdd:pfam00627    1 EDEEAIQRLVEMGFDREQVREALRATGNnVERAAEYL 37
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
 1399-1434 1.97e-03

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: 38.62  E-value: 1.97e-03
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2062392405  1399 NQAQLTQLMDMGFSREHAMEALLNTSTMEQ-ATEYLL 1434
Cdd:smart00165    1 DEEKIDQLLEMGFSREEALKALRAANGNVErAAEYLL 37
PHA03255 PHA03255
BDLF3; Provisional
 3636-3743 3.65e-03

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 42.20  E-value: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 3636 NKATEVPAGHPTPQAPNPNT---ATSSGATASVTTqgTAAVGAMQSTVAGPGASVGAVAQgTSSGTSIATSQTSSTTISI 3712
Cdd:PHA03255    36 NVTGTTAVTTPSPSASGPSTnqsTTLTTTSAPITT--TAILSTNTTTVTSTGTTVTPVPT-TSNASTINVTTKVTAQNIT 112

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2062392405 3713 PTSTGTiSTgrkQRGAVSNTESEKLASTGLT 3743
Cdd:PHA03255   113 ATEAGT-GT---STGVTSNVTTRSSSTTSAT 139
Rev1_UBM2 cd19318
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
 3066-3084 6.41e-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: 37.20  E-value: 6.41e-03
                           10
                   ....*....|....*....
gi 2062392405 3066 VDPSFLAALPEDIRREVLQ 3084
Cdd:cd19318     12 VDPSVLAALPPDLQEELEA 30
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 4225-4578 7.73e-160

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: 499.01  E-value: 7.73e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4225 VHVRRDHVFEDSYRELHRKSPEDMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSH 4304
Cdd:cd00078      3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4305 CNPNHLSYFKFVGRVVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYPFFQGLVYLLENDVSTLGYELTFSTEV 4384
Cdd:cd00078     83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4385 QE-FGVCEVRDLKPNGANILVTEENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPAI 4463
Cdd:cd00078    163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4464 DIDDLKANTEY-HKYQSSSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEgmngiQKFQIHRDDRSTDRLP 4542
Cdd:cd00078    243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2062392405 4543 SAHTCFNQLDLPAYESYEKLRHMLLLAIQECsEGFG 4578
Cdd:cd00078    318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 4249-4577 9.55e-156

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: 486.36  E-value: 9.55e-156
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  4249 KNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGRVVAKAVYDNR 4328
Cdd:smart00119    4 KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHLSYFRFIGRVLGKALYDNR 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  4329 LLECYFTRSFYKHILGKSVRYTDMESEDYPFFQGLVYL-LENDVSTLgYELTFSTEVQE-FGVCEVRDLKPNGANILVTE 4406
Cdd:smart00119   84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSIVLTSeFGQVKVVELKPGGSNIPVTE 162

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  4407 ENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPAIDIDDLKANTEY-HKYQSSSIQIQ 4485
Cdd:smart00119  163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYkGGYSANSQTIK 242

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  4486 WFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGmngiqKFQIHRDDRSTDRLPSAHTCFNQLDLPAYESYEKLRHM 4565
Cdd:smart00119  243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317

                           330
                    ....*....|..
gi 2062392405  4566 LLLAIQECsEGF 4577
Cdd:smart00119  318 LLLAINEG-KGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
4163-4580 4.62e-147

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 483.11  E-value: 4.62e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4163 RFAETHRTVLNQILRQSTTHL--ADGPFAVLVDYIRILDFDVKRKYFRQeleRLDEGLRKEDMAVH--VRRDHVFEDSYR 4238
Cdd:COG5021    454 RLNNLYRFYFVEHRKKTLTKNdsRLGSFISLNKLDIRRIKEDKRRKLFY---SLKQKAKIFDPYLHikVRRDRVFEDSYR 530

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4239 ELHRKSPEDMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGR 4318
Cdd:COG5021    531 EIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGR 610

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4319 VVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYPFFQGLVYLLENDVSTLGYELTFSTEVQEFGVCEVRDLKPN 4398
Cdd:COG5021    611 VIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPN 690

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4399 GANILVTEENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLP-AIDIDDLKANTEYHKY 4477
Cdd:COG5021    691 GRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPeDIDIDDWKSNTAYHGY 770

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4478 QSSSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGMNGIQKFQIHRDDRSTDRLPSAHTCFNQLDLPAYE 4557
Cdd:COG5021    771 TEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYS 850

                          410       420
                   ....*....|....*....|...
gi 2062392405 4558 SYEKLRHMLLLAIQECSeGFGLA 4580
Cdd:COG5021    851 SKEKLRSKLLTAINEGA-GFGLL 872
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 4274-4580 7.40e-118

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 376.57  E-value: 7.40e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4274 IISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNH--LSYFKFVGRVVAKAVYDNRLLECYFTRSFYKHILGKSVRYTD 4351
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4352 MESEDYPFFQGLVYLLENDVSTLG-YELTFSteVQEFGVCEVRDLKPNGANILVTEENKKEYVHLVCQMKMTGAIRKQLA 4430
Cdd:pfam00632   82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 4431 AFLEGFYEIIPKRLISIFTEQELELLISGLPAIDIDDLKANTEY-HKYQSSSIQIQWFWRALRSFDQADRAKFLQFVTGT 4509
Cdd:pfam00632  160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYdGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2062392405 4510 SKVPLQGFAALegmngiQKFQIHR-DDRSTDRLPSAHTCFNQLDLPAYESYEKLRHMLLLAIQECsEGFGLA 4580
Cdd:pfam00632  240 SRLPVGGFKSL------PKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
DUF913 pfam06025
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ...
 431-853 3.72e-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: 331.12  E-value: 3.72e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  431 RAVRVVD-LITNLD--MAAFQSHSGLSIFICRLEHEVDLSRKECPFVIKPKIQRPSAAVESEdmdtdmemsevamesspr 507
Cdd:pfam06025    1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALELAEAGKGTPSEYKSSVVDYE------------------ 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  508 pstssssraegdhraqssttntpragmqcIP-QRAALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGS-LPTSLKHIISNA 583
Cdd:pfam06025   63 -----------------------------IPyYRQQLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENA 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  584 EYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLTDVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLHSFVQCQPF 663
Cdd:pfam06025  114 KVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAGLSKAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNAL 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  664 ERLFKVLLSPDYLPAMRrrrssdPLGDTASNLGSAVDELMRHQPTLKTDATTAIIKLLEEICNLGRAPEY---ICQKPSI 740
Cdd:pfam06025  194 ESFFEIFESPDHVKAME------TDGELASNLGSSFDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEpdgWGAKLWV 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  741 QKADGTVAVPPARSSHAAEEASsedeeeeealhtfsqQQGEAESSRQSVPLELVVGTEERIP-------IPLMDYILNVM 813
Cdd:pfam06025  268 GCSSSSSFSPASSGSLPMETDG---------------ESGDESSSDEDVEMEDAPDTDSTEEtepeshgNSLTDYIDNVA 332

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 2062392405  814 KFVESILSNNTtddHCQEFVNQKGLLPLVSILGLPNLPID 853
Cdd:pfam06025  333 RFLEAFFSNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
DUF908 pfam06012
Domain of Unknown Function (DUF908);
90-367 1.68e-23

Domain of Unknown Function (DUF908);


Pssm-ID: 428721  Cd Length: 351  Bit Score: 105.49  E-value: 1.68e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405   90 KALLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASCDMQVVLSVLNLLYVFSKR-SNYITRLGSEKRT---PLLA---- 161
Cdd:pfam06012    3 RELVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLLRLAQRySASNSRRGSAPRHiqqSLLAnhyn 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  162 ----RLQHLAESWG------------------GKENGFGLAECCRDLPmTKYPPSATTLHFEFYAEPGPEVKVERKTSSN 219
Cdd:pfam06012   83 idldRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKEDS-KVLPSEWGSVKFTYYPSSSSDEAPTSSKSST 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  220 T-----------------------------------------LHYIHIEQLDKISESPSEIMESLtmMYNIPKDKQTLLF 258
Cdd:pfam06012  162 SsnsspstptplrrsstlgtspdspsspststpssaadsdegLRTFEIPESKVASKSLEDILAKA--IEDLPKESRFELL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405  259 THIRLAHGFSNHK--KRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQITDKQLVDIKAASLRTLTSI 334
Cdd:pfam06012  240 HRIRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEAL 319

                          330       340       350
                   ....*....|....*....|....*....|...
gi 2062392405  335 VHleRTPKLSNIIDCTGTASYHGFLPVLVRNCI 367
Cdd:pfam06012  320 AR--HRAKLSDVLSALGANVNHGILLYVLRKAV 350
UBA_HUWE1 cd14288
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ...
 1398-1437 3.89e-19

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: 83.22  E-value: 3.89e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2062392405 1398 VNQAQLTQLMDMGFSREHAMEALLNTSTMEQATEYLLTHP 1437
Cdd:cd14288      1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP 40
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 1698-1759 6.76e-14

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 69.25  E-value: 6.76e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2062392405 1698 WRWFDDRsGRWCSYSASNNSTIDSAWRAGESSV--RFTAGRRRYTVQFNTMVQVNEETGNRRPV 1759
Cdd:pfam02825    2 WEWEDDN-GGWHPYDPEVSSLIEEAYQKGKPSVdlSITTAGFPYTIDFKSMTQTNKDTGTTRPV 64
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 1698-1759 1.06e-12

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 65.82  E-value: 1.06e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2062392405  1698 WRW-FDDRSGRWCSYSASNNSTIDSAWRAGESSVRFTAGRRRYTVQFNTMVQVNEETGNRRPV 1759
Cdd:smart00678    1 YVWeYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKV 63
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
 3110-3143 1.59e-07

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: 50.19  E-value: 1.59e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2062392405 3110 GGPGVTEVSPEFLAALPPAIQEEVLAQQRAEQQR 3143
Cdd:pfam14377    1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
 3063-3090 1.03e-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: 47.88  E-value: 1.03e-06
                           10        20
                   ....*....|....*....|....*...
gi 2062392405 3063 PEGVDPSFLAALPEDIRREVLQNQLGIR 3090
Cdd:pfam14377    5 PEGIDPSFLAALPPDLRQEVLAQQDDER 32
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
 1401-1436 1.07e-06

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: 47.68  E-value: 1.07e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2062392405 1401 AQLTQLMDMGFSREHAMEAL--LNTSTMEQATEYLLTH 1436
Cdd:cd14327      1 EAVAQLVEMGFSRERAEEALraVGTNSVELAMEWLFTN 38
UBA1_atUBP14 cd14295
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
 1399-1436 5.68e-06

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: 45.83  E-value: 5.68e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2062392405 1399 NQAQLTQLMDMGFSREHAMEALLNTSTM--EQATEYLLTH 1436
Cdd:cd14295      1 DQELVAQLMEMGFPKVRAEKALFFTQNKglEEAMEWLEEH 40
PHA03247 PHA03247
large tegument protein UL36; Provisional
 2838-3167 1.81e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 1.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 2838 DPPRVSEGFLTAPPSG---EVTPTTPAPHEQALVSLETAISQQVHQPIADLLLAESHASSLAALAGAGLPPLSTAERPN- 2913
Cdd:PHA03247  2606 GDPRGPAPPSPLPPDThapDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRr 2685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 2914 -----------SEAEASQMEMSPAPAIGERVGGGGGGTLDEGREASLSPDIVENSEPAAAGVSQLEGS------PMDTSS 2976
Cdd:PHA03247  2686 raarptvgsltSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGparparPPTTAG 2765

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 2977 PASATQEE---AAPNPAQPTQLSQELSGSGESGLTDRQTDAETGSTSVSSPGETM---PRSDSADSQSQAIQEEPLPSTS 3050
Cdd:PHA03247  2766 PPAPAPPAapaAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPaasPAGPLPPPTSAQPTAPPPPPGP 2845

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 3051 NEEEDPLAGISLPEGvdpsflaalpeDIRREVLQNQLGI------RPPSRPPAATSLPSSTAPVLGGPGVTEVSPeflaa 3124
Cdd:PHA03247  2846 PPPSLPLGGSVAPGG-----------DVRRRPPSRSPAAkpaapaRPPVRRLARPAVSRSTESFALPPDQPERPP----- 2909

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2062392405 3125 lPPAIQEEVLAQQRAEQQRRELAQQPPQG--DTPLDPVTFIQTLP 3167
Cdd:PHA03247  2910 -QPQAPPPPQPQPQPPPPPQPQPPPPPPPrpQPPLAPTTDPAGAG 2953
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
 1400-1436 2.05e-05

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: 44.16  E-value: 2.05e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2062392405 1400 QAQLTQLMDMGFSREHAMEALLNT--STMEQATEYLLTH 1436
Cdd:cd14296      1 EEAVSQLMSMGFSENAAKRALYYTgnSSVEAAMNWLFEH 39
UBA1_NUB1_like cd14291
UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called ...
 1399-1433 2.31e-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: 43.98  E-value: 2.31e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2062392405 1399 NQAQLTQLMDMGFSREHAMEALLNTS-TMEQATEYL 1433
Cdd:cd14291      1 DEDKLQQLMEMGFSEAEARLALRACNgNVERAVDYI 36
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
 1398-1433 3.58e-05

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: 43.58  E-value: 3.58e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2062392405 1398 VNQAQLTQLMDMGFSREHAMEALLNTST-MEQATEYL 1433
Cdd:pfam00627    1 EDEEAIQRLVEMGFDREQVREALRATGNnVERAAEYL 37
UBA_TNR6C cd14283
UBA domain found in trinucleotide repeat-containing gene 6C protein (TNRC6C) and similar ...
 1402-1435 4.68e-05

UBA domain found in trinucleotide repeat-containing gene 6C protein (TNRC6C) and similar proteins; TNRC6C is one of three GW182 paralogs in mammalian genomes. It is enriched in P-bodies and important for efficient miRNA-mediated repression. TNRC6C is composed of an N-terminal glycine/tryptophan (G/W)-rich region containing an Ago hook responsible for Ago protein-binding; a ubiquitin-associated (UBA) domain and a glutamine (Q)-rich region in the middle region; a middle G/W-rich region, a RNA recognition motif (RRM), also called RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal G/W-rich region, at the C-terminus. A bipartite C-terminal region including the middle and C-terminal G/W-rich regions is referred as silencing domain that triggers silencing of bound transcripts by inhibiting protein expression and promoting mRNA decay via deadenylation. The C-terminal half containing the RRM domain functions as a key effector domain mediating protein synthesis repression by TNRC6C.


Pssm-ID: 270469  Cd Length: 38  Bit Score: 43.26  E-value: 4.68e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2062392405 1402 QLTQLMDMGFSREHAMEAL-LNTSTMEQATEYLLT 1435
Cdd:cd14283      3 LLKQLTDMGFKREPAEEALkSNNMNLEQAVSALLS 37
UBA2_UBP5 cd14386
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
 1398-1437 1.78e-04

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: 41.55  E-value: 1.78e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2062392405 1398 VNQAQLTQLMDMGFSREHAMEALLNTS-TMEQATEYLLTHP 1437
Cdd:cd14386      1 VPEEAVAMLVSMGFTRDQAIKALKATDnNVERAADWIFSHP 41
UBA cd14270
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ...
 1403-1431 2.58e-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: 40.80  E-value: 2.58e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2062392405 1403 LTQLMDMGFSREHAMEALLNTS-TMEQATE 1431
Cdd:cd14270      1 LAQLVEMGFSREQARRALRATNgDVEAAVE 30
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
 1395-1437 3.25e-04

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: 40.93  E-value: 3.25e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2062392405 1395 EPQVNQaqltqLMDMGFSREHAMEALLNT-STMEQATEYLLTHP 1437
Cdd:cd14297      1 EDLVKQ-----LVDMGFTEAQARKALRKTnNNVERAVDWLFEGP 39
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
 1403-1436 5.63e-04

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: 40.12  E-value: 5.63e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2062392405 1403 LTQLMDMGFSREHAMEALLNTS-TMEQATEYLLTH 1436
Cdd:cd14306      1 VAKLMELGFPEEDCIRALRACGgNVEEAANWLLEN 35
UBA_UBXN1 cd14302
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ...
 1403-1436 8.51e-04

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: 39.58  E-value: 8.51e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2062392405 1403 LTQLMDMGFSREHAMEALLNTST--MEQATEYLLTH 1436
Cdd:cd14302      3 LQTLIEMGFSRNRAEKALAKTGNqgVEAAMEWLLAH 38
UBA1_KPC2 cd14303
UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
 1398-1436 1.48e-03

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: 38.91  E-value: 1.48e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2062392405 1398 VNQAQLTQLMDMGFSREHAMEAL-LNTSTMEQATEYLLTH 1436
Cdd:cd14303      1 VDPEALKQLTEMGFPEARATKALlLNRMSPTQAMEWLLEH 40
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
 1399-1434 1.97e-03

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: 38.62  E-value: 1.97e-03
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2062392405  1399 NQAQLTQLMDMGFSREHAMEALLNTSTMEQ-ATEYLL 1434
Cdd:smart00165    1 DEEKIDQLLEMGFSREEALKALRAANGNVErAAEYLL 37
UBA_UBAC2 cd14305
UBA domain found in ubiquitin-associated domain-containing protein 2 (UBAC2) and similar ...
 1398-1434 3.12e-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: 38.10  E-value: 3.12e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2062392405 1398 VNQAQLTQLMDMGFSREHAMEALL--NTSTMEqATEYLL 1434
Cdd:cd14305      1 PSEEQVQQLVDMGFSREDVLEALRqsNNDVNA-ATNLLL 38
PHA03255 PHA03255
BDLF3; Provisional
 3636-3743 3.65e-03

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 42.20  E-value: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 3636 NKATEVPAGHPTPQAPNPNT---ATSSGATASVTTqgTAAVGAMQSTVAGPGASVGAVAQgTSSGTSIATSQTSSTTISI 3712
Cdd:PHA03255    36 NVTGTTAVTTPSPSASGPSTnqsTTLTTTSAPITT--TAILSTNTTTVTSTGTTVTPVPT-TSNASTINVTTKVTAQNIT 112

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2062392405 3713 PTSTGTiSTgrkQRGAVSNTESEKLASTGLT 3743
Cdd:PHA03255   113 ATEAGT-GT---STGVTSNVTTRSSSTTSAT 139
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
2909-3155 4.09e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.33  E-value: 4.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 2909 AERPNSEAEASQMEMSPAPAIGERVGGGGGGTldegrEASLSPDIVENSEPAAAGVSQLEGSPMDTSSPAsatqeeAAPN 2988
Cdd:PRK12323   391 APAAAAPAPAAPPAAPAAAPAAAAAARAVAAA-----PARRSPAPEALAAARQASARGPGGAPAPAPAPA------AAPA 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 2989 PAQPTqlsqelsgsgesgltdrqtdAETGSTSVSSPGETMPRSDSADSQSQAIQEEPLPSTSNEEEDPLAGislPEGVDP 3068
Cdd:PRK12323   460 AAARP--------------------AAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPA---PAQPDA 516

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 3069 SFLAALPEDIRREVLQNQLGIRPPSRPPAATS-----------LPSSTAPVLGGPGVTEVS----PEFLAALPPaiqeEV 3133
Cdd:PRK12323   517 APAGWVAESIPDPATADPDDAFETLAPAPAAApapraaaatepVVAPRPPRASASGLPDMFdgdwPALAARLPV----RG 592

                          250       260
                   ....*....|....*....|..
gi 2062392405 3134 LAQQRAEQQrrELAQQppQGDT 3155
Cdd:PRK12323   593 LAQQLARQS--ELAGV--EGDT 610
UBA2_UBP13 cd14387
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ...
 1405-1433 4.69e-03

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: 37.35  E-value: 4.69e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2062392405 1405 QLMDMGFSREHAMEALLNT-STMEQATEYL 1433
Cdd:cd14387      6 ILMSMGFPRNRAIEALKRTnNNLDRALDWL 35
UBA2_KPC2 cd14304
UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
 1399-1434 6.25e-03

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: 37.24  E-value: 6.25e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2062392405 1399 NQAQLTQLMDMGFSREHAMEAL-LNTSTMEQATEYLL 1434
Cdd:cd14304      2 NPRAVQSLMEMGFEEEDVLEALrVTRNNQNAACEWLL 38
Rev1_UBM2 cd19318
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
 3066-3084 6.41e-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: 37.20  E-value: 6.41e-03
                           10
                   ....*....|....*....
gi 2062392405 3066 VDPSFLAALPEDIRREVLQ 3084
Cdd:cd19318     12 VDPSVLAALPPDLQEELEA 30
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
2912-3158 9.50e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.14  E-value: 9.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 2912 PNSEAEASQMEMSPAPAiGERVGGGGGGTLDEGREASLSPDIVENSEPAAAGVSQLEGSPMDTSSPASATQEEAAPNPAQ 2991
Cdd:PRK07003   368 PGGGVPARVAGAVPAPG-ARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGD 446

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 2992 -PTQLSQELSGSGESGLTDRQTDAETGSTSVSSPGETMPRSDSADSQSQAIQEEPLPSTSNEEEDPLAGISLPEGV---- 3066
Cdd:PRK07003   447 aPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPaaaa 526

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062392405 3067 DPSFLAALPE-----DIRR--------EVLQN-------QLGIRPPSRPPAATSLPSSTAPVLGGPGVTEVSPEflaALP 3126
Cdd:PRK07003   527 PPAPEARPPTpaaaaPAARaggaaaalDVLRNagmrvssDRGARAAAAAKPAAAPAAAPKPAAPRVAVQVPTPR---ARA 603

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2062392405 3127 PAIQEEVLAQQRAEQQRRELAQQPPQGDTPLD 3158
Cdd:PRK07003   604 ATGDAPPNGAARAEQAAESRGAPPPWEDIPPD 635
 
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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