|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
4100-4453 |
4.26e-161 |
|
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: 502.48 E-value: 4.26e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4100 VHVRRDHVFEDSYRELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSH 4179
Cdd:cd00078 3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4180 CNPNHLSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEV 4259
Cdd:cd00078 83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4260 QE-FGVCEVRDLKPNGANILVTEENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTI 4338
Cdd:cd00078 163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4339 DIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEgmngiQKFQIHRDDRSTDRLP 4417
Cdd:cd00078 243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 1622968668 4418 SAHTCFNQLDLPAYESFEKLRHMLLLAIQECsEGFG 4453
Cdd:cd00078 318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
|
|
| DUF913 |
pfam06025 |
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ... |
431-895 |
5.32e-96 |
|
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin protein ligases. :
Pssm-ID: 461803 Cd Length: 369 Bit Score: 316.48 E-value: 5.32e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 431 RAVRVVD-LITNLD--MAAFQSHSGLSIFIYRLEHEVDLCRKECpfvikpkiqrpsttQEGEEMETDMdvadvamessPG 507
Cdd:pfam06025 1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALELA--------------EAGKGTPSEY----------KS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 508 SSISMEhrldvelrasgsssstnissgpspgpspgpgpgpgpgpgpgpgpgpgpgpgpgpgpgpgpgprpgaqcIP-QRA 586
Cdd:pfam06025 57 SVVDYE--------------------------------------------------------------------IPyYRQ 68
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 587 ALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGS-LPTSLKHIISNAEYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLT 663
Cdd:pfam06025 69 QLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENAKVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAGLS 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 664 DVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLQSFVQCQPFERLFKVLLSPDYLPAMRrrrssdPLGDTASNLGSA 743
Cdd:pfam06025 149 KAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNALESFFEIFESPDHVKAME------TDGELASNLGSS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 744 VDELMRHQPTLKTDATTAIIKLLEEICNLGRDPKY---ICQKPSIQKADGTATAPPPRSNHAAEEASSEDEEEEEVQ--A 818
Cdd:pfam06025 223 FDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEpdgWGAKLWVGCSSSSSFSPASSGSLPMETDGESGDESSSDEdvE 302
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622968668 819 MQSFNSTQQNESEPNqqvvgteERIPIPLMDYILNVMKFVESILSNNTtddHCQEFVNQKGLLPLVTILGLPNLPID 895
Cdd:pfam06025 303 MEDAPDTDSTEETEP-------ESHGNSLTDYIDNVARFLEAFFSNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
|
|
| DUF908 super family |
cl20318 |
Domain of Unknown Function (DUF908); |
92-367 |
7.12e-24 |
|
Domain of Unknown Function (DUF908); The actual alignment was detected with superfamily member pfam06012:
Pssm-ID: 428721 Cd Length: 351 Bit Score: 106.65 E-value: 7.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 92 LLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASSDMQVVLAVLNLLYVFSKR-SNYITRLGSDKRTP-----------L 159
Cdd:pfam06012 5 LVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLLRLAQRySASNSRRGSAPRHIqqsllanhyniD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 160 LTRLQHLAESWG------------------GKENGFGLAECCRDLHmmKYPPS-ATTLHFEFYADPGAEVKIEK------ 214
Cdd:pfam06012 85 LDRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKEDS--KVLPSeWGSVKFTYYPSSSSDEAPTSskssts 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 215 -----------------------------------RTTSNTLHYIHIEQLDKISESPSEIMESLtkMYSIPKDKQMLLFT 259
Cdd:pfam06012 163 snsspstptplrrsstlgtspdspsspststpssaADSDEGLRTFEIPESKVASKSLEDILAKA--IEDLPKESRFELLH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 260 HIRLAHGFSNHR--KRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQITDKQLMEIKAASLRTLTSIV 335
Cdd:pfam06012 241 RIRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEALA 320
|
330 340 350
....*....|....*....|....*....|..
gi 1622968668 336 HleRTPKLSSIIDCTGTASYHGFLPVLVRNCI 367
Cdd:pfam06012 321 R--HRAKLSDVLSALGANVNHGILLYVLRKAV 350
|
|
| UBA_HUWE1 |
cd14288 |
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ... |
1398-1437 |
6.18e-15 |
|
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: 71.28 E-value: 6.18e-15
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1622968668 1398 VNQQQLQQLMDMGFTREHAMEALLNTSTMEQATEYLLTHP 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 |
4.54e-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: 69.63 E-value: 4.54e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622968668 1698 WRWFDDRsGRWCSYSASNNSTIDSAWKSGETSV--RFTAGRRRYTVQFTTMVQVNEETGNRRPV 1759
Cdd:pfam02825 2 WEWEDDN-GGWHPYDPEVSSLIEEAYQKGKPSVdlSITTAGFPYTIDFKSMTQTNKDTGTTRPV 64
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
3091-3124 |
1.07e-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: 50.58 E-value: 1.07e-07
10 20 30
....*....|....*....|....*....|....
gi 1622968668 3091 GNPGVTEVSPEFLAALPPAIQEEVLAQQRAEQQR 3124
Cdd:pfam14377 1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
3046-3073 |
2.16e-06 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM). :
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 46.73 E-value: 2.16e-06
10 20
....*....|....*....|....*...
gi 1622968668 3046 PEGVDPSFLAALPDDIRREVLQNQLGIR 3073
Cdd:pfam14377 5 PEGIDPSFLAALPPDLRQEVLAQQDDER 32
|
|
| Herpes_BLLF1 super family |
cl37540 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
2803-3039 |
3.03e-06 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo. The actual alignment was detected with superfamily member pfam05109:
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 53.77 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2803 TASKTNDSTEQNLSDGTPMPDSYPTTPSSTDAATSESKETLGTlQSSQQQPTLPTPPALGEVPQeLQSPAGEGGSSTqll 2882
Cdd:pfam05109 499 TESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGK-TSPTSAVTTPTPNATSPTPA-VTTPTPNATIPT--- 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2883 mpvepeeLGPTRPSgEAETTQMELSPAPTITSLSPERAEDSDALTAVSSqlegSPMDTSSLASCTLEEAVGDASATGSSe 2962
Cdd:pfam05109 574 -------LGKTSPT-SAVTTPTPNATSPTVGETSPQANTTNHTLGGTSS----TPVVTSPPKNATSAVTTGQHNITSSS- 640
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622968668 2963 qpragSSTPGDAPPAVAEVQGRSDGSGESAQPPEDSSPPASSESSSTRDSAVAISGADSRGILEEPLPSTSSEEEDP 3039
Cdd:pfam05109 641 -----TSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGP 712
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
4100-4453 |
4.26e-161 |
|
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: 502.48 E-value: 4.26e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4100 VHVRRDHVFEDSYRELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSH 4179
Cdd:cd00078 3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4180 CNPNHLSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEV 4259
Cdd:cd00078 83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4260 QE-FGVCEVRDLKPNGANILVTEENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTI 4338
Cdd:cd00078 163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4339 DIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEgmngiQKFQIHRDDRSTDRLP 4417
Cdd:cd00078 243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 1622968668 4418 SAHTCFNQLDLPAYESFEKLRHMLLLAIQECsEGFG 4453
Cdd:cd00078 318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
4124-4452 |
3.73e-159 |
|
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: 495.99 E-value: 3.73e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4124 KNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGRIVAKAVYDNR 4203
Cdd:smart00119 4 KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHLSYFRFIGRVLGKALYDNR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4204 LLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYL-LENDVSTLgYDLTFSTEVQE-FGVCEVRDLKPNGANILVTE 4281
Cdd:smart00119 84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSIVLTSeFGQVKVVELKPGGSNIPVTE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4282 ENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKSNTEY-HKYQSNSIQIQ 4360
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYkGGYSANSQTIK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4361 WFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGmngiqKFQIHRDDRSTDRLPSAHTCFNQLDLPAYESFEKLRHM 4440
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317
|
330
....*....|..
gi 1622968668 4441 LLLAIQECsEGF 4452
Cdd:smart00119 318 LLLAINEG-KGF 328
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
4038-4455 |
4.87e-147 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 483.11 E-value: 4.87e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4038 RFAETHRTVLNQILRQSTTHL--ADGPFAVLVDYIRVLDFDVKRKYFRQeleRLDEGLRKEDMAVH--VRRDHVFEDSYR 4113
Cdd:COG5021 454 RLNNLYRFYFVEHRKKTLTKNdsRLGSFISLNKLDIRRIKEDKRRKLFY---SLKQKAKIFDPYLHikVRRDRVFEDSYR 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4114 ELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGR 4193
Cdd:COG5021 531 EIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGR 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4194 IVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEVQEFGVCEVRDLKPN 4273
Cdd:COG5021 611 VIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPN 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4274 GANILVTEENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPT-IDIDDLKSNTEYHKY 4352
Cdd:COG5021 691 GRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGY 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4353 QSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGMNGIQKFQIHRDDRSTDRLPSAHTCFNQLDLPAYE 4432
Cdd:COG5021 771 TEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYS 850
|
410 420
....*....|....*....|...
gi 1622968668 4433 SFEKLRHMLLLAIQECSeGFGLA 4455
Cdd:COG5021 851 SKEKLRSKLLTAINEGA-GFGLL 872
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
4149-4455 |
2.06e-120 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 383.88 E-value: 2.06e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4149 IISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNH--LSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTD 4226
Cdd:pfam00632 2 LLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4227 MESEDYHFYQGLVYLLENDVSTLG-YDLTFSteVQEFGVCEVRDLKPNGANILVTEENKKEYVHLVCQMRMTGAIRKQLA 4305
Cdd:pfam00632 82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4306 AFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGT 4384
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYdGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622968668 4385 SKVPLQGFAALegmngiQKFQIHR-DDRSTDRLPSAHTCFNQLDLPAYESFEKLRHMLLLAIQECsEGFGLA 4455
Cdd:pfam00632 240 SRLPVGGFKSL------PKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
|
|
| DUF913 |
pfam06025 |
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ... |
431-895 |
5.32e-96 |
|
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin protein ligases.
Pssm-ID: 461803 Cd Length: 369 Bit Score: 316.48 E-value: 5.32e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 431 RAVRVVD-LITNLD--MAAFQSHSGLSIFIYRLEHEVDLCRKECpfvikpkiqrpsttQEGEEMETDMdvadvamessPG 507
Cdd:pfam06025 1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALELA--------------EAGKGTPSEY----------KS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 508 SSISMEhrldvelrasgsssstnissgpspgpspgpgpgpgpgpgpgpgpgpgpgpgpgpgpgpgpgprpgaqcIP-QRA 586
Cdd:pfam06025 57 SVVDYE--------------------------------------------------------------------IPyYRQ 68
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 587 ALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGS-LPTSLKHIISNAEYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLT 663
Cdd:pfam06025 69 QLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENAKVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAGLS 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 664 DVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLQSFVQCQPFERLFKVLLSPDYLPAMRrrrssdPLGDTASNLGSA 743
Cdd:pfam06025 149 KAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNALESFFEIFESPDHVKAME------TDGELASNLGSS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 744 VDELMRHQPTLKTDATTAIIKLLEEICNLGRDPKY---ICQKPSIQKADGTATAPPPRSNHAAEEASSEDEEEEEVQ--A 818
Cdd:pfam06025 223 FDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEpdgWGAKLWVGCSSSSSFSPASSGSLPMETDGESGDESSSDEdvE 302
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622968668 819 MQSFNSTQQNESEPNqqvvgteERIPIPLMDYILNVMKFVESILSNNTtddHCQEFVNQKGLLPLVTILGLPNLPID 895
Cdd:pfam06025 303 MEDAPDTDSTEETEP-------ESHGNSLTDYIDNVARFLEAFFSNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
|
|
| DUF908 |
pfam06012 |
Domain of Unknown Function (DUF908); |
92-367 |
7.12e-24 |
|
Domain of Unknown Function (DUF908);
Pssm-ID: 428721 Cd Length: 351 Bit Score: 106.65 E-value: 7.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 92 LLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASSDMQVVLAVLNLLYVFSKR-SNYITRLGSDKRTP-----------L 159
Cdd:pfam06012 5 LVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLLRLAQRySASNSRRGSAPRHIqqsllanhyniD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 160 LTRLQHLAESWG------------------GKENGFGLAECCRDLHmmKYPPS-ATTLHFEFYADPGAEVKIEK------ 214
Cdd:pfam06012 85 LDRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKEDS--KVLPSeWGSVKFTYYPSSSSDEAPTSskssts 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 215 -----------------------------------RTTSNTLHYIHIEQLDKISESPSEIMESLtkMYSIPKDKQMLLFT 259
Cdd:pfam06012 163 snsspstptplrrsstlgtspdspsspststpssaADSDEGLRTFEIPESKVASKSLEDILAKA--IEDLPKESRFELLH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 260 HIRLAHGFSNHR--KRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQITDKQLMEIKAASLRTLTSIV 335
Cdd:pfam06012 241 RIRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEALA 320
|
330 340 350
....*....|....*....|....*....|..
gi 1622968668 336 HleRTPKLSSIIDCTGTASYHGFLPVLVRNCI 367
Cdd:pfam06012 321 R--HRAKLSDVLSALGANVNHGILLYVLRKAV 350
|
|
| UBA_HUWE1 |
cd14288 |
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ... |
1398-1437 |
6.18e-15 |
|
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: 71.28 E-value: 6.18e-15
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1622968668 1398 VNQQQLQQLMDMGFTREHAMEALLNTSTMEQATEYLLTHP 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 |
4.54e-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: 69.63 E-value: 4.54e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622968668 1698 WRWFDDRsGRWCSYSASNNSTIDSAWKSGETSV--RFTAGRRRYTVQFTTMVQVNEETGNRRPV 1759
Cdd:pfam02825 2 WEWEDDN-GGWHPYDPEVSSLIEEAYQKGKPSVdlSITTAGFPYTIDFKSMTQTNKDTGTTRPV 64
|
|
| WWE |
smart00678 |
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ... |
1698-1759 |
9.64e-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: 63.13 E-value: 9.64e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622968668 1698 WRW-FDDRSGRWCSYSASNNSTIDSAWKSGETSVRFTAGRRRYTVQFTTMVQVNEETGNRRPV 1759
Cdd:smart00678 1 YVWeYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKV 63
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
3091-3124 |
1.07e-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: 50.58 E-value: 1.07e-07
10 20 30
....*....|....*....|....*....|....
gi 1622968668 3091 GNPGVTEVSPEFLAALPPAIQEEVLAQQRAEQQR 3124
Cdd:pfam14377 1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
3046-3073 |
2.16e-06 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 46.73 E-value: 2.16e-06
10 20
....*....|....*....|....*...
gi 1622968668 3046 PEGVDPSFLAALPDDIRREVLQNQLGIR 3073
Cdd:pfam14377 5 PEGIDPSFLAALPPDLRQEVLAQQDDER 32
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
2803-3039 |
3.03e-06 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 53.77 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2803 TASKTNDSTEQNLSDGTPMPDSYPTTPSSTDAATSESKETLGTlQSSQQQPTLPTPPALGEVPQeLQSPAGEGGSSTqll 2882
Cdd:pfam05109 499 TESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGK-TSPTSAVTTPTPNATSPTPA-VTTPTPNATIPT--- 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2883 mpvepeeLGPTRPSgEAETTQMELSPAPTITSLSPERAEDSDALTAVSSqlegSPMDTSSLASCTLEEAVGDASATGSSe 2962
Cdd:pfam05109 574 -------LGKTSPT-SAVTTPTPNATSPTVGETSPQANTTNHTLGGTSS----TPVVTSPPKNATSAVTTGQHNITSSS- 640
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622968668 2963 qpragSSTPGDAPPAVAEVQGRSDGSGESAQPPEDSSPPASSESSSTRDSAVAISGADSRGILEEPLPSTSSEEEDP 3039
Cdd:pfam05109 641 -----TSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGP 712
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
2816-3110 |
1.39e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 51.71 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2816 SDGTPMPDSYPTTPSSTDAATSESK------ETLGTLQSSQQQPTLPTPPAlGEVPQELQSPAGEGGSSTQLL-MPVE-- 2886
Cdd:PHA03307 105 SPTPPGPSSPDPPPPTPPPASPPPSpapdlsEMLRPVGSPGPPPAASPPAA-GASPAAVASDAASSRQAALPLsSPEEta 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2887 ------PEELGPTRPSGEAETT-----------QMELSPAPTITSLSPERAEDSDALTAVSSQLEGSPMDTSSLASCTLE 2949
Cdd:PHA03307 184 rapsspPAEPPPSTPPAAASPRpprrsspisasASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPI 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2950 EAVG--DASATGSSEQPRAGSSTPGDAPPAVAEVQGRSDGSGESAQPPEDSSPPASsessstRDSAVAISGADSRGILEE 3027
Cdd:PHA03307 264 TLPTriWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSS------SSRESSSSSTSSSSESSR 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 3028 PLPSTSSEEEDPLAGISLPEGV-DPSFLAALPDDIRREVLQNQLGIRPPTRTApstnssAPAVVGNPGVTEVSPEFLAAL 3106
Cdd:PHA03307 338 GAAVSPGPSPSRSPSPSRPPPPaDPSSPRKRPRPSRAPSSPAASAGRPTRRRA------RAAVAGRARRRDATGRFPAGR 411
|
....
gi 1622968668 3107 PPAI 3110
Cdd:PHA03307 412 PRPS 415
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
3049-3067 |
9.71e-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: 36.43 E-value: 9.71e-03
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
4100-4453 |
4.26e-161 |
|
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: 502.48 E-value: 4.26e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4100 VHVRRDHVFEDSYRELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSH 4179
Cdd:cd00078 3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4180 CNPNHLSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEV 4259
Cdd:cd00078 83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4260 QE-FGVCEVRDLKPNGANILVTEENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTI 4338
Cdd:cd00078 163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4339 DIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEgmngiQKFQIHRDDRSTDRLP 4417
Cdd:cd00078 243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 1622968668 4418 SAHTCFNQLDLPAYESFEKLRHMLLLAIQECsEGFG 4453
Cdd:cd00078 318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
4124-4452 |
3.73e-159 |
|
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: 495.99 E-value: 3.73e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4124 KNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGRIVAKAVYDNR 4203
Cdd:smart00119 4 KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHLSYFRFIGRVLGKALYDNR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4204 LLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYL-LENDVSTLgYDLTFSTEVQE-FGVCEVRDLKPNGANILVTE 4281
Cdd:smart00119 84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSIVLTSeFGQVKVVELKPGGSNIPVTE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4282 ENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKSNTEY-HKYQSNSIQIQ 4360
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYkGGYSANSQTIK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4361 WFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGmngiqKFQIHRDDRSTDRLPSAHTCFNQLDLPAYESFEKLRHM 4440
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317
|
330
....*....|..
gi 1622968668 4441 LLLAIQECsEGF 4452
Cdd:smart00119 318 LLLAINEG-KGF 328
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
4038-4455 |
4.87e-147 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 483.11 E-value: 4.87e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4038 RFAETHRTVLNQILRQSTTHL--ADGPFAVLVDYIRVLDFDVKRKYFRQeleRLDEGLRKEDMAVH--VRRDHVFEDSYR 4113
Cdd:COG5021 454 RLNNLYRFYFVEHRKKTLTKNdsRLGSFISLNKLDIRRIKEDKRRKLFY---SLKQKAKIFDPYLHikVRRDRVFEDSYR 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4114 ELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGR 4193
Cdd:COG5021 531 EIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGR 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4194 IVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEVQEFGVCEVRDLKPN 4273
Cdd:COG5021 611 VIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPN 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4274 GANILVTEENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPT-IDIDDLKSNTEYHKY 4352
Cdd:COG5021 691 GRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGY 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4353 QSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGMNGIQKFQIHRDDRSTDRLPSAHTCFNQLDLPAYE 4432
Cdd:COG5021 771 TEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYS 850
|
410 420
....*....|....*....|...
gi 1622968668 4433 SFEKLRHMLLLAIQECSeGFGLA 4455
Cdd:COG5021 851 SKEKLRSKLLTAINEGA-GFGLL 872
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
4149-4455 |
2.06e-120 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 383.88 E-value: 2.06e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4149 IISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNH--LSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTD 4226
Cdd:pfam00632 2 LLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4227 MESEDYHFYQGLVYLLENDVSTLG-YDLTFSteVQEFGVCEVRDLKPNGANILVTEENKKEYVHLVCQMRMTGAIRKQLA 4305
Cdd:pfam00632 82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 4306 AFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGT 4384
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYdGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622968668 4385 SKVPLQGFAALegmngiQKFQIHR-DDRSTDRLPSAHTCFNQLDLPAYESFEKLRHMLLLAIQECsEGFGLA 4455
Cdd:pfam00632 240 SRLPVGGFKSL------PKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
|
|
| DUF913 |
pfam06025 |
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ... |
431-895 |
5.32e-96 |
|
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin protein ligases.
Pssm-ID: 461803 Cd Length: 369 Bit Score: 316.48 E-value: 5.32e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 431 RAVRVVD-LITNLD--MAAFQSHSGLSIFIYRLEHEVDLCRKECpfvikpkiqrpsttQEGEEMETDMdvadvamessPG 507
Cdd:pfam06025 1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALELA--------------EAGKGTPSEY----------KS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 508 SSISMEhrldvelrasgsssstnissgpspgpspgpgpgpgpgpgpgpgpgpgpgpgpgpgpgpgpgprpgaqcIP-QRA 586
Cdd:pfam06025 57 SVVDYE--------------------------------------------------------------------IPyYRQ 68
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 587 ALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGS-LPTSLKHIISNAEYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLT 663
Cdd:pfam06025 69 QLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENAKVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAGLS 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 664 DVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLQSFVQCQPFERLFKVLLSPDYLPAMRrrrssdPLGDTASNLGSA 743
Cdd:pfam06025 149 KAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNALESFFEIFESPDHVKAME------TDGELASNLGSS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 744 VDELMRHQPTLKTDATTAIIKLLEEICNLGRDPKY---ICQKPSIQKADGTATAPPPRSNHAAEEASSEDEEEEEVQ--A 818
Cdd:pfam06025 223 FDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEpdgWGAKLWVGCSSSSSFSPASSGSLPMETDGESGDESSSDEdvE 302
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622968668 819 MQSFNSTQQNESEPNqqvvgteERIPIPLMDYILNVMKFVESILSNNTtddHCQEFVNQKGLLPLVTILGLPNLPID 895
Cdd:pfam06025 303 MEDAPDTDSTEETEP-------ESHGNSLTDYIDNVARFLEAFFSNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
|
|
| DUF908 |
pfam06012 |
Domain of Unknown Function (DUF908); |
92-367 |
7.12e-24 |
|
Domain of Unknown Function (DUF908);
Pssm-ID: 428721 Cd Length: 351 Bit Score: 106.65 E-value: 7.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 92 LLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASSDMQVVLAVLNLLYVFSKR-SNYITRLGSDKRTP-----------L 159
Cdd:pfam06012 5 LVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLLRLAQRySASNSRRGSAPRHIqqsllanhyniD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 160 LTRLQHLAESWG------------------GKENGFGLAECCRDLHmmKYPPS-ATTLHFEFYADPGAEVKIEK------ 214
Cdd:pfam06012 85 LDRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKEDS--KVLPSeWGSVKFTYYPSSSSDEAPTSskssts 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 215 -----------------------------------RTTSNTLHYIHIEQLDKISESPSEIMESLtkMYSIPKDKQMLLFT 259
Cdd:pfam06012 163 snsspstptplrrsstlgtspdspsspststpssaADSDEGLRTFEIPESKVASKSLEDILAKA--IEDLPKESRFELLH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 260 HIRLAHGFSNHR--KRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQITDKQLMEIKAASLRTLTSIV 335
Cdd:pfam06012 241 RIRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEALA 320
|
330 340 350
....*....|....*....|....*....|..
gi 1622968668 336 HleRTPKLSSIIDCTGTASYHGFLPVLVRNCI 367
Cdd:pfam06012 321 R--HRAKLSDVLSALGANVNHGILLYVLRKAV 350
|
|
| UBA_HUWE1 |
cd14288 |
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ... |
1398-1437 |
6.18e-15 |
|
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: 71.28 E-value: 6.18e-15
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1622968668 1398 VNQQQLQQLMDMGFTREHAMEALLNTSTMEQATEYLLTHP 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 |
4.54e-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: 69.63 E-value: 4.54e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622968668 1698 WRWFDDRsGRWCSYSASNNSTIDSAWKSGETSV--RFTAGRRRYTVQFTTMVQVNEETGNRRPV 1759
Cdd:pfam02825 2 WEWEDDN-GGWHPYDPEVSSLIEEAYQKGKPSVdlSITTAGFPYTIDFKSMTQTNKDTGTTRPV 64
|
|
| WWE |
smart00678 |
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ... |
1698-1759 |
9.64e-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: 63.13 E-value: 9.64e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622968668 1698 WRW-FDDRSGRWCSYSASNNSTIDSAWKSGETSVRFTAGRRRYTVQFTTMVQVNEETGNRRPV 1759
Cdd:smart00678 1 YVWeYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKV 63
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
3091-3124 |
1.07e-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: 50.58 E-value: 1.07e-07
10 20 30
....*....|....*....|....*....|....
gi 1622968668 3091 GNPGVTEVSPEFLAALPPAIQEEVLAQQRAEQQR 3124
Cdd:pfam14377 1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
3046-3073 |
2.16e-06 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 46.73 E-value: 2.16e-06
10 20
....*....|....*....|....*...
gi 1622968668 3046 PEGVDPSFLAALPDDIRREVLQNQLGIR 3073
Cdd:pfam14377 5 PEGIDPSFLAALPPDLRQEVLAQQDDER 32
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
2803-3039 |
3.03e-06 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 53.77 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2803 TASKTNDSTEQNLSDGTPMPDSYPTTPSSTDAATSESKETLGTlQSSQQQPTLPTPPALGEVPQeLQSPAGEGGSSTqll 2882
Cdd:pfam05109 499 TESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGK-TSPTSAVTTPTPNATSPTPA-VTTPTPNATIPT--- 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2883 mpvepeeLGPTRPSgEAETTQMELSPAPTITSLSPERAEDSDALTAVSSqlegSPMDTSSLASCTLEEAVGDASATGSSe 2962
Cdd:pfam05109 574 -------LGKTSPT-SAVTTPTPNATSPTVGETSPQANTTNHTLGGTSS----TPVVTSPPKNATSAVTTGQHNITSSS- 640
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622968668 2963 qpragSSTPGDAPPAVAEVQGRSDGSGESAQPPEDSSPPASSESSSTRDSAVAISGADSRGILEEPLPSTSSEEEDP 3039
Cdd:pfam05109 641 -----TSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGP 712
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
2816-3110 |
1.39e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 51.71 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2816 SDGTPMPDSYPTTPSSTDAATSESK------ETLGTLQSSQQQPTLPTPPAlGEVPQELQSPAGEGGSSTQLL-MPVE-- 2886
Cdd:PHA03307 105 SPTPPGPSSPDPPPPTPPPASPPPSpapdlsEMLRPVGSPGPPPAASPPAA-GASPAAVASDAASSRQAALPLsSPEEta 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2887 ------PEELGPTRPSGEAETT-----------QMELSPAPTITSLSPERAEDSDALTAVSSQLEGSPMDTSSLASCTLE 2949
Cdd:PHA03307 184 rapsspPAEPPPSTPPAAASPRpprrsspisasASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPI 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2950 EAVG--DASATGSSEQPRAGSSTPGDAPPAVAEVQGRSDGSGESAQPPEDSSPPASsessstRDSAVAISGADSRGILEE 3027
Cdd:PHA03307 264 TLPTriWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSS------SSRESSSSSTSSSSESSR 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 3028 PLPSTSSEEEDPLAGISLPEGV-DPSFLAALPDDIRREVLQNQLGIRPPTRTApstnssAPAVVGNPGVTEVSPEFLAAL 3106
Cdd:PHA03307 338 GAAVSPGPSPSRSPSPSRPPPPaDPSSPRKRPRPSRAPSSPAASAGRPTRRRA------RAAVAGRARRRDATGRFPAGR 411
|
....
gi 1622968668 3107 PPAI 3110
Cdd:PHA03307 412 PRPS 415
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
2803-3109 |
1.49e-05 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 51.46 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2803 TASKTNDSTEQNLSDGTPMPDSYPTTPSSTDAATSESKETLGtLQSSQQQPT-LPTPPALGEV--PQELQSPAGEGGSST 2879
Cdd:pfam05109 406 TRTATNATTTTHKVIFSKAPESTTTSPTLNTTGFAAPNTTTG-LPSSTHVPTnLTAPASTGPTvsTADVTSPTPAGTTSG 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2880 QllMPVEP---------EELGP--TRPSGEAET-TQMELSPAPTITSLSPERAEDSDALTAVSSQLEG-SPMDTSSLASC 2946
Cdd:pfam05109 485 A--SPVTPspsprdngtESKAPdmTSPTSAVTTpTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTpTPNATSPTPAV 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2947 TLEE------AVGDASATG--SSEQPRAGSSTPGDAPPAVAEVQGRSDGSGES---AQPPEDSSPPASSESSSTRDSAVA 3015
Cdd:pfam05109 563 TTPTpnatipTLGKTSPTSavTTPTPNATSPTVGETSPQANTTNHTLGGTSSTpvvTSPPKNATSAVTTGQHNITSSSTS 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 3016 ISGADSRGILEEPLPSTS--SEEEDPLAGISLPEGVDPSFLAALPDDIRREVLQNQLGIRPPTRTAPS--TNSSAPAVVG 3091
Cdd:pfam05109 643 SMSLRPSSISETLSPSTSdnSTSHMPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASgpGNSSTSTKPG 722
|
330
....*....|....*...
gi 1622968668 3092 NPGVTEVSPEFLAALPPA 3109
Cdd:pfam05109 723 EVNVTKGTPPKNATSPQA 740
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2816-3147 |
1.60e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.48 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2816 SDGTPMPDSYPTTPSSTDAAtSESKETLGTLQSSQQQPTLPTPPALGEVPQELQSPAGeggSSTQLLMPVEPEELGPTRP 2895
Cdd:PHA03247 2637 EPDPHPPPTVPPPERPRDDP-APGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVG---SLTSLADPPPPPPTPEPAP 2712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2896 SGEAETTQMELSPAPTITSLSPERAEDSDALTAVSSQLEGSPMDTSSLASctleeavgdASATGSSEQPRAgsstPGDAP 2975
Cdd:PHA03247 2713 HALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPT---------TAGPPAPAPPAA----PAAGP 2779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2976 PAVAEVQGRSDGSGESAQPPEDSSPPASSESSSTRDSAVAISGADSRGileEPLPSTSSEEEDPLAGISLPEGVDPSFLA 3055
Cdd:PHA03247 2780 PRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP---LPPPTSAQPTAPPPPPGPPPPSLPLGGSV 2856
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 3056 ALPDDIRREVLQNQLGIRPPTRTAPSTNS-SAPAVVGNPGVTEVSPEFLAALP-PAIQEEVLAQQRAEQQRRE---LAQN 3130
Cdd:PHA03247 2857 APGGDVRRRPPSRSPAAKPAAPARPPVRRlARPAVSRSTESFALPPDQPERPPqPQAPPPPQPQPQPPPPPQPqppPPPP 2936
|
330
....*....|....*..
gi 1622968668 3131 ASSDTPMDPVTFIQTLP 3147
Cdd:PHA03247 2937 PRPQPPLAPTTDPAGAG 2953
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2822-3207 |
5.67e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.94 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2822 PDSYPTTPSSTDAATSESKETLGTLQSSQQQPTLPTPPALGEVPQELQSPAGEG-----------GSSTQLLMPVEPEEL 2890
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPArparppttagpPAPAPPAAPAAGPPR 2781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2891 GPTRPSGEAETTQMELSPAPTITSLSPERAED-SDALTAVSSQLEGSPMDTSSL------------ASCTLEEAV---GD 2954
Cdd:PHA03247 2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLApAAALPPAASPAGPLPPPTSAQptapppppgpppPSLPLGGSVapgGD 2861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2955 ASATGSSEQPRAGSSTPGDaPPAVAEVQGRSDGSGESAQPPEDSSPPASSESSSTRDSAVAISGADSRgilEEPLPSTSS 3034
Cdd:PHA03247 2862 VRRRPPSRSPAAKPAAPAR-PPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ---PQPPPPPPP 2937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 3035 EEEDPL------AGISLPEGVDPSFLAALPDDIRREVLQNQLGIRPPTRTAPSTNSSAPAVVGNPGVTEVSpeflaalpp 3108
Cdd:PHA03247 2938 RPQPPLapttdpAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWA--------- 3008
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 3109 aiqeevlaqqraeqqrRELAQNASSDTPmdPVTFIQTL-PSD---------LRRSVLEDMEDSVLAVMPPD----IAAEA 3174
Cdd:PHA03247 3009 ----------------SSLALHEETDPP--PVSLKQTLwPPDdtedsdadsLFDSDSERSDLEALDPLPPEphdpFAHEP 3070
|
410 420 430
....*....|....*....|....*....|...
gi 1622968668 3175 QALRREQEARQRQLMHerlFGHSSTSALSAILR 3207
Cdd:PHA03247 3071 DPATPEAGARESPSSQ---FGPPPLSANAALSR 3100
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
2852-3074 |
1.29e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 48.44 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2852 QPTLPTPPALGEVPQELQSPAGeggsstqllmPVEPEELGPTRPSGEAeTTQMELSPAPTITSLSPERAEDSDALTAVSS 2931
Cdd:PRK07764 596 GGEGPPAPASSGPPEEAARPAA----------PAAPAAPAAPAPAGAA-AAPAEASAAPAPGVAAPEHHPKHVAVPDASD 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2932 QLEGSPMDTSSLASCTLEEA------VGDASATGSSEQPR-------AGSSTPGDAPPAVAEVQGRSDGSGESAQPPEDS 2998
Cdd:PRK07764 665 GGDGWPAKAGGAAPAAPPPApapaapAAPAGAAPAQPAPApaatppaGQADDPAAQPPQAAQGASAPSPAADDPVPLPPE 744
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622968668 2999 SPPASSESSSTRDSAVAISGADSRGILEEPLPSTSSEEEDPLAgiSLPEGVDPSFLAAlPDDIRREVLQNQLGIRP 3074
Cdd:PRK07764 745 PDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAE--DDAPSMDDEDRRD-AEEVAMELLEEELGAKK 817
|
|
| UBA_atUPL1_2_like |
cd14327 |
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ... |
1407-1436 |
2.60e-04 |
|
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: 41.13 E-value: 2.60e-04
10 20 30
....*....|....*....|....*....|..
gi 1622968668 1407 MDMGFTREHAMEAL--LNTSTMEQATEYLLTH 1436
Cdd:cd14327 7 VEMGFSRERAEEALraVGTNSVELAMEWLFTN 38
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2816-3140 |
5.22e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.47 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2816 SDGTPMPDSyPTTPSS------TDAATSESK-----------ETLGTLQSSQQQPTLP--TPPALGE----VPQELQSPA 2872
Cdd:PHA03247 2500 GGGPPDPDA-PPAPSRlapailPDEPVGEPVhprmltwirglEELASDDAGDPPPPLPpaAPPAAPDrsvpPPRPAPRPS 2578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2873 GEGGSSTQLLMPVEPEELGPTRPSGEAETTQMELSPAPTITSLSPERAEDSDALTAVSSQLEGSPMDTSSLASCTLEEAV 2952
Cdd:PHA03247 2579 EPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAP 2658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2953 GDAS----ATGSSEQPRAGSST----PGDAPPAVAEVQgrsdgsgESAQPPEDSSPPASSESSSTrdSAVAISGADSRGI 3024
Cdd:PHA03247 2659 GRVSrprrARRLGRAAQASSPPqrprRRAARPTVGSLT-------SLADPPPPPPTPEPAPHALV--SATPLPPGPAAAR 2729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 3025 LEEPLPSTSSEEEDPLAGISLPEGVDPSFLAALPDDIRREVL-QNQLGIRPPTRTAPSTNSSAPAVVGNPGVTEVSPEFL 3103
Cdd:PHA03247 2730 QASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPpAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPA 2809
|
330 340 350
....*....|....*....|....*....|....*..
gi 1622968668 3104 AALPPAIQEEVLAQQRAEQQRRELAQNASSDTPMDPV 3140
Cdd:PHA03247 2810 AVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPP 2846
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
2858-3131 |
1.39e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 44.84 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2858 PPALGEVPQELQSPAGEGGSSTQLLMPVEPEELGPTRPSGEAETTQMELSPAPTITS---LSPERAEDSDAltAVSSQLE 2934
Cdd:PRK07003 368 PGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEappAAPAPPATADR--GDDAADG 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2935 GSPMDTSSLASCTLEEAVGDASATGSSeQPRAGSSTPGDAPPAVA-EVQGRSDGSGESAQPPEDSSPPASsessstrdsa 3013
Cdd:PRK07003 446 DAPVPAKANARASADSRCDERDAQPPA-DSGSASAPASDAPPDAAfEPAPRAAAPSAATPAAVPDARAPA---------- 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 3014 vAISGADSRGILEEPLPSTSSEEedPLAGISLPEGVDPSflAALpddirrEVLQNQlGIRpptrtAPSTNSSAPAVVGNP 3093
Cdd:PRK07003 515 -AASREDAPAAAAPPAPEARPPT--PAAAAPAARAGGAA--AAL------DVLRNA-GMR-----VSSDRGARAAAAAKP 577
|
250 260 270
....*....|....*....|....*....|....*....
gi 1622968668 3094 GVTEVSPEFLAALPPAIQEEVL-AQQRAEQQRRELAQNA 3131
Cdd:PRK07003 578 AAAPAAAPKPAAPRVAVQVPTPrARAATGDAPPNGAARA 616
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
2871-3129 |
4.79e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 43.33 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2871 PAGEGGSStqllmpvepeelGPTRPSGEAETTQMELSPAPTITSLSPERAEDSDALTAVSSQLEGSPMDTSSLASCTLEE 2950
Cdd:PRK12323 365 PGQSGGGA------------GPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2951 AvgdASATGSSEQPRAGSSTPGDAPPAVAEVQGRSdgSGESAQPPEDSSPPASSESSSTRDSAVAISGADSRGILEEPLP 3030
Cdd:PRK12323 433 L---AAARQASARGPGGAPAPAPAPAAAPAAAARP--AAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 3031 STSSEEEDP-LAGISLPEGVDPSflAALPDDIRREVLQNQLGIRPPTRTAPSTNSSA--PAVVGNPGVTEVS----PEFL 3103
Cdd:PRK12323 508 SPAPAQPDAaPAGWVAESIPDPA--TADPDDAFETLAPAPAAAPAPRAAAATEPVVAprPPRASASGLPDMFdgdwPALA 585
|
250 260
....*....|....*....|....*.
gi 1622968668 3104 AALPPaiqeEVLAQQRAEQQrrELAQ 3129
Cdd:PRK12323 586 ARLPV----RGLAQQLARQS--ELAG 605
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
2791-3100 |
8.99e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.47 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2791 EDKENRDQSAQCTASKTNDSTEQNLSDGTPMpdsypTTPSSTDAATSESKETLGTlQSSQQQPTLPTP-PALGEVPQELQ 2869
Cdd:PHA03307 12 EAAAEGGEFFPRPPATPGDAADDLLSGSQGQ-----LVSDSAELAAVTVVAGAAA-CDRFEPPTGPPPgPGTEAPANESR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2870 SPAGEGGSSTQLLMPVEPEELGPTRPSGEAETTQME--LSPAPtitSLSPERAEDSDALTAVSSQLEGSPMDTSSLASCT 2947
Cdd:PHA03307 86 STPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPppASPPP---SPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2948 ---LEEAVGDASATGSSEQPRAGSSTPGDAPPavaevqGRSDGSGESAQPPEdsspPASSESSSTRDSAVAISGADSRGI 3024
Cdd:PHA03307 163 asdAASSRQAALPLSSPEETARAPSSPPAEPP------PSTPPAAASPRPPR----RSSPISASASSPAPAPGRSAADDA 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622968668 3025 LEEPLPSTSSEEEDPLAGISLPEGVDPSFLAALPDDIRREVLQNQLGIRP-PTRTAPSTNSSAPAVV-GNPGVTEVSP 3100
Cdd:PHA03307 233 GASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPgPASSSSSPRERSPSPSpSSPGSGPAPS 310
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
2816-3046 |
9.38e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.47 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2816 SDGTPMP---DSYPTTPSSTDAATSESKETLGTLQSSQQQP-----TLPTPPALGEVPQELQSPAGEGGSSTQllmpvEP 2887
Cdd:PHA03307 218 SSPAPAPgrsAADDAGASSSDSSSSESSGCGWGPENECPLPrpapiTLPTRIWEASGWNGPSSRPGPASSSSS-----PR 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2888 EELGPTRPSGEAETtqmELSPAPTITSLSPERAEDSDALTAVSSQLEGSPMDTSSLASCTL-----EEAVGDASATGSSE 2962
Cdd:PHA03307 293 ERSPSPSPSSPGSG---PAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSpspsrPPPPADPSSPRKRP 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968668 2963 QPRAGSSTPGDAPP---------AVAEVQGRSDGSGESAQPPedssppassesssTRDSAVAISGADSRGILEEPLPSTS 3033
Cdd:PHA03307 370 RPSRAPSSPAASAGrptrrraraAVAGRARRRDATGRFPAGR-------------PRPSPLDAGAASGAFYARYPLLTPS 436
|
250
....*....|...
gi 1622968668 3034 SEeedPLAGISLP 3046
Cdd:PHA03307 437 GE---PWPGSPPP 446
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
3049-3067 |
9.71e-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: 36.43 E-value: 9.71e-03
|
|