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Conserved domains on  [gi|688612066|ref|XP_009295238|]
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E3 ubiquitin-protein ligase HUWE1 isoform X6 [Danio rerio]

Protein Classification

DUF913 and HECTc domain-containing protein( domain architecture ID 11003809)

protein containing domains DUF913, UBA_HUWE1, 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 ...
 4156-4509 9.56e-159

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: 495.93  E-value: 9.56e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4156 VHVRRDHVFEDSYRELHRKSPEDMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSH 4235
Cdd:cd00078     3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4236 CNPNHLSYFKFVGRVVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYPFFQGLVYLLENDVSTLGYELTFSTEV 4315
Cdd:cd00078    83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4316 QE-FGVCEVRDLKANGANILVTEENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTI 4394
Cdd:cd00078   163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4395 DIDDLKANTEY-HKYQSSSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEgmngiQKFQIHRDDRSTDRLP 4473
Cdd:cd00078   243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 688612066 4474 SAHTCFNQLDLPAYESYEKLRHMLLLAIQECsEGFG 4509
Cdd:cd00078   318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
DUF913 pfam06025
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ...
 431-847 5.87e-102

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


:

Pssm-ID: 461803  Cd Length: 369  Bit Score: 333.43  E-value: 5.87e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   431 RAVRVVD-LITNLD--MAAFQSHGGLSIFICRLEHEVDLSRKECPFVIKPKIQRPSTATETEdmdtdmdmsevamesspg 507
Cdd:pfam06025    1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALELAEAGKGTPSEYKSSVVDYE------------------ 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   508 pstssgsraetdsraqsnasstpragvqcIP-QRAALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGS-LPTSLKHIISNA 583
Cdd:pfam06025   63 -----------------------------IPyYRQQLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENA 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   584 EYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLTDVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLHSFVQCQPF 663
Cdd:pfam06025  114 KVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAGLSKAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNAL 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   664 ERLFKVLLSPDYLPAMRrrrssdPLGDTASNLGSAVDELMRHQPTLKTDATTAIIKLLEEICNLGRSPEY---ICQKPSI 740
Cdd:pfam06025  194 ESFFEIFESPDHVKAME------TDGELASNLGSSFDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEpdgWGAKLWV 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   741 QKADGTVTVPPARSNHAAEEASSEDEEEEEalHTFSQQQGEPESNRQVVGTEERIPIPLMDYILNVMKFVESILSNNTtd 820
Cdd:pfam06025  268 GCSSSSSFSPASSGSLPMETDGESGDESSS--DEDVEMEDAPDTDSTEETEPESHGNSLTDYIDNVARFLEAFFSNNS-- 343

                          410       420
                   ....*....|....*....|....*..
gi 688612066   821 dHCQEFVNQKGLLPLVSILGLPNLPID 847
Cdd:pfam06025  344 -HCSDFIEKGGIELLLDLATLPSLPYD 369
DUF908 super family cl20318
Domain of Unknown Function (DUF908);
90-367 1.59e-24

Domain of Unknown Function (DUF908);


The actual alignment was detected with superfamily member pfam06012:

Pssm-ID: 428721  Cd Length: 351  Bit Score: 108.58  E-value: 1.59e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066    90 KALLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASCDMQVVLSVLNLLYVFSKR-SNYITRLGSDKRS---PLLA---- 161
Cdd:pfam06012    3 RELVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLLRLAQRySASNSRRGSAPRHiqqSLLAnhyn 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   162 ----RLQHLAESWG------------------GKENGFGLAECCRDLPmSKYPPSATTLHFEFYAEPSSEVKVEKKSSSN 219
Cdd:pfam06012   83 idldRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKEDS-KVLPSEWGSVKFTYYPSSSSDEAPTSSKSST 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   220 T-----------------------------------------LHYIHIEQLDKISESPSEIMESltAMYNIPKDKQILLF 258
Cdd:pfam06012  162 SsnsspstptplrrsstlgtspdspsspststpssaadsdegLRTFEIPESKVASKSLEDILAK--AIEDLPKESRFELL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   259 THIRLAHGFSNHK--RRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQITDKQLVDIKAASLRTLTSI 334
Cdd:pfam06012  240 HRIRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEAL 319

                          330       340       350
                   ....*....|....*....|....*....|...
gi 688612066   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, ...
 1389-1428 3.87e-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: 3.87e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 688612066 1389 VNQAQLTQLMDMGFSREHAMEALLNTSTMEQATEYLLTHP 1428
Cdd:cd14288     1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP 40
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 1689-1750 3.33e-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: 70.02  E-value: 3.33e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688612066  1689 WRWFDDRsGRWCSYSASNNSTIDSAWRAGETSV--RFTAGRRRYTVQFNTMVQVNEETGNRRPV 1750
Cdd:pfam02825    2 WEWEDDN-GGWHPYDPEVSSLIEEAYQKGKPSVdlSITTAGFPYTIDFKSMTQTNKDTGTTRPV 64
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
 3099-3132 1.46e-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: 1.46e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 688612066  3099 GGPGVTEVSPEFLAALPPAIQEEVLAQQRAEQQR 3132
Cdd:pfam14377    1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
 3051-3078 9.68e-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: 47.88  E-value: 9.68e-07
                           10        20
                   ....*....|....*....|....*...
gi 688612066  3051 PEGVDPSFLAALPEDIRREVLQNQLGIR 3078
Cdd:pfam14377    5 PEGIDPSFLAALPPDLRQEVLAQQDDER 32
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 2884-3156 7.57e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 7.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 2884 PDSHGALAGAGLPqlSAPDRPNCEAEASQMEMSPAPTIGERGGGALDAVREASLSPDIAESSePVPVGVSQlEGSPMDTS 2963
Cdd:PHA03247 2689 RPTVGSLTSLADP--PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGP-ATPGGPAR-PARPPTTA 2764

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 2964 SPasgtqEEPAASSVPSNHMSQELSGSGDSGLTDRQTDAETGSTSVSSPGETMPRSDSADSQSQAIQEEPLPSTSNEEED 3043
Cdd:PHA03247 2765 GP-----PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP 2839

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 3044 PLAGISLPEGVDPSFLAALPEDIRRevlqnqlgiRPPSRPPVASTLTTTASAVLGGGPGVTEVSPEFLAALP-------- 3115
Cdd:PHA03247 2840 PPPPGPPPPSLPLGGSVAPGGDVRR---------RPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPdqperppq 2910

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 688612066 3116 PAIQEEVLAQQRAEQQRRELSQQPTQG--DQPLDPVTFIQTLP 3156
Cdd:PHA03247 2911 PQAPPPPQPQPQPPPPPQPQPPPPPPPrpQPPLAPTTDPAGAG 2953
 
Name Accession Description Interval E-value
HECTc cd00078
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ...
 4156-4509 9.56e-159

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: 495.93  E-value: 9.56e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4156 VHVRRDHVFEDSYRELHRKSPEDMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSH 4235
Cdd:cd00078     3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4236 CNPNHLSYFKFVGRVVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYPFFQGLVYLLENDVSTLGYELTFSTEV 4315
Cdd:cd00078    83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4316 QE-FGVCEVRDLKANGANILVTEENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTI 4394
Cdd:cd00078   163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4395 DIDDLKANTEY-HKYQSSSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEgmngiQKFQIHRDDRSTDRLP 4473
Cdd:cd00078   243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 688612066 4474 SAHTCFNQLDLPAYESYEKLRHMLLLAIQECsEGFG 4509
Cdd:cd00078   318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 4180-4508 6.25e-155

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: 484.04  E-value: 6.25e-155
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   4180 KNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGRVVAKAVYDNR 4259
Cdd:smart00119    4 KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHLSYFRFIGRVLGKALYDNR 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   4260 LLECYFTRSFYKHILGKSVRYTDMESEDYPFFQGLVYL-LENDVSTLgYELTFSTEVQE-FGVCEVRDLKANGANILVTE 4337
Cdd:smart00119   84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSIVLTSeFGQVKVVELKPGGSNIPVTE 162

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   4338 ENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKANTEY-HKYQSSSIQIQ 4416
Cdd:smart00119  163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYkGGYSANSQTIK 242

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   4417 WFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGmngiqKFQIHRDDRSTDRLPSAHTCFNQLDLPAYESYEKLRHM 4496
Cdd:smart00119  243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317

                           330
                    ....*....|..
gi 688612066   4497 LLLAIQECsEGF 4508
Cdd:smart00119  318 LLLAINEG-KGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
4094-4511 1.40e-145

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 478.88  E-value: 1.40e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4094 RFAETHRTVLNQILRQSTTHL--ADGPFAVLVDYIRILDFDVKRKYFRQeleRLDEGLRKEDMAVH--VRRDHVFEDSYR 4169
Cdd:COG5021   454 RLNNLYRFYFVEHRKKTLTKNdsRLGSFISLNKLDIRRIKEDKRRKLFY---SLKQKAKIFDPYLHikVRRDRVFEDSYR 530

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4170 ELHRKSPEDMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGR 4249
Cdd:COG5021   531 EIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGR 610

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4250 VVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYPFFQGLVYLLENDVSTLGYELTFSTEVQEFGVCEVRDLKAN 4329
Cdd:COG5021   611 VIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPN 690

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4330 GANILVTEENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPT-IDIDDLKANTEYHKY 4408
Cdd:COG5021   691 GRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGY 770

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4409 QSSSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGMNGIQKFQIHRDDRSTDRLPSAHTCFNQLDLPAYE 4488
Cdd:COG5021   771 TEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYS 850

                         410       420
                  ....*....|....*....|...
gi 688612066 4489 SYEKLRHMLLLAIQECSeGFGLA 4511
Cdd:COG5021   851 SKEKLRSKLLTAINEGA-GFGLL 872
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 4205-4511 3.95e-117

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 374.25  E-value: 3.95e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066  4205 IISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNH--LSYFKFVGRVVAKAVYDNRLLECYFTRSFYKHILGKSVRYTD 4282
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066  4283 MESEDYPFFQGLVYLLENDVSTLG-YELTFSteVQEFGVCEVRDLKANGANILVTEENKKEYVHLVCQMKMTGAIRKQLA 4361
Cdd:pfam00632   82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066  4362 AFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKANTEY-HKYQSSSIQIQWFWRALRSFDQADRAKFLQFVTGT 4440
Cdd:pfam00632  160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYdGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688612066  4441 SKVPLQGFAALegmngiQKFQIHR-DDRSTDRLPSAHTCFNQLDLPAYESYEKLRHMLLLAIQECsEGFGLA 4511
Cdd:pfam00632  240 SRLPVGGFKSL------PKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
DUF913 pfam06025
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ...
 431-847 5.87e-102

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


Pssm-ID: 461803  Cd Length: 369  Bit Score: 333.43  E-value: 5.87e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   431 RAVRVVD-LITNLD--MAAFQSHGGLSIFICRLEHEVDLSRKECPFVIKPKIQRPSTATETEdmdtdmdmsevamesspg 507
Cdd:pfam06025    1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALELAEAGKGTPSEYKSSVVDYE------------------ 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   508 pstssgsraetdsraqsnasstpragvqcIP-QRAALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGS-LPTSLKHIISNA 583
Cdd:pfam06025   63 -----------------------------IPyYRQQLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENA 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   584 EYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLTDVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLHSFVQCQPF 663
Cdd:pfam06025  114 KVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAGLSKAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNAL 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   664 ERLFKVLLSPDYLPAMRrrrssdPLGDTASNLGSAVDELMRHQPTLKTDATTAIIKLLEEICNLGRSPEY---ICQKPSI 740
Cdd:pfam06025  194 ESFFEIFESPDHVKAME------TDGELASNLGSSFDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEpdgWGAKLWV 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   741 QKADGTVTVPPARSNHAAEEASSEDEEEEEalHTFSQQQGEPESNRQVVGTEERIPIPLMDYILNVMKFVESILSNNTtd 820
Cdd:pfam06025  268 GCSSSSSFSPASSGSLPMETDGESGDESSS--DEDVEMEDAPDTDSTEETEPESHGNSLTDYIDNVARFLEAFFSNNS-- 343

                          410       420
                   ....*....|....*....|....*..
gi 688612066   821 dHCQEFVNQKGLLPLVSILGLPNLPID 847
Cdd:pfam06025  344 -HCSDFIEKGGIELLLDLATLPSLPYD 369
DUF908 pfam06012
Domain of Unknown Function (DUF908);
90-367 1.59e-24

Domain of Unknown Function (DUF908);


Pssm-ID: 428721  Cd Length: 351  Bit Score: 108.58  E-value: 1.59e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066    90 KALLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASCDMQVVLSVLNLLYVFSKR-SNYITRLGSDKRS---PLLA---- 161
Cdd:pfam06012    3 RELVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLLRLAQRySASNSRRGSAPRHiqqSLLAnhyn 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   162 ----RLQHLAESWG------------------GKENGFGLAECCRDLPmSKYPPSATTLHFEFYAEPSSEVKVEKKSSSN 219
Cdd:pfam06012   83 idldRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKEDS-KVLPSEWGSVKFTYYPSSSSDEAPTSSKSST 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   220 T-----------------------------------------LHYIHIEQLDKISESPSEIMESltAMYNIPKDKQILLF 258
Cdd:pfam06012  162 SsnsspstptplrrsstlgtspdspsspststpssaadsdegLRTFEIPESKVASKSLEDILAK--AIEDLPKESRFELL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   259 THIRLAHGFSNHK--RRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQITDKQLVDIKAASLRTLTSI 334
Cdd:pfam06012  240 HRIRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEAL 319

                          330       340       350
                   ....*....|....*....|....*....|...
gi 688612066   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, ...
 1389-1428 3.87e-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: 3.87e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 688612066 1389 VNQAQLTQLMDMGFSREHAMEALLNTSTMEQATEYLLTHP 1428
Cdd:cd14288     1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP 40
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 1689-1750 3.33e-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: 70.02  E-value: 3.33e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688612066  1689 WRWFDDRsGRWCSYSASNNSTIDSAWRAGETSV--RFTAGRRRYTVQFNTMVQVNEETGNRRPV 1750
Cdd:pfam02825    2 WEWEDDN-GGWHPYDPEVSSLIEEAYQKGKPSVdlSITTAGFPYTIDFKSMTQTNKDTGTTRPV 64
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 1689-1761 3.37e-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: 64.67  E-value: 3.37e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688612066   1689 WRW-FDDRSGRWCSYSASNNSTIDSAWRAGETSVRFTAGRRRYTVQFNTMVQVNEETGNRRPvmltVQRVPRIP 1761
Cdd:smart00678    1 YVWeYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRK----VRRVTYSP 70
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
 3099-3132 1.46e-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: 1.46e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 688612066  3099 GGPGVTEVSPEFLAALPPAIQEEVLAQQRAEQQR 3132
Cdd:pfam14377    1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
 3051-3078 9.68e-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: 47.88  E-value: 9.68e-07
                           10        20
                   ....*....|....*....|....*...
gi 688612066  3051 PEGVDPSFLAALPEDIRREVLQNQLGIR 3078
Cdd:pfam14377    5 PEGIDPSFLAALPPDLRQEVLAQQDDER 32
PHA03247 PHA03247
large tegument protein UL36; Provisional
 2884-3156 7.57e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 7.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 2884 PDSHGALAGAGLPqlSAPDRPNCEAEASQMEMSPAPTIGERGGGALDAVREASLSPDIAESSePVPVGVSQlEGSPMDTS 2963
Cdd:PHA03247 2689 RPTVGSLTSLADP--PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGP-ATPGGPAR-PARPPTTA 2764

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 2964 SPasgtqEEPAASSVPSNHMSQELSGSGDSGLTDRQTDAETGSTSVSSPGETMPRSDSADSQSQAIQEEPLPSTSNEEED 3043
Cdd:PHA03247 2765 GP-----PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP 2839

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 3044 PLAGISLPEGVDPSFLAALPEDIRRevlqnqlgiRPPSRPPVASTLTTTASAVLGGGPGVTEVSPEFLAALP-------- 3115
Cdd:PHA03247 2840 PPPPGPPPPSLPLGGSVAPGGDVRR---------RPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPdqperppq 2910

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 688612066 3116 PAIQEEVLAQQRAEQQRRELSQQPTQG--DQPLDPVTFIQTLP 3156
Cdd:PHA03247 2911 PQAPPPPQPQPQPPPPPQPQPPPPPPPrpQPPLAPTTDPAGAG 2953
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
 1389-1424 3.63e-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: 3.63e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 688612066  1389 VNQAQLTQLMDMGFSREHAMEALLNTST-MEQATEYL 1424
Cdd:pfam00627    1 EDEEAIQRLVEMGFDREQVREALRATGNnVERAAEYL 37
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
 1390-1425 2.03e-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: 2.03e-03
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 688612066   1390 NQAQLTQLMDMGFSREHAMEALLNTSTMEQ-ATEYLL 1425
Cdd:smart00165    1 DEEKIDQLLEMGFSREEALKALRAANGNVErAAEYLL 37
Rev1_UBM2 cd19318
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
 3054-3072 5.78e-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: 5.78e-03
                          10
                  ....*....|....*....
gi 688612066 3054 VDPSFLAALPEDIRREVLQ 3072
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 ...
 4156-4509 9.56e-159

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: 495.93  E-value: 9.56e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4156 VHVRRDHVFEDSYRELHRKSPEDMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSH 4235
Cdd:cd00078     3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4236 CNPNHLSYFKFVGRVVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYPFFQGLVYLLENDVSTLGYELTFSTEV 4315
Cdd:cd00078    83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4316 QE-FGVCEVRDLKANGANILVTEENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTI 4394
Cdd:cd00078   163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4395 DIDDLKANTEY-HKYQSSSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEgmngiQKFQIHRDDRSTDRLP 4473
Cdd:cd00078   243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 688612066 4474 SAHTCFNQLDLPAYESYEKLRHMLLLAIQECsEGFG 4509
Cdd:cd00078   318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
HECTc smart00119
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ...
 4180-4508 6.25e-155

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: 484.04  E-value: 6.25e-155
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   4180 KNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGRVVAKAVYDNR 4259
Cdd:smart00119    4 KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHLSYFRFIGRVLGKALYDNR 83

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   4260 LLECYFTRSFYKHILGKSVRYTDMESEDYPFFQGLVYL-LENDVSTLgYELTFSTEVQE-FGVCEVRDLKANGANILVTE 4337
Cdd:smart00119   84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSIVLTSeFGQVKVVELKPGGSNIPVTE 162

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   4338 ENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKANTEY-HKYQSSSIQIQ 4416
Cdd:smart00119  163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYkGGYSANSQTIK 242

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   4417 WFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGmngiqKFQIHRDDRSTDRLPSAHTCFNQLDLPAYESYEKLRHM 4496
Cdd:smart00119  243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317

                           330
                    ....*....|..
gi 688612066   4497 LLLAIQECsEGF 4508
Cdd:smart00119  318 LLLAINEG-KGF 328
HUL4 COG5021
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
4094-4511 1.40e-145

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


Pssm-ID: 227354 [Multi-domain]  Cd Length: 872  Bit Score: 478.88  E-value: 1.40e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4094 RFAETHRTVLNQILRQSTTHL--ADGPFAVLVDYIRILDFDVKRKYFRQeleRLDEGLRKEDMAVH--VRRDHVFEDSYR 4169
Cdd:COG5021   454 RLNNLYRFYFVEHRKKTLTKNdsRLGSFISLNKLDIRRIKEDKRRKLFY---SLKQKAKIFDPYLHikVRRDRVFEDSYR 530

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4170 ELHRKSPEDMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGR 4249
Cdd:COG5021   531 EIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGR 610

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4250 VVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYPFFQGLVYLLENDVSTLGYELTFSTEVQEFGVCEVRDLKAN 4329
Cdd:COG5021   611 VIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPN 690

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4330 GANILVTEENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPT-IDIDDLKANTEYHKY 4408
Cdd:COG5021   691 GRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGY 770

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 4409 QSSSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGMNGIQKFQIHRDDRSTDRLPSAHTCFNQLDLPAYE 4488
Cdd:COG5021   771 TEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYS 850

                         410       420
                  ....*....|....*....|...
gi 688612066 4489 SYEKLRHMLLLAIQECSeGFGLA 4511
Cdd:COG5021   851 SKEKLRSKLLTAINEGA-GFGLL 872
HECT pfam00632
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ...
 4205-4511 3.95e-117

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


Pssm-ID: 459880  Cd Length: 304  Bit Score: 374.25  E-value: 3.95e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066  4205 IISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNH--LSYFKFVGRVVAKAVYDNRLLECYFTRSFYKHILGKSVRYTD 4282
Cdd:pfam00632    2 LLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066  4283 MESEDYPFFQGLVYLLENDVSTLG-YELTFSteVQEFGVCEVRDLKANGANILVTEENKKEYVHLVCQMKMTGAIRKQLA 4361
Cdd:pfam00632   82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066  4362 AFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKANTEY-HKYQSSSIQIQWFWRALRSFDQADRAKFLQFVTGT 4440
Cdd:pfam00632  160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYdGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688612066  4441 SKVPLQGFAALegmngiQKFQIHR-DDRSTDRLPSAHTCFNQLDLPAYESYEKLRHMLLLAIQECsEGFGLA 4511
Cdd:pfam00632  240 SRLPVGGFKSL------PKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
DUF913 pfam06025
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ...
 431-847 5.87e-102

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


Pssm-ID: 461803  Cd Length: 369  Bit Score: 333.43  E-value: 5.87e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   431 RAVRVVD-LITNLD--MAAFQSHGGLSIFICRLEHEVDLSRKECPFVIKPKIQRPSTATETEdmdtdmdmsevamesspg 507
Cdd:pfam06025    1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALELAEAGKGTPSEYKSSVVDYE------------------ 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   508 pstssgsraetdsraqsnasstpragvqcIP-QRAALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGS-LPTSLKHIISNA 583
Cdd:pfam06025   63 -----------------------------IPyYRQQLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENA 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   584 EYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLTDVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLHSFVQCQPF 663
Cdd:pfam06025  114 KVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAGLSKAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNAL 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   664 ERLFKVLLSPDYLPAMRrrrssdPLGDTASNLGSAVDELMRHQPTLKTDATTAIIKLLEEICNLGRSPEY---ICQKPSI 740
Cdd:pfam06025  194 ESFFEIFESPDHVKAME------TDGELASNLGSSFDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEpdgWGAKLWV 267

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   741 QKADGTVTVPPARSNHAAEEASSEDEEEEEalHTFSQQQGEPESNRQVVGTEERIPIPLMDYILNVMKFVESILSNNTtd 820
Cdd:pfam06025  268 GCSSSSSFSPASSGSLPMETDGESGDESSS--DEDVEMEDAPDTDSTEETEPESHGNSLTDYIDNVARFLEAFFSNNS-- 343

                          410       420
                   ....*....|....*....|....*..
gi 688612066   821 dHCQEFVNQKGLLPLVSILGLPNLPID 847
Cdd:pfam06025  344 -HCSDFIEKGGIELLLDLATLPSLPYD 369
DUF908 pfam06012
Domain of Unknown Function (DUF908);
90-367 1.59e-24

Domain of Unknown Function (DUF908);


Pssm-ID: 428721  Cd Length: 351  Bit Score: 108.58  E-value: 1.59e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066    90 KALLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASCDMQVVLSVLNLLYVFSKR-SNYITRLGSDKRS---PLLA---- 161
Cdd:pfam06012    3 RELVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLLRLAQRySASNSRRGSAPRHiqqSLLAnhyn 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   162 ----RLQHLAESWG------------------GKENGFGLAECCRDLPmSKYPPSATTLHFEFYAEPSSEVKVEKKSSSN 219
Cdd:pfam06012   83 idldRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKEDS-KVLPSEWGSVKFTYYPSSSSDEAPTSSKSST 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   220 T-----------------------------------------LHYIHIEQLDKISESPSEIMESltAMYNIPKDKQILLF 258
Cdd:pfam06012  162 SsnsspstptplrrsstlgtspdspsspststpssaadsdegLRTFEIPESKVASKSLEDILAK--AIEDLPKESRFELL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066   259 THIRLAHGFSNHK--RRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQITDKQLVDIKAASLRTLTSI 334
Cdd:pfam06012  240 HRIRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEAL 319

                          330       340       350
                   ....*....|....*....|....*....|...
gi 688612066   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, ...
 1389-1428 3.87e-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: 3.87e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 688612066 1389 VNQAQLTQLMDMGFSREHAMEALLNTSTMEQATEYLLTHP 1428
Cdd:cd14288     1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP 40
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 1689-1750 3.33e-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: 70.02  E-value: 3.33e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688612066  1689 WRWFDDRsGRWCSYSASNNSTIDSAWRAGETSV--RFTAGRRRYTVQFNTMVQVNEETGNRRPV 1750
Cdd:pfam02825    2 WEWEDDN-GGWHPYDPEVSSLIEEAYQKGKPSVdlSITTAGFPYTIDFKSMTQTNKDTGTTRPV 64
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 1689-1761 3.37e-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: 64.67  E-value: 3.37e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688612066   1689 WRW-FDDRSGRWCSYSASNNSTIDSAWRAGETSVRFTAGRRRYTVQFNTMVQVNEETGNRRPvmltVQRVPRIP 1761
Cdd:smart00678    1 YVWeYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRK----VRRVTYSP 70
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
 3099-3132 1.46e-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: 1.46e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 688612066  3099 GGPGVTEVSPEFLAALPPAIQEEVLAQQRAEQQR 3132
Cdd:pfam14377    1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
UBM pfam14377
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ...
 3051-3078 9.68e-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: 47.88  E-value: 9.68e-07
                           10        20
                   ....*....|....*....|....*...
gi 688612066  3051 PEGVDPSFLAALPEDIRREVLQNQLGIR 3078
Cdd:pfam14377    5 PEGIDPSFLAALPPDLRQEVLAQQDDER 32
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
 1392-1427 1.10e-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: 1.10e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 688612066 1392 AQLTQLMDMGFSREHAMEAL--LNTSTMEQATEYLLTH 1427
Cdd:cd14327     1 EAVAQLVEMGFSRERAEEALraVGTNSVELAMEWLFTN 38
UBA1_atUBP14 cd14295
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
 1390-1427 5.43e-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: 46.21  E-value: 5.43e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 688612066 1390 NQAQLTQLMDMGFSREHAMEALLNTSTM--EQATEYLLTH 1427
Cdd:cd14295     1 DQELVAQLMEMGFPKVRAEKALFFTQNKglEEAMEWLEEH 40
PHA03247 PHA03247
large tegument protein UL36; Provisional
 2884-3156 7.57e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 7.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 2884 PDSHGALAGAGLPqlSAPDRPNCEAEASQMEMSPAPTIGERGGGALDAVREASLSPDIAESSePVPVGVSQlEGSPMDTS 2963
Cdd:PHA03247 2689 RPTVGSLTSLADP--PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGP-ATPGGPAR-PARPPTTA 2764

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 2964 SPasgtqEEPAASSVPSNHMSQELSGSGDSGLTDRQTDAETGSTSVSSPGETMPRSDSADSQSQAIQEEPLPSTSNEEED 3043
Cdd:PHA03247 2765 GP-----PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP 2839

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 3044 PLAGISLPEGVDPSFLAALPEDIRRevlqnqlgiRPPSRPPVASTLTTTASAVLGGGPGVTEVSPEFLAALP-------- 3115
Cdd:PHA03247 2840 PPPPGPPPPSLPLGGSVAPGGDVRR---------RPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPdqperppq 2910

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 688612066 3116 PAIQEEVLAQQRAEQQRRELSQQPTQG--DQPLDPVTFIQTLP 3156
Cdd:PHA03247 2911 PQAPPPPQPQPQPPPPPQPQPPPPPPPrpQPPLAPTTDPAGAG 2953
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
 1391-1427 2.01e-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: 2.01e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 688612066 1391 QAQLTQLMDMGFSREHAMEALLNT--STMEQATEYLLTH 1427
Cdd:cd14296     1 EEAVSQLMSMGFSENAAKRALYYTgnSSVEAAMNWLFEH 39
UBA1_NUB1_like cd14291
UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called ...
 1390-1424 2.25e-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: 2.25e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 688612066 1390 NQAQLTQLMDMGFSREHAMEALLNTS-TMEQATEYL 1424
Cdd:cd14291     1 DEDKLQQLMEMGFSEAEARLALRACNgNVERAVDYI 36
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
 1389-1424 3.63e-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: 3.63e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 688612066  1389 VNQAQLTQLMDMGFSREHAMEALLNTST-MEQATEYL 1424
Cdd:pfam00627    1 EDEEAIQRLVEMGFDREQVREALRATGNnVERAAEYL 37
UBA_TNR6C cd14283
UBA domain found in trinucleotide repeat-containing gene 6C protein (TNRC6C) and similar ...
 1393-1426 4.31e-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: 4.31e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 688612066 1393 QLTQLMDMGFSREHAMEAL-LNTSTMEQATEYLLT 1426
Cdd:cd14283     3 LLKQLTDMGFKREPAEEALkSNNMNLEQAVSALLS 37
UBA2_UBP5 cd14386
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
 1389-1428 1.75e-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: 1.75e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 688612066 1389 VNQAQLTQLMDMGFSREHAMEALLNTS-TMEQATEYLLTHP 1428
Cdd:cd14386     1 VPEEAVAMLVSMGFTRDQAIKALKATDnNVERAADWIFSHP 41
UBA cd14270
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ...
 1394-1422 2.59e-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: 2.59e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 688612066 1394 LTQLMDMGFSREHAMEALLNTS-TMEQATE 1422
Cdd:cd14270     1 LAQLVEMGFSREQARRALRATNgDVEAAVE 30
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
 1386-1428 3.20e-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: 3.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 688612066 1386 EPQVNQaqltqLMDMGFSREHAMEALLNT-STMEQATEYLLTHP 1428
Cdd:cd14297     1 EDLVKQ-----LVDMGFTEAQARKALRKTnNNVERAVDWLFEGP 39
PHA03247 PHA03247
large tegument protein UL36; Provisional
 2807-3104 4.15e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 2807 TVNGAAENAAEGEQAQSGVSSCLDPPRTSEGFLTAPPSGEVTPTTPAPHEQALVSLETAisqqvhqpiTELLLADSNPDS 2886
Cdd:PHA03247 2736 PAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSES---------RESLPSPWDPAD 2806

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 2887 HGALAGAGLPQLSAPDRPNceaeasqmEMSPAPTigergggaldAVREASLSPDIAESSEPVPVGVSQLEGSPMDTSSPA 2966
Cdd:PHA03247 2807 PPAAVLAPAAALPPAASPA--------GPLPPPT----------SAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPS 2868

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 2967 SGTQEEPAASS-VPSNHMSQ-ELSGSGDSGLTDRQTDAETGSTSVSSPGETMPRSDSADSQSQAIQEEPLPSTSNEEEDP 3044
Cdd:PHA03247 2869 RSPAAKPAAPArPPVRRLARpAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTD 2948

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688612066 3045 LAGISLPEGVDPSFLAALPEDIRREVLQNQLGIRPPSRP-PVASTLTTTASAVlgggPGVT 3104
Cdd:PHA03247 2949 PAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREaPASSTPPLTGHSL----SRVS 3005
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
 1394-1427 5.55e-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: 5.55e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 688612066 1394 LTQLMDMGFSREHAMEALLNTS-TMEQATEYLLTH 1427
Cdd:cd14306     1 VAKLMELGFPEEDCIRALRACGgNVEEAANWLLEN 35
UBA_UBXN1 cd14302
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ...
 1394-1427 8.22e-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: 8.22e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 688612066 1394 LTQLMDMGFSREHAMEALLNTST--MEQATEYLLTH 1427
Cdd:cd14302     3 LQTLIEMGFSRNRAEKALAKTGNqgVEAAMEWLLAH 38
UBA1_KPC2 cd14303
UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
 1389-1427 1.41e-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: 39.30  E-value: 1.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 688612066 1389 VNQAQLTQLMDMGFSREHAMEAL-LNTSTMEQATEYLLTH 1427
Cdd:cd14303     1 VDPEALKQLTEMGFPEARATKALlLNRMSPTQAMEWLLEH 40
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
 1390-1425 2.03e-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: 2.03e-03
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 688612066   1390 NQAQLTQLMDMGFSREHAMEALLNTSTMEQ-ATEYLL 1425
Cdd:smart00165    1 DEEKIDQLLEMGFSREEALKALRAANGNVErAAEYLL 37
UBA_UBAC2 cd14305
UBA domain found in ubiquitin-associated domain-containing protein 2 (UBAC2) and similar ...
 1389-1425 3.11e-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: 3.11e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 688612066 1389 VNQAQLTQLMDMGFSREHAMEALL--NTSTMEqATEYLL 1425
Cdd:cd14305     1 PSEEQVQQLVDMGFSREDVLEALRqsNNDVNA-ATNLLL 38
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 2840-3117 4.13e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 2840 TAPPSGEVTPTTPAPHEQALVSLETAISQQVHQPITELLLADSNPDSHG----ALAGAGLPQLSAPDRPNCEAEASQMEM 2915
Cdd:PHA03307  160 AAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRrsspISASASSPAPAPGRSAADDAGASSSDS 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 2916 SPAP----TIGERGGGALDAVREASLSPDIAESSEPVPvgvsqlEGSPMDTSSPASGTQEE-----------PAASSVPS 2980
Cdd:PHA03307  240 SSSEssgcGWGPENECPLPRPAPITLPTRIWEASGWNG------PSSRPGPASSSSSPRERspspspsspgsGPAPSSPR 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 2981 NHMSQELSGSGDSGLTDRQTDAETGSTSVSSPGETMPRSDSADSQSQAiqeePLPSTSNEEEDPLAGISLPEGVDPSFLA 3060
Cdd:PHA03307  314 ASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPAD----PSSPRKRPRPSRAPSSPAASAGRPTRRR 389

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688612066 3061 ALPEDIRREVLQNQLGIRPPSRPP-VASTLTTTASAVLGGGPGVT---EVSPEflAALPPA 3117
Cdd:PHA03307  390 ARAAVAGRARRRDATGRFPAGRPRpSPLDAGAASGAFYARYPLLTpsgEPWPG--SPPPPP 448
UBA2_UBP13 cd14387
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ...
 1396-1424 4.62e-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: 4.62e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 688612066 1396 QLMDMGFSREHAMEALLNT-STMEQATEYL 1424
Cdd:cd14387     6 ILMSMGFPRNRAIEALKRTnNNLDRALDWL 35
Rev1_UBM2 cd19318
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ...
 3054-3072 5.78e-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: 5.78e-03
                          10
                  ....*....|....*....
gi 688612066 3054 VDPSFLAALPEDIRREVLQ 3072
Cdd:cd19318    12 VDPSVLAALPPDLQEELEA 30
UBA2_KPC2 cd14304
UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
 1390-1425 6.28e-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: 6.28e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 688612066 1390 NQAQLTQLMDMGFSREHAMEAL-LNTSTMEQATEYLL 1425
Cdd:cd14304     2 NPRAVQSLMEMGFEEEDVLEALrVTRNNQNAACEWLL 38
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
2884-3147 9.92e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.14  E-value: 9.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 2884 PDSHGALAGAGLPQLSAPD--RPNCEAEASQMEMSPAPTIGERGGGALDAVREASLSPDIAESSEPVPVGVSQLE----- 2956
Cdd:PRK07003  360 PAVTGGGAPGGGVPARVAGavPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPAtadrg 439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 2957 GSPMDTSSPASGTQEEPAASSvpsnhmSQELSGSGDSGLTDRQTDAETGSTSVSSPGETMPRSDSADSQSQAIQEEPLPS 3036
Cdd:PRK07003  440 DDAADGDAPVPAKANARASAD------SRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAP 513

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688612066 3037 TSNEEEDPLAGISLPEGVDPSFLAALPEDIRR--------EVLQNQlGIR--------------PPSRPPVASTLTTTAS 3094
Cdd:PRK07003  514 AAASREDAPAAAAPPAPEARPPTPAAAAPAARaggaaaalDVLRNA-GMRvssdrgaraaaaakPAAAPAAAPKPAAPRV 592

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 688612066 3095 AVLGGGPGvtevspeflaALPPAIQEEVLAQQRAEQQRRELSQQPTQGDQPLD 3147
Cdd:PRK07003  593 AVQVPTPR----------ARAATGDAPPNGAARAEQAAESRGAPPPWEDIPPD 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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