|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
3966-4319 |
4.13e-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: 4.13e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 3966 VHVRRDHVFEDSYRELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSH 4045
Cdd:cd00078 3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4046 CNPNHLSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEV 4125
Cdd:cd00078 83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4126 QE-FGVCEVRDLKPNGANILVTEENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTI 4204
Cdd:cd00078 163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4205 DIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEgmngiQKFQIHRDDRSTDRLP 4283
Cdd:cd00078 243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 1622968700 4284 SAHTCFNQLDLPAYESFEKLRHMLLLAIQECsEGFG 4319
Cdd:cd00078 318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
|
|
| DUF913 |
pfam06025 |
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ... |
431-895 |
3.78e-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: 316.86 E-value: 3.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 431 RAVRVVD-LITNLD--MAAFQSHSGLSIFIYRLEHEVDLCRKECpfvikpkiqrpsttQEGEEMETDMdvadvamessPG 507
Cdd:pfam06025 1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALELA--------------EAGKGTPSEY----------KS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 508 SSISMEhrldvelrasgsssstnissgpspgpspgpgpgpgpgpgpgpgpgpgpgpgpgpgpgpgpgprpgaqcIP-QRA 586
Cdd:pfam06025 57 SVVDYE--------------------------------------------------------------------IPyYRQ 68
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 587 ALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGS-LPTSLKHIISNAEYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLT 663
Cdd:pfam06025 69 QLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENAKVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAGLS 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 664 DVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLQSFVQCQPFERLFKVLLSPDYLPAMRrrrssdPLGDTASNLGSA 743
Cdd:pfam06025 149 KAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNALESFFEIFESPDHVKAME------TDGELASNLGSS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 744 VDELMRHQPTLKTDATTAIIKLLEEICNLGRDPKY---ICQKPSIQKADGTATAPPPRSNHAAEEASSEDEEEEEVQ--A 818
Cdd:pfam06025 223 FDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEpdgWGAKLWVGCSSSSSFSPASSGSLPMETDGESGDESSSDEdvE 302
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622968700 819 MQSFNSTQQNESEPNqqvvgteERIPIPLMDYILNVMKFVESILSNNTtddHCQEFVNQKGLLPLVTILGLPNLPID 895
Cdd:pfam06025 303 MEDAPDTDSTEETEP-------ESHGNSLTDYIDNVARFLEAFFSNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
|
|
| DUF908 super family |
cl20318 |
Domain of Unknown Function (DUF908); |
92-367 |
6.83e-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: 6.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 92 LLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASSDMQVVLAVLNLLYVFSKR-SNYITRLGSDKRTP-----------L 159
Cdd:pfam06012 5 LVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLLRLAQRySASNSRRGSAPRHIqqsllanhyniD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 160 LTRLQHLAESWG------------------GKENGFGLAECCRDLHmmKYPPS-ATTLHFEFYADPGAEVKIEK------ 214
Cdd:pfam06012 85 LDRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKEDS--KVLPSeWGSVKFTYYPSSSSDEAPTSskssts 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 215 -----------------------------------RTTSNTLHYIHIEQLDKISESPSEIMESLtkMYSIPKDKQMLLFT 259
Cdd:pfam06012 163 snsspstptplrrsstlgtspdspsspststpssaADSDEGLRTFEIPESKVASKSLEDILAKA--IEDLPKESRFELLH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 260 HIRLAHGFSNHR--KRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQITDKQLMEIKAASLRTLTSIV 335
Cdd:pfam06012 241 RIRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEALA 320
|
330 340 350
....*....|....*....|....*....|..
gi 1622968700 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 |
5.49e-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: 5.49e-15
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1622968700 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 |
4.40e-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: 4.40e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622968700 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 ... |
2957-2990 |
8.84e-08 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM). :
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 50.58 E-value: 8.84e-08
10 20 30
....*....|....*....|....*....|....
gi 1622968700 2957 GNPGVTEVSPEFLAALPPAIQEEVLAQQRAEQQR 2990
Cdd:pfam14377 1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
2912-2939 |
1.81e-06 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM). :
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 47.11 E-value: 1.81e-06
10 20
....*....|....*....|....*...
gi 1622968700 2912 PEGVDPSFLAALPDDIRREVLQNQLGIR 2939
Cdd:pfam14377 5 PEGIDPSFLAALPPDLRQEVLAQQDDER 32
|
|
| Herpes_BLLF1 super family |
cl37540 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
2669-2905 |
2.93e-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: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2669 TASKTNDSTEQNLSDGTPMPDSYPTTPSSTDAATSESKETLGTlQSSQQQPTLPTPPALGEVPQeLQSPAGEGGSSTqll 2748
Cdd:pfam05109 499 TESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGK-TSPTSAVTTPTPNATSPTPA-VTTPTPNATIPT--- 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2749 mpvepeeLGPTRPSgEAETTQMELSPAPTITSLSPERAEDSDALTAVSSqlegSPMDTSSLASCTLEEAVGDASATGSSe 2828
Cdd:pfam05109 574 -------LGKTSPT-SAVTTPTPNATSPTVGETSPQANTTNHTLGGTSS----TPVVTSPPKNATSAVTTGQHNITSSS- 640
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622968700 2829 qpragSSTPGDAPPAVAEVQGRSDGSGESAQPPEDSSPPASSESSSTRDSAVAISGADSRGILEEPLPSTSSEEEDP 2905
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 ... |
3966-4319 |
4.13e-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: 4.13e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 3966 VHVRRDHVFEDSYRELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSH 4045
Cdd:cd00078 3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4046 CNPNHLSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEV 4125
Cdd:cd00078 83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4126 QE-FGVCEVRDLKPNGANILVTEENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTI 4204
Cdd:cd00078 163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4205 DIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEgmngiQKFQIHRDDRSTDRLP 4283
Cdd:cd00078 243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 1622968700 4284 SAHTCFNQLDLPAYESFEKLRHMLLLAIQECsEGFG 4319
Cdd:cd00078 318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
3990-4318 |
3.62e-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: 3.62e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 3990 KNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGRIVAKAVYDNR 4069
Cdd:smart00119 4 KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHLSYFRFIGRVLGKALYDNR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4070 LLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYL-LENDVSTLgYDLTFSTEVQE-FGVCEVRDLKPNGANILVTE 4147
Cdd:smart00119 84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSIVLTSeFGQVKVVELKPGGSNIPVTE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4148 ENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKSNTEY-HKYQSNSIQIQ 4226
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYkGGYSANSQTIK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4227 WFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGmngiqKFQIHRDDRSTDRLPSAHTCFNQLDLPAYESFEKLRHM 4306
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317
|
330
....*....|..
gi 1622968700 4307 LLLAIQECsEGF 4318
Cdd:smart00119 318 LLLAINEG-KGF 328
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
3904-4321 |
1.92e-147 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 484.27 E-value: 1.92e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 3904 RFAETHRTVLNQILRQSTTHL--ADGPFAVLVDYIRVLDFDVKRKYFRQeleRLDEGLRKEDMAVH--VRRDHVFEDSYR 3979
Cdd:COG5021 454 RLNNLYRFYFVEHRKKTLTKNdsRLGSFISLNKLDIRRIKEDKRRKLFY---SLKQKAKIFDPYLHikVRRDRVFEDSYR 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 3980 ELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGR 4059
Cdd:COG5021 531 EIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGR 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4060 IVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEVQEFGVCEVRDLKPN 4139
Cdd:COG5021 611 VIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPN 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4140 GANILVTEENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPT-IDIDDLKSNTEYHKY 4218
Cdd:COG5021 691 GRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGY 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4219 QSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGMNGIQKFQIHRDDRSTDRLPSAHTCFNQLDLPAYE 4298
Cdd:COG5021 771 TEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYS 850
|
410 420
....*....|....*....|...
gi 1622968700 4299 SFEKLRHMLLLAIQECSeGFGLA 4321
Cdd:COG5021 851 SKEKLRSKLLTAINEGA-GFGLL 872
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
4015-4321 |
2.00e-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: 2.00e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4015 IISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNH--LSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTD 4092
Cdd:pfam00632 2 LLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4093 MESEDYHFYQGLVYLLENDVSTLG-YDLTFSteVQEFGVCEVRDLKPNGANILVTEENKKEYVHLVCQMRMTGAIRKQLA 4171
Cdd:pfam00632 82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4172 AFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGT 4250
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYdGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622968700 4251 SKVPLQGFAALegmngiQKFQIHR-DDRSTDRLPSAHTCFNQLDLPAYESFEKLRHMLLLAIQECsEGFGLA 4321
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 |
3.78e-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: 316.86 E-value: 3.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 431 RAVRVVD-LITNLD--MAAFQSHSGLSIFIYRLEHEVDLCRKECpfvikpkiqrpsttQEGEEMETDMdvadvamessPG 507
Cdd:pfam06025 1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALELA--------------EAGKGTPSEY----------KS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 508 SSISMEhrldvelrasgsssstnissgpspgpspgpgpgpgpgpgpgpgpgpgpgpgpgpgpgpgpgprpgaqcIP-QRA 586
Cdd:pfam06025 57 SVVDYE--------------------------------------------------------------------IPyYRQ 68
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 587 ALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGS-LPTSLKHIISNAEYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLT 663
Cdd:pfam06025 69 QLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENAKVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAGLS 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 664 DVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLQSFVQCQPFERLFKVLLSPDYLPAMRrrrssdPLGDTASNLGSA 743
Cdd:pfam06025 149 KAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNALESFFEIFESPDHVKAME------TDGELASNLGSS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 744 VDELMRHQPTLKTDATTAIIKLLEEICNLGRDPKY---ICQKPSIQKADGTATAPPPRSNHAAEEASSEDEEEEEVQ--A 818
Cdd:pfam06025 223 FDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEpdgWGAKLWVGCSSSSSFSPASSGSLPMETDGESGDESSSDEdvE 302
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622968700 819 MQSFNSTQQNESEPNqqvvgteERIPIPLMDYILNVMKFVESILSNNTtddHCQEFVNQKGLLPLVTILGLPNLPID 895
Cdd:pfam06025 303 MEDAPDTDSTEETEP-------ESHGNSLTDYIDNVARFLEAFFSNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
|
|
| DUF908 |
pfam06012 |
Domain of Unknown Function (DUF908); |
92-367 |
6.83e-24 |
|
Domain of Unknown Function (DUF908);
Pssm-ID: 428721 Cd Length: 351 Bit Score: 106.65 E-value: 6.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 92 LLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASSDMQVVLAVLNLLYVFSKR-SNYITRLGSDKRTP-----------L 159
Cdd:pfam06012 5 LVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLLRLAQRySASNSRRGSAPRHIqqsllanhyniD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 160 LTRLQHLAESWG------------------GKENGFGLAECCRDLHmmKYPPS-ATTLHFEFYADPGAEVKIEK------ 214
Cdd:pfam06012 85 LDRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKEDS--KVLPSeWGSVKFTYYPSSSSDEAPTSskssts 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 215 -----------------------------------RTTSNTLHYIHIEQLDKISESPSEIMESLtkMYSIPKDKQMLLFT 259
Cdd:pfam06012 163 snsspstptplrrsstlgtspdspsspststpssaADSDEGLRTFEIPESKVASKSLEDILAKA--IEDLPKESRFELLH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 260 HIRLAHGFSNHR--KRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQITDKQLMEIKAASLRTLTSIV 335
Cdd:pfam06012 241 RIRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEALA 320
|
330 340 350
....*....|....*....|....*....|..
gi 1622968700 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 |
5.49e-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: 5.49e-15
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1622968700 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 |
4.40e-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: 4.40e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622968700 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 |
9.35e-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: 9.35e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622968700 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 ... |
2957-2990 |
8.84e-08 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 50.58 E-value: 8.84e-08
10 20 30
....*....|....*....|....*....|....
gi 1622968700 2957 GNPGVTEVSPEFLAALPPAIQEEVLAQQRAEQQR 2990
Cdd:pfam14377 1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
2912-2939 |
1.81e-06 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 47.11 E-value: 1.81e-06
10 20
....*....|....*....|....*...
gi 1622968700 2912 PEGVDPSFLAALPDDIRREVLQNQLGIR 2939
Cdd:pfam14377 5 PEGIDPSFLAALPPDLRQEVLAQQDDER 32
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
2669-2905 |
2.93e-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: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2669 TASKTNDSTEQNLSDGTPMPDSYPTTPSSTDAATSESKETLGTlQSSQQQPTLPTPPALGEVPQeLQSPAGEGGSSTqll 2748
Cdd:pfam05109 499 TESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGK-TSPTSAVTTPTPNATSPTPA-VTTPTPNATIPT--- 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2749 mpvepeeLGPTRPSgEAETTQMELSPAPTITSLSPERAEDSDALTAVSSqlegSPMDTSSLASCTLEEAVGDASATGSSe 2828
Cdd:pfam05109 574 -------LGKTSPT-SAVTTPTPNATSPTVGETSPQANTTNHTLGGTSS----TPVVTSPPKNATSAVTTGQHNITSSS- 640
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622968700 2829 qpragSSTPGDAPPAVAEVQGRSDGSGESAQPPEDSSPPASSESSSTRDSAVAISGADSRGILEEPLPSTSSEEEDP 2905
Cdd:pfam05109 641 -----TSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGP 712
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
2682-2976 |
1.34e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 51.71 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2682 SDGTPMPDSYPTTPSSTDAATSESK------ETLGTLQSSQQQPTLPTPPAlGEVPQELQSPAGEGGSSTQLL-MPVE-- 2752
Cdd:PHA03307 105 SPTPPGPSSPDPPPPTPPPASPPPSpapdlsEMLRPVGSPGPPPAASPPAA-GASPAAVASDAASSRQAALPLsSPEEta 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2753 ------PEELGPTRPSGEAETT-----------QMELSPAPTITSLSPERAEDSDALTAVSSQLEGSPMDTSSLASCTLE 2815
Cdd:PHA03307 184 rapsspPAEPPPSTPPAAASPRpprrsspisasASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPI 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2816 EAVG--DASATGSSEQPRAGSSTPGDAPPAVAEVQGRSDGSGESAQPPEDSSPPASsessstRDSAVAISGADSRGILEE 2893
Cdd:PHA03307 264 TLPTriWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSS------SSRESSSSSTSSSSESSR 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2894 PLPSTSSEEEDPLAGISLPEGV-DPSFLAALPDDIRREVLQNQLGIRPPTRTApstnssAPAVVGNPGVTEVSPEFLAAL 2972
Cdd:PHA03307 338 GAAVSPGPSPSRSPSPSRPPPPaDPSSPRKRPRPSRAPSSPAASAGRPTRRRA------RAAVAGRARRRDATGRFPAGR 411
|
....
gi 1622968700 2973 PPAI 2976
Cdd:PHA03307 412 PRPS 415
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
2915-2933 |
8.80e-03 |
|
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen.
Pssm-ID: 412037 Cd Length: 36 Bit Score: 36.82 E-value: 8.80e-03
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
3966-4319 |
4.13e-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: 4.13e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 3966 VHVRRDHVFEDSYRELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSH 4045
Cdd:cd00078 3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4046 CNPNHLSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEV 4125
Cdd:cd00078 83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4126 QE-FGVCEVRDLKPNGANILVTEENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTI 4204
Cdd:cd00078 163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4205 DIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEgmngiQKFQIHRDDRSTDRLP 4283
Cdd:cd00078 243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 1622968700 4284 SAHTCFNQLDLPAYESFEKLRHMLLLAIQECsEGFG 4319
Cdd:cd00078 318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
3990-4318 |
3.62e-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: 3.62e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 3990 KNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGRIVAKAVYDNR 4069
Cdd:smart00119 4 KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHLSYFRFIGRVLGKALYDNR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4070 LLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYL-LENDVSTLgYDLTFSTEVQE-FGVCEVRDLKPNGANILVTE 4147
Cdd:smart00119 84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSIVLTSeFGQVKVVELKPGGSNIPVTE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4148 ENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKSNTEY-HKYQSNSIQIQ 4226
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYkGGYSANSQTIK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4227 WFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGmngiqKFQIHRDDRSTDRLPSAHTCFNQLDLPAYESFEKLRHM 4306
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317
|
330
....*....|..
gi 1622968700 4307 LLLAIQECsEGF 4318
Cdd:smart00119 318 LLLAINEG-KGF 328
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
3904-4321 |
1.92e-147 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 484.27 E-value: 1.92e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 3904 RFAETHRTVLNQILRQSTTHL--ADGPFAVLVDYIRVLDFDVKRKYFRQeleRLDEGLRKEDMAVH--VRRDHVFEDSYR 3979
Cdd:COG5021 454 RLNNLYRFYFVEHRKKTLTKNdsRLGSFISLNKLDIRRIKEDKRRKLFY---SLKQKAKIFDPYLHikVRRDRVFEDSYR 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 3980 ELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGR 4059
Cdd:COG5021 531 EIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGR 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4060 IVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEVQEFGVCEVRDLKPN 4139
Cdd:COG5021 611 VIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPN 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4140 GANILVTEENKKEYVHLVCQMRMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPT-IDIDDLKSNTEYHKY 4218
Cdd:COG5021 691 GRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGY 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4219 QSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGMNGIQKFQIHRDDRSTDRLPSAHTCFNQLDLPAYE 4298
Cdd:COG5021 771 TEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYS 850
|
410 420
....*....|....*....|...
gi 1622968700 4299 SFEKLRHMLLLAIQECSeGFGLA 4321
Cdd:COG5021 851 SKEKLRSKLLTAINEGA-GFGLL 872
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
4015-4321 |
2.00e-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: 2.00e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4015 IISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNH--LSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTD 4092
Cdd:pfam00632 2 LLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4093 MESEDYHFYQGLVYLLENDVSTLG-YDLTFSteVQEFGVCEVRDLKPNGANILVTEENKKEYVHLVCQMRMTGAIRKQLA 4171
Cdd:pfam00632 82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 4172 AFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGT 4250
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYdGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622968700 4251 SKVPLQGFAALegmngiQKFQIHR-DDRSTDRLPSAHTCFNQLDLPAYESFEKLRHMLLLAIQECsEGFGLA 4321
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 |
3.78e-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: 316.86 E-value: 3.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 431 RAVRVVD-LITNLD--MAAFQSHSGLSIFIYRLEHEVDLCRKECpfvikpkiqrpsttQEGEEMETDMdvadvamessPG 507
Cdd:pfam06025 1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALELA--------------EAGKGTPSEY----------KS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 508 SSISMEhrldvelrasgsssstnissgpspgpspgpgpgpgpgpgpgpgpgpgpgpgpgpgpgpgpgprpgaqcIP-QRA 586
Cdd:pfam06025 57 SVVDYE--------------------------------------------------------------------IPyYRQ 68
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 587 ALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGS-LPTSLKHIISNAEYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLT 663
Cdd:pfam06025 69 QLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENAKVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAGLS 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 664 DVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLQSFVQCQPFERLFKVLLSPDYLPAMRrrrssdPLGDTASNLGSA 743
Cdd:pfam06025 149 KAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNALESFFEIFESPDHVKAME------TDGELASNLGSS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 744 VDELMRHQPTLKTDATTAIIKLLEEICNLGRDPKY---ICQKPSIQKADGTATAPPPRSNHAAEEASSEDEEEEEVQ--A 818
Cdd:pfam06025 223 FDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEpdgWGAKLWVGCSSSSSFSPASSGSLPMETDGESGDESSSDEdvE 302
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622968700 819 MQSFNSTQQNESEPNqqvvgteERIPIPLMDYILNVMKFVESILSNNTtddHCQEFVNQKGLLPLVTILGLPNLPID 895
Cdd:pfam06025 303 MEDAPDTDSTEETEP-------ESHGNSLTDYIDNVARFLEAFFSNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
|
|
| DUF908 |
pfam06012 |
Domain of Unknown Function (DUF908); |
92-367 |
6.83e-24 |
|
Domain of Unknown Function (DUF908);
Pssm-ID: 428721 Cd Length: 351 Bit Score: 106.65 E-value: 6.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 92 LLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASSDMQVVLAVLNLLYVFSKR-SNYITRLGSDKRTP-----------L 159
Cdd:pfam06012 5 LVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLLRLAQRySASNSRRGSAPRHIqqsllanhyniD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 160 LTRLQHLAESWG------------------GKENGFGLAECCRDLHmmKYPPS-ATTLHFEFYADPGAEVKIEK------ 214
Cdd:pfam06012 85 LDRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKEDS--KVLPSeWGSVKFTYYPSSSSDEAPTSskssts 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 215 -----------------------------------RTTSNTLHYIHIEQLDKISESPSEIMESLtkMYSIPKDKQMLLFT 259
Cdd:pfam06012 163 snsspstptplrrsstlgtspdspsspststpssaADSDEGLRTFEIPESKVASKSLEDILAKA--IEDLPKESRFELLH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 260 HIRLAHGFSNHR--KRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQITDKQLMEIKAASLRTLTSIV 335
Cdd:pfam06012 241 RIRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEALA 320
|
330 340 350
....*....|....*....|....*....|..
gi 1622968700 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 |
5.49e-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: 5.49e-15
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1622968700 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 |
4.40e-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: 4.40e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622968700 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 |
9.35e-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: 9.35e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622968700 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 ... |
2957-2990 |
8.84e-08 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 50.58 E-value: 8.84e-08
10 20 30
....*....|....*....|....*....|....
gi 1622968700 2957 GNPGVTEVSPEFLAALPPAIQEEVLAQQRAEQQR 2990
Cdd:pfam14377 1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
2912-2939 |
1.81e-06 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 47.11 E-value: 1.81e-06
10 20
....*....|....*....|....*...
gi 1622968700 2912 PEGVDPSFLAALPDDIRREVLQNQLGIR 2939
Cdd:pfam14377 5 PEGIDPSFLAALPPDLRQEVLAQQDDER 32
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
2669-2905 |
2.93e-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: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2669 TASKTNDSTEQNLSDGTPMPDSYPTTPSSTDAATSESKETLGTlQSSQQQPTLPTPPALGEVPQeLQSPAGEGGSSTqll 2748
Cdd:pfam05109 499 TESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGK-TSPTSAVTTPTPNATSPTPA-VTTPTPNATIPT--- 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2749 mpvepeeLGPTRPSgEAETTQMELSPAPTITSLSPERAEDSDALTAVSSqlegSPMDTSSLASCTLEEAVGDASATGSSe 2828
Cdd:pfam05109 574 -------LGKTSPT-SAVTTPTPNATSPTVGETSPQANTTNHTLGGTSS----TPVVTSPPKNATSAVTTGQHNITSSS- 640
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622968700 2829 qpragSSTPGDAPPAVAEVQGRSDGSGESAQPPEDSSPPASSESSSTRDSAVAISGADSRGILEEPLPSTSSEEEDP 2905
Cdd:pfam05109 641 -----TSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGP 712
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
2682-2976 |
1.34e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 51.71 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2682 SDGTPMPDSYPTTPSSTDAATSESK------ETLGTLQSSQQQPTLPTPPAlGEVPQELQSPAGEGGSSTQLL-MPVE-- 2752
Cdd:PHA03307 105 SPTPPGPSSPDPPPPTPPPASPPPSpapdlsEMLRPVGSPGPPPAASPPAA-GASPAAVASDAASSRQAALPLsSPEEta 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2753 ------PEELGPTRPSGEAETT-----------QMELSPAPTITSLSPERAEDSDALTAVSSQLEGSPMDTSSLASCTLE 2815
Cdd:PHA03307 184 rapsspPAEPPPSTPPAAASPRpprrsspisasASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPI 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2816 EAVG--DASATGSSEQPRAGSSTPGDAPPAVAEVQGRSDGSGESAQPPEDSSPPASsessstRDSAVAISGADSRGILEE 2893
Cdd:PHA03307 264 TLPTriWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSS------SSRESSSSSTSSSSESSR 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2894 PLPSTSSEEEDPLAGISLPEGV-DPSFLAALPDDIRREVLQNQLGIRPPTRTApstnssAPAVVGNPGVTEVSPEFLAAL 2972
Cdd:PHA03307 338 GAAVSPGPSPSRSPSPSRPPPPaDPSSPRKRPRPSRAPSSPAASAGRPTRRRA------RAAVAGRARRRDATGRFPAGR 411
|
....
gi 1622968700 2973 PPAI 2976
Cdd:PHA03307 412 PRPS 415
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
2669-2975 |
1.45e-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: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2669 TASKTNDSTEQNLSDGTPMPDSYPTTPSSTDAATSESKETLGtLQSSQQQPT-LPTPPALGEV--PQELQSPAGEGGSST 2745
Cdd:pfam05109 406 TRTATNATTTTHKVIFSKAPESTTTSPTLNTTGFAAPNTTTG-LPSSTHVPTnLTAPASTGPTvsTADVTSPTPAGTTSG 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2746 QllMPVEP---------EELGP--TRPSGEAET-TQMELSPAPTITSLSPERAEDSDALTAVSSQLEG-SPMDTSSLASC 2812
Cdd:pfam05109 485 A--SPVTPspsprdngtESKAPdmTSPTSAVTTpTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTpTPNATSPTPAV 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2813 TLEE------AVGDASATG--SSEQPRAGSSTPGDAPPAVAEVQGRSDGSGES---AQPPEDSSPPASSESSSTRDSAVA 2881
Cdd:pfam05109 563 TTPTpnatipTLGKTSPTSavTTPTPNATSPTVGETSPQANTTNHTLGGTSSTpvvTSPPKNATSAVTTGQHNITSSSTS 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2882 ISGADSRGILEEPLPSTS--SEEEDPLAGISLPEGVDPSFLAALPDDIRREVLQNQLGIRPPTRTAPS--TNSSAPAVVG 2957
Cdd:pfam05109 643 SMSLRPSSISETLSPSTSdnSTSHMPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASgpGNSSTSTKPG 722
|
330
....*....|....*...
gi 1622968700 2958 NPGVTEVSPEFLAALPPA 2975
Cdd:pfam05109 723 EVNVTKGTPPKNATSPQA 740
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2682-3013 |
1.59e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.48 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2682 SDGTPMPDSYPTTPSSTDAAtSESKETLGTLQSSQQQPTLPTPPALGEVPQELQSPAGeggSSTQLLMPVEPEELGPTRP 2761
Cdd:PHA03247 2637 EPDPHPPPTVPPPERPRDDP-APGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVG---SLTSLADPPPPPPTPEPAP 2712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2762 SGEAETTQMELSPAPTITSLSPERAEDSDALTAVSSQLEGSPMDTSSLASctleeavgdASATGSSEQPRAgsstPGDAP 2841
Cdd:PHA03247 2713 HALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPT---------TAGPPAPAPPAA----PAAGP 2779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2842 PAVAEVQGRSDGSGESAQPPEDSSPPASSESSSTRDSAVAISGADSRGileEPLPSTSSEEEDPLAGISLPEGVDPSFLA 2921
Cdd:PHA03247 2780 PRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP---LPPPTSAQPTAPPPPPGPPPPSLPLGGSV 2856
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2922 ALPDDIRREVLQNQLGIRPPTRTAPSTNS-SAPAVVGNPGVTEVSPEFLAALP-PAIQEEVLAQQRAEQQRRE---LAQN 2996
Cdd:PHA03247 2857 APGGDVRRRPPSRSPAAKPAAPARPPVRRlARPAVSRSTESFALPPDQPERPPqPQAPPPPQPQPQPPPPPQPqppPPPP 2936
|
330
....*....|....*..
gi 1622968700 2997 ASSDTPMDPVTFIQTLP 3013
Cdd:PHA03247 2937 PRPQPPLAPTTDPAGAG 2953
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2688-3073 |
5.68e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.94 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2688 PDSYPTTPSSTDAATSESKETLGTLQSSQQQPTLPTPPALGEVPQELQSPAGEG-----------GSSTQLLMPVEPEEL 2756
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPArparppttagpPAPAPPAAPAAGPPR 2781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2757 GPTRPSGEAETTQMELSPAPTITSLSPERAED-SDALTAVSSQLEGSPMDTSSL------------ASCTLEEAV---GD 2820
Cdd:PHA03247 2782 RLTRPAVASLSESRESLPSPWDPADPPAAVLApAAALPPAASPAGPLPPPTSAQptapppppgpppPSLPLGGSVapgGD 2861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2821 ASATGSSEQPRAGSSTPGDaPPAVAEVQGRSDGSGESAQPPEDSSPPASSESSSTRDSAVAISGADSRgilEEPLPSTSS 2900
Cdd:PHA03247 2862 VRRRPPSRSPAAKPAAPAR-PPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ---PQPPPPPPP 2937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2901 EEEDPL------AGISLPEGVDPSFLAALPDDIRREVLQNQLGIRPPTRTAPSTNSSAPAVVGNPGVTEVSpeflaalpp 2974
Cdd:PHA03247 2938 RPQPPLapttdpAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWA--------- 3008
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2975 aiqeevlaqqraeqqrRELAQNASSDTPmdPVTFIQTL-PSD---------LRRSVLEDMEDSVLAVMPPD----IAAEA 3040
Cdd:PHA03247 3009 ----------------SSLALHEETDPP--PVSLKQTLwPPDdtedsdadsLFDSDSERSDLEALDPLPPEphdpFAHEP 3070
|
410 420 430
....*....|....*....|....*....|...
gi 1622968700 3041 QALRREQEARQRQLMHerlFGHSSTSALSAILR 3073
Cdd:PHA03247 3071 DPATPEAGARESPSSQ---FGPPPLSANAALSR 3100
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
2718-2940 |
1.27e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 48.44 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2718 QPTLPTPPALGEVPQELQSPAGeggsstqllmPVEPEELGPTRPSGEAeTTQMELSPAPTITSLSPERAEDSDALTAVSS 2797
Cdd:PRK07764 596 GGEGPPAPASSGPPEEAARPAA----------PAAPAAPAAPAPAGAA-AAPAEASAAPAPGVAAPEHHPKHVAVPDASD 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2798 QLEGSPMDTSSLASCTLEEA------VGDASATGSSEQPR-------AGSSTPGDAPPAVAEVQGRSDGSGESAQPPEDS 2864
Cdd:PRK07764 665 GGDGWPAKAGGAAPAAPPPApapaapAAPAGAAPAQPAPApaatppaGQADDPAAQPPQAAQGASAPSPAADDPVPLPPE 744
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622968700 2865 SPPASSESSSTRDSAVAISGADSRGILEEPLPSTSSEEEDPLAgiSLPEGVDPSFLAAlPDDIRREVLQNQLGIRP 2940
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 |
2.38e-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: 2.38e-04
10 20 30
....*....|....*....|....*....|..
gi 1622968700 1407 MDMGFTREHAMEAL--LNTSTMEQATEYLLTH 1436
Cdd:cd14327 7 VEMGFSRERAEEALraVGTNSVELAMEWLFTN 38
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2682-3006 |
5.06e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.47 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2682 SDGTPMPDSyPTTPSS------TDAATSESK-----------ETLGTLQSSQQQPTLP--TPPALGE----VPQELQSPA 2738
Cdd:PHA03247 2500 GGGPPDPDA-PPAPSRlapailPDEPVGEPVhprmltwirglEELASDDAGDPPPPLPpaAPPAAPDrsvpPPRPAPRPS 2578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2739 GEGGSSTQLLMPVEPEELGPTRPSGEAETTQMELSPAPTITSLSPERAEDSDALTAVSSQLEGSPMDTSSLASCTLEEAV 2818
Cdd:PHA03247 2579 EPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAP 2658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2819 GDAS----ATGSSEQPRAGSST----PGDAPPAVAEVQgrsdgsgESAQPPEDSSPPASSESSSTrdSAVAISGADSRGI 2890
Cdd:PHA03247 2659 GRVSrprrARRLGRAAQASSPPqrprRRAARPTVGSLT-------SLADPPPPPPTPEPAPHALV--SATPLPPGPAAAR 2729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2891 LEEPLPSTSSEEEDPLAGISLPEGVDPSFLAALPDDIRREVL-QNQLGIRPPTRTAPSTNSSAPAVVGNPGVTEVSPEFL 2969
Cdd:PHA03247 2730 QASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPpAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPA 2809
|
330 340 350
....*....|....*....|....*....|....*..
gi 1622968700 2970 AALPPAIQEEVLAQQRAEQQRRELAQNASSDTPMDPV 3006
Cdd:PHA03247 2810 AVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPP 2846
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
2724-2997 |
1.36e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 44.84 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2724 PPALGEVPQELQSPAGEGGSSTQLLMPVEPEELGPTRPSGEAETTQMELSPAPTITS---LSPERAEDSDAltAVSSQLE 2800
Cdd:PRK07003 368 PGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEappAAPAPPATADR--GDDAADG 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2801 GSPMDTSSLASCTLEEAVGDASATGSSeQPRAGSSTPGDAPPAVA-EVQGRSDGSGESAQPPEDSSPPASsessstrdsa 2879
Cdd:PRK07003 446 DAPVPAKANARASADSRCDERDAQPPA-DSGSASAPASDAPPDAAfEPAPRAAAPSAATPAAVPDARAPA---------- 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2880 vAISGADSRGILEEPLPSTSSEEedPLAGISLPEGVDPSflAALpddirrEVLQNQlGIRpptrtAPSTNSSAPAVVGNP 2959
Cdd:PRK07003 515 -AASREDAPAAAAPPAPEARPPT--PAAAAPAARAGGAA--AAL------DVLRNA-GMR-----VSSDRGARAAAAAKP 577
|
250 260 270
....*....|....*....|....*....|....*....
gi 1622968700 2960 GVTEVSPEFLAALPPAIQEEVL-AQQRAEQQRRELAQNA 2997
Cdd:PRK07003 578 AAAPAAAPKPAAPRVAVQVPTPrARAATGDAPPNGAARA 616
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
2737-2995 |
5.00e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.94 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2737 PAGEGGSStqllmpvepeelGPTRPSGEAETTQMELSPAPTITSLSPERAEDSDALTAVSSQLEGSPMDTSSLASCTLEE 2816
Cdd:PRK12323 365 PGQSGGGA------------GPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2817 AvgdASATGSSEQPRAGSSTPGDAPPAVAEVQGRSdgSGESAQPPEDSSPPASSESSSTRDSAVAISGADSRGILEEPLP 2896
Cdd:PRK12323 433 L---AAARQASARGPGGAPAPAPAPAAAPAAAARP--AAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2897 STSSEEEDP-LAGISLPEGVDPSflAALPDDIRREVLQNQLGIRPPTRTAPSTNSSA--PAVVGNPGVTEVS----PEFL 2969
Cdd:PRK12323 508 SPAPAQPDAaPAGWVAESIPDPA--TADPDDAFETLAPAPAAAPAPRAAAATEPVVAprPPRASASGLPDMFdgdwPALA 585
|
250 260
....*....|....*....|....*.
gi 1622968700 2970 AALPPaiqeEVLAQQRAEQQrrELAQ 2995
Cdd:PRK12323 586 ARLPV----RGLAQQLARQS--ELAG 605
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
2915-2933 |
8.80e-03 |
|
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen.
Pssm-ID: 412037 Cd Length: 36 Bit Score: 36.82 E-value: 8.80e-03
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
2657-2966 |
8.86e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.47 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2657 EDKENRDQSAQCTASKTNDSTEQNLSDGTPMpdsypTTPSSTDAATSESKETLGTlQSSQQQPTLPTP-PALGEVPQELQ 2735
Cdd:PHA03307 12 EAAAEGGEFFPRPPATPGDAADDLLSGSQGQ-----LVSDSAELAAVTVVAGAAA-CDRFEPPTGPPPgPGTEAPANESR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2736 SPAGEGGSSTQLLMPVEPEELGPTRPSGEAETTQME--LSPAPtitSLSPERAEDSDALTAVSSQLEGSPMDTSSLASCT 2813
Cdd:PHA03307 86 STPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPppASPPP---SPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2814 ---LEEAVGDASATGSSEQPRAGSSTPGDAPPavaevqGRSDGSGESAQPPEdsspPASSESSSTRDSAVAISGADSRGI 2890
Cdd:PHA03307 163 asdAASSRQAALPLSSPEETARAPSSPPAEPP------PSTPPAAASPRPPR----RSSPISASASSPAPAPGRSAADDA 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622968700 2891 LEEPLPSTSSEEEDPLAGISLPEGVDPSFLAALPDDIRREVLQNQLGIRP-PTRTAPSTNSSAPAVV-GNPGVTEVSP 2966
Cdd:PHA03307 233 GASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPgPASSSSSPRERSPSPSpSSPGSGPAPS 310
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
2682-2912 |
9.08e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.47 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2682 SDGTPMP---DSYPTTPSSTDAATSESKETLGTLQSSQQQP-----TLPTPPALGEVPQELQSPAGEGGSSTQllmpvEP 2753
Cdd:PHA03307 218 SSPAPAPgrsAADDAGASSSDSSSSESSGCGWGPENECPLPrpapiTLPTRIWEASGWNGPSSRPGPASSSSS-----PR 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2754 EELGPTRPSGEAETtqmELSPAPTITSLSPERAEDSDALTAVSSQLEGSPMDTSSLASCTL-----EEAVGDASATGSSE 2828
Cdd:PHA03307 293 ERSPSPSPSSPGSG---PAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSpspsrPPPPADPSSPRKRP 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622968700 2829 QPRAGSSTPGDAPP---------AVAEVQGRSDGSGESAQPPedssppassesssTRDSAVAISGADSRGILEEPLPSTS 2899
Cdd:PHA03307 370 RPSRAPSSPAASAGrptrrraraAVAGRARRRDATGRFPAGR-------------PRPSPLDAGAASGAFYARYPLLTPS 436
|
250
....*....|...
gi 1622968700 2900 SEeedPLAGISLP 2912
Cdd:PHA03307 437 GE---PWPGSPPP 446
|
|
|