|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
3998-4351 |
4.32e-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: 4.32e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 3998 VHVRRDHVFEDSYRELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSH 4077
Cdd:cd00078 3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4078 CNPNHLSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEV 4157
Cdd:cd00078 83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4158 QE-FGVCEVRDLKPNGANILVTEENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTI 4236
Cdd:cd00078 163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4237 DIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEgmngiQKFQIHRDDRSTDRLP 4315
Cdd:cd00078 243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 2038296688 4316 SAHTCFNQLDLPAYESYEKLRHMLLLAIQECsEGFG 4351
Cdd:cd00078 318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
|
|
| DUF913 |
pfam06025 |
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ... |
431-859 |
7.54e-102 |
|
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin protein ligases.
:
Pssm-ID: 461803 Cd Length: 369 Bit Score: 333.04 E-value: 7.54e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 431 RAVRVVD-LITNLD--MAAFQSHSGLSIFIYRLEHEVDLCRKecpfvikpkiqrpaNVQEGEEMETDMevsdvamescpg 507
Cdd:pfam06025 1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALE--------------LAEAGKGTPSEY------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 508 PSTSSDHRpslstssssssivvprtgvqcIP-QRAALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGT-LPTSLKHIISNA 583
Cdd:pfam06025 55 KSSVVDYE---------------------IPyYRQQLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 584 EYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLTDVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLQSFVQCQPF 663
Cdd:pfam06025 114 KVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAGLSKAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNAL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 664 ERLFKVLLSPDYLPAMRrrrssdplaltslrsPAGDTASNLGSAVDELMRHQPTLKTDATTAIIKLLEEICNLGRDPKY- 742
Cdd:pfam06025 194 ESFFEIFESPDHVKAME---------------TDGELASNLGSSFDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEp 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 743 --ICQKPSIQKADGTATAPPPRTNHAAEEASSEDEEEEE---VQAMQSFSTNQQSEVEPSQHvvgteeriPIPLMDYILN 817
Cdd:pfam06025 259 dgWGAKLWVGCSSSSSFSPASSGSLPMETDGESGDESSSdedVEMEDAPDTDSTEETEPESH--------GNSLTDYIDN 330
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2038296688 818 VMKFVESILSNNTtddHCQEFVSQKGLLPLVTILGLPNLPID 859
Cdd:pfam06025 331 VARFLEAFFSNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
|
|
| DUF908 super family |
cl20318 |
Domain of Unknown Function (DUF908); |
90-367 |
7.01e-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: 7.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 90 KALLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASSDMQVVLAVLNLL------YVFSKRSNYITRLASDKRTP----- 158
Cdd:pfam06012 3 RELVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLlrlaqrYSASNSRRGSAPRHIQQSLLanhyn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 159 -LLSRLQHLAESWG------------------GKENGFGLAECCKDMHmLKYPPSATTLHFEFYAELGSEVKVEK----- 214
Cdd:pfam06012 83 iDLDRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKEDS-KVLPSEWGSVKFTYYPSSSSDEAPTSsksst 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 215 ------------------------------------RTSSNTLHYIHIEQLDKISESPSEIMESLtkMYSIPKDKQMLLF 258
Cdd:pfam06012 162 ssnsspstptplrrsstlgtspdspsspststpssaADSDEGLRTFEIPESKVASKSLEDILAKA--IEDLPKESRFELL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 259 THIRLAHGFSNHK--KRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQIADKQLMEIKAASLRTLTSI 334
Cdd:pfam06012 240 HRIRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEAL 319
|
330 340 350
....*....|....*....|....*....|...
gi 2038296688 335 VHleRTPKLSSIIDCTGTASYHGFLPVLVRNCI 367
Cdd:pfam06012 320 AR--HRAKLSDVLSALGANVNHGILLYVLRKAV 350
|
|
| UBA_HUWE1 |
cd14288 |
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ... |
1361-1401 |
8.47e-19 |
|
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, also called ARF-binding protein 1 (ARF-BP1), HECT, UBA and WWE domain-containing protein 1, homologous to E6AP carboxyl terminus homologs protein 9 (HectH9), large structure of UREB1 (LASU1), Mcl-1 ubiquitin ligase E3 (Mule), upstream regulatory element-binding protein 1 (URE-B1), or URE-binding protein 1, may function as a ubiquitin-protein ligase that involves in the ubiquitination cascade that targets specific substrate proteins in proteolysis. It can ubiquitylate DNA polymerase beta (Pol beta), the major BER DNA polymerase and modulates base excision repair (BER). HUWE1 also acts as a critical mediator of both the p53-independent and p53-dependent tumor suppressor functions of ARF tumor suppressor in p53 regulation. Moreover, HUWE1 is both required and sufficient for the polyubiquitination of Mcl-1, an anti-apoptotic Bcl-2 family member involving in DNA damage-induced apoptosis. Furthermore, HUWE1 plays an important role in the regulation of Cdc6 stability after DNA damage. In addition, HUWE1 works as a partner of N-Myc oncoprotein in neural cells. It ubiquitinates N-Myc and primes it for proteasomal-mediated degradation. HUWE1 contains a ubiquitin-associated (UBA) domain, a WWE domain, and a Bcl-2 homology region 3 (BH3) domain at the N-terminus and a HECT domain at the C-terminus. WWE domain plays a role in the regulation of specific protein-protein interactions in a ubiquitin conjugation system. BH3 domain is responsible for the specific binding to Mcl-1. HECT domain involves in the inhibition of the transcriptional activity of p53 via a ubiquitin-dependent degradation pathway. It also controls neural differentiation and proliferation by destabilizing the N-Myc oncoprotein.
:
Pssm-ID: 270474 Cd Length: 40 Bit Score: 82.06 E-value: 8.47e-19
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2038296688 1361 VNQQHLQQvLMDMGFTREHALEALLNTSTMEQATEYLLTHP 1401
Cdd:cd14288 1 VNEAHLQQ-LMDMGFTREHALEALLHTSTLEQATEYLLTHP 40
|
|
| WWE |
pfam02825 |
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ... |
1631-1692 |
2.11e-13 |
|
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: 67.71 E-value: 2.11e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038296688 1631 WRWFDDRsGRWCSYSASNNNTIDAAWKAGET--CVRFTAGRRRYTVQFTTMVQVNEETGNRRPV 1692
Cdd:pfam02825 2 WEWEDDN-GGWHPYDPEVSSLIEEAYQKGKPsvDLSITTAGFPYTIDFKSMTQTNKDTGTTRPV 64
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
3016-3049 |
2.26e-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: 49.42 E-value: 2.26e-07
10 20 30
....*....|....*....|....*....|....
gi 2038296688 3016 ANAGVTEVSPEFLAALPPAIQEEVLAQQRAEQQR 3049
Cdd:pfam14377 1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
2970-2997 |
9.62e-07 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).
:
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 47.88 E-value: 9.62e-07
10 20
....*....|....*....|....*...
gi 2038296688 2970 PEGVDPSFLAALPEDIRREVLQNQLGIR 2997
Cdd:pfam14377 5 PEGIDPSFLAALPPDLRQEVLAQQDDER 32
|
|
| PHA03247 super family |
cl33720 |
large tegument protein UL36; Provisional |
2751-3094 |
1.11e-06 |
|
large tegument protein UL36; Provisional
The actual alignment was detected with superfamily member PHA03247:
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 55.33 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2751 PENFPTAPSSAEGTPTSPEivrldpTLRAHPPEATLAQLPQGLPADSGTeDAGLQLMSSHQEDSGPGHPSTEGD--ATQM 2828
Cdd:PHA03247 2708 PEPAPHALVSATPLPPGPA------AARQASPALPAAPAPPAVPAGPAT-PGGPARPARPPTTAGPPAPAPPAApaAGPP 2780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2829 ELSPAPTITSLSPERAedsdaltavSSQLEGSPMDTSSLASGPledgVGEIPGIVNPEQPLVVGSSIavgqQPVEPPTTG 2908
Cdd:PHA03247 2781 RRLTRPAVASLSESRE---------SLPSPWDPADPPAAVLAP----AAALPPAASPAGPLPPPTSA----QPTAPPPPP 2843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2909 EAQPVVSQHSDESSPIAPSSELPSLRESAVTLLATDSSGI--LEEPLPSTSSED----EDPLAGINLPEGVDPsflaALP 2982
Cdd:PHA03247 2844 GPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVrrLARPAVSRSTESfalpPDQPERPPQPQAPPP----PQP 2919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2983 EDIRREVLQNQLGIRPPSRPPPTAAPVIPPPVVANAGVTEVSPEfLAALPPAIQEEVLAQQRAEQQRRELTQSITS---- 3058
Cdd:PHA03247 2920 QPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPW-LGALVPGRVAVPRFRVPQPAPSREAPASSTPpltg 2998
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038296688 3059 -----------------DTPMDPVTFIQTL-PSD---------LRRSVLEDMEESVLAVMPPD 3094
Cdd:PHA03247 2999 hslsrvsswasslalheETDPPPVSLKQTLwPPDdtedsdadsLFDSDSERSDLEALDPLPPE 3061
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
3998-4351 |
4.32e-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: 4.32e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 3998 VHVRRDHVFEDSYRELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSH 4077
Cdd:cd00078 3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4078 CNPNHLSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEV 4157
Cdd:cd00078 83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4158 QE-FGVCEVRDLKPNGANILVTEENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTI 4236
Cdd:cd00078 163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4237 DIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEgmngiQKFQIHRDDRSTDRLP 4315
Cdd:cd00078 243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 2038296688 4316 SAHTCFNQLDLPAYESYEKLRHMLLLAIQECsEGFG 4351
Cdd:cd00078 318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
4022-4350 |
4.01e-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: 4.01e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4022 KNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGRIVAKAVYDNR 4101
Cdd:smart00119 4 KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHLSYFRFIGRVLGKALYDNR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4102 LLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYL-LENDVSTLgYDLTFSTEVQE-FGVCEVRDLKPNGANILVTE 4179
Cdd:smart00119 84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSIVLTSeFGQVKVVELKPGGSNIPVTE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4180 ENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKSNTEY-HKYQSNSIQIQ 4258
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYkGGYSANSQTIK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4259 WFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGmngiqKFQIHRDDRSTDRLPSAHTCFNQLDLPAYESYEKLRHM 4338
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317
|
330
....*....|..
gi 2038296688 4339 LLLAIQECsEGF 4350
Cdd:smart00119 318 LLLAINEG-KGF 328
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
3936-4353 |
3.02e-148 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 486.58 E-value: 3.02e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 3936 RFAETHRTVLNQILRQSTTHL--ADGPFAVLVDYIRVLDFDVKRKYFRQeleRLDEGLRKEDMAVH--VRRDHVFEDSYR 4011
Cdd:COG5021 454 RLNNLYRFYFVEHRKKTLTKNdsRLGSFISLNKLDIRRIKEDKRRKLFY---SLKQKAKIFDPYLHikVRRDRVFEDSYR 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4012 ELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGR 4091
Cdd:COG5021 531 EIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGR 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4092 IVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEVQEFGVCEVRDLKPN 4171
Cdd:COG5021 611 VIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPN 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4172 GANILVTEENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPT-IDIDDLKSNTEYHKY 4250
Cdd:COG5021 691 GRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGY 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4251 QSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGMNGIQKFQIHRDDRSTDRLPSAHTCFNQLDLPAYE 4330
Cdd:COG5021 771 TEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYS 850
|
410 420
....*....|....*....|...
gi 2038296688 4331 SYEKLRHMLLLAIQECSeGFGLA 4353
Cdd:COG5021 851 SKEKLRSKLLTAINEGA-GFGLL 872
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
4047-4353 |
1.28e-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: 384.27 E-value: 1.28e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4047 IISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNH--LSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTD 4124
Cdd:pfam00632 2 LLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4125 MESEDYHFYQGLVYLLENDVSTLG-YDLTFSteVQEFGVCEVRDLKPNGANILVTEENKKEYVHLVCQMKMTGAIRKQLA 4203
Cdd:pfam00632 82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4204 AFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGT 4282
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYdGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038296688 4283 SKVPLQGFAALegmngiQKFQIHR-DDRSTDRLPSAHTCFNQLDLPAYESYEKLRHMLLLAIQECsEGFGLA 4353
Cdd:pfam00632 240 SRLPVGGFKSL------PKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
|
|
| DUF913 |
pfam06025 |
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ... |
431-859 |
7.54e-102 |
|
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin protein ligases.
Pssm-ID: 461803 Cd Length: 369 Bit Score: 333.04 E-value: 7.54e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 431 RAVRVVD-LITNLD--MAAFQSHSGLSIFIYRLEHEVDLCRKecpfvikpkiqrpaNVQEGEEMETDMevsdvamescpg 507
Cdd:pfam06025 1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALE--------------LAEAGKGTPSEY------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 508 PSTSSDHRpslstssssssivvprtgvqcIP-QRAALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGT-LPTSLKHIISNA 583
Cdd:pfam06025 55 KSSVVDYE---------------------IPyYRQQLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 584 EYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLTDVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLQSFVQCQPF 663
Cdd:pfam06025 114 KVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAGLSKAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNAL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 664 ERLFKVLLSPDYLPAMRrrrssdplaltslrsPAGDTASNLGSAVDELMRHQPTLKTDATTAIIKLLEEICNLGRDPKY- 742
Cdd:pfam06025 194 ESFFEIFESPDHVKAME---------------TDGELASNLGSSFDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEp 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 743 --ICQKPSIQKADGTATAPPPRTNHAAEEASSEDEEEEE---VQAMQSFSTNQQSEVEPSQHvvgteeriPIPLMDYILN 817
Cdd:pfam06025 259 dgWGAKLWVGCSSSSSFSPASSGSLPMETDGESGDESSSdedVEMEDAPDTDSTEETEPESH--------GNSLTDYIDN 330
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2038296688 818 VMKFVESILSNNTtddHCQEFVSQKGLLPLVTILGLPNLPID 859
Cdd:pfam06025 331 VARFLEAFFSNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
|
|
| DUF908 |
pfam06012 |
Domain of Unknown Function (DUF908); |
90-367 |
7.01e-24 |
|
Domain of Unknown Function (DUF908);
Pssm-ID: 428721 Cd Length: 351 Bit Score: 106.65 E-value: 7.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 90 KALLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASSDMQVVLAVLNLL------YVFSKRSNYITRLASDKRTP----- 158
Cdd:pfam06012 3 RELVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLlrlaqrYSASNSRRGSAPRHIQQSLLanhyn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 159 -LLSRLQHLAESWG------------------GKENGFGLAECCKDMHmLKYPPSATTLHFEFYAELGSEVKVEK----- 214
Cdd:pfam06012 83 iDLDRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKEDS-KVLPSEWGSVKFTYYPSSSSDEAPTSsksst 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 215 ------------------------------------RTSSNTLHYIHIEQLDKISESPSEIMESLtkMYSIPKDKQMLLF 258
Cdd:pfam06012 162 ssnsspstptplrrsstlgtspdspsspststpssaADSDEGLRTFEIPESKVASKSLEDILAKA--IEDLPKESRFELL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 259 THIRLAHGFSNHK--KRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQIADKQLMEIKAASLRTLTSI 334
Cdd:pfam06012 240 HRIRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEAL 319
|
330 340 350
....*....|....*....|....*....|...
gi 2038296688 335 VHleRTPKLSSIIDCTGTASYHGFLPVLVRNCI 367
Cdd:pfam06012 320 AR--HRAKLSDVLSALGANVNHGILLYVLRKAV 350
|
|
| UBA_HUWE1 |
cd14288 |
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ... |
1361-1401 |
8.47e-19 |
|
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, also called ARF-binding protein 1 (ARF-BP1), HECT, UBA and WWE domain-containing protein 1, homologous to E6AP carboxyl terminus homologs protein 9 (HectH9), large structure of UREB1 (LASU1), Mcl-1 ubiquitin ligase E3 (Mule), upstream regulatory element-binding protein 1 (URE-B1), or URE-binding protein 1, may function as a ubiquitin-protein ligase that involves in the ubiquitination cascade that targets specific substrate proteins in proteolysis. It can ubiquitylate DNA polymerase beta (Pol beta), the major BER DNA polymerase and modulates base excision repair (BER). HUWE1 also acts as a critical mediator of both the p53-independent and p53-dependent tumor suppressor functions of ARF tumor suppressor in p53 regulation. Moreover, HUWE1 is both required and sufficient for the polyubiquitination of Mcl-1, an anti-apoptotic Bcl-2 family member involving in DNA damage-induced apoptosis. Furthermore, HUWE1 plays an important role in the regulation of Cdc6 stability after DNA damage. In addition, HUWE1 works as a partner of N-Myc oncoprotein in neural cells. It ubiquitinates N-Myc and primes it for proteasomal-mediated degradation. HUWE1 contains a ubiquitin-associated (UBA) domain, a WWE domain, and a Bcl-2 homology region 3 (BH3) domain at the N-terminus and a HECT domain at the C-terminus. WWE domain plays a role in the regulation of specific protein-protein interactions in a ubiquitin conjugation system. BH3 domain is responsible for the specific binding to Mcl-1. HECT domain involves in the inhibition of the transcriptional activity of p53 via a ubiquitin-dependent degradation pathway. It also controls neural differentiation and proliferation by destabilizing the N-Myc oncoprotein.
Pssm-ID: 270474 Cd Length: 40 Bit Score: 82.06 E-value: 8.47e-19
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2038296688 1361 VNQQHLQQvLMDMGFTREHALEALLNTSTMEQATEYLLTHP 1401
Cdd:cd14288 1 VNEAHLQQ-LMDMGFTREHALEALLHTSTLEQATEYLLTHP 40
|
|
| WWE |
pfam02825 |
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ... |
1631-1692 |
2.11e-13 |
|
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: 67.71 E-value: 2.11e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038296688 1631 WRWFDDRsGRWCSYSASNNNTIDAAWKAGET--CVRFTAGRRRYTVQFTTMVQVNEETGNRRPV 1692
Cdd:pfam02825 2 WEWEDDN-GGWHPYDPEVSSLIEEAYQKGKPsvDLSITTAGFPYTIDFKSMTQTNKDTGTTRPV 64
|
|
| WWE |
smart00678 |
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ... |
1631-1692 |
1.52e-11 |
|
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;
Pssm-ID: 128922 [Multi-domain] Cd Length: 73 Bit Score: 62.74 E-value: 1.52e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038296688 1631 WRW-FDDRSGRWCSYSASNNNTIDAAWKAGE-TCVRFTAGRRrYTVQFTTMVQVNEETGNRRPV 1692
Cdd:smart00678 1 YVWeYEGRNGKWWPYDPRVSEDIEEAYAAGKkLCELSICGFP-YTIDFNAMTQYNQATGTTRKV 63
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
3016-3049 |
2.26e-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: 49.42 E-value: 2.26e-07
10 20 30
....*....|....*....|....*....|....
gi 2038296688 3016 ANAGVTEVSPEFLAALPPAIQEEVLAQQRAEQQR 3049
Cdd:pfam14377 1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
2970-2997 |
9.62e-07 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 47.88 E-value: 9.62e-07
10 20
....*....|....*....|....*...
gi 2038296688 2970 PEGVDPSFLAALPEDIRREVLQNQLGIR 2997
Cdd:pfam14377 5 PEGIDPSFLAALPPDLRQEVLAQQDDER 32
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2751-3094 |
1.11e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 55.33 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2751 PENFPTAPSSAEGTPTSPEivrldpTLRAHPPEATLAQLPQGLPADSGTeDAGLQLMSSHQEDSGPGHPSTEGD--ATQM 2828
Cdd:PHA03247 2708 PEPAPHALVSATPLPPGPA------AARQASPALPAAPAPPAVPAGPAT-PGGPARPARPPTTAGPPAPAPPAApaAGPP 2780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2829 ELSPAPTITSLSPERAedsdaltavSSQLEGSPMDTSSLASGPledgVGEIPGIVNPEQPLVVGSSIavgqQPVEPPTTG 2908
Cdd:PHA03247 2781 RRLTRPAVASLSESRE---------SLPSPWDPADPPAAVLAP----AAALPPAASPAGPLPPPTSA----QPTAPPPPP 2843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2909 EAQPVVSQHSDESSPIAPSSELPSLRESAVTLLATDSSGI--LEEPLPSTSSED----EDPLAGINLPEGVDPsflaALP 2982
Cdd:PHA03247 2844 GPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVrrLARPAVSRSTESfalpPDQPERPPQPQAPPP----PQP 2919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2983 EDIRREVLQNQLGIRPPSRPPPTAAPVIPPPVVANAGVTEVSPEfLAALPPAIQEEVLAQQRAEQQRRELTQSITS---- 3058
Cdd:PHA03247 2920 QPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPW-LGALVPGRVAVPRFRVPQPAPSREAPASSTPpltg 2998
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038296688 3059 -----------------DTPMDPVTFIQTL-PSD---------LRRSVLEDMEESVLAVMPPD 3094
Cdd:PHA03247 2999 hslsrvsswasslalheETDPPPVSLKQTLwPPDdtedsdadsLFDSDSERSDLEALDPLPPE 3061
|
|
| UBA |
pfam00627 |
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ... |
1361-1397 |
8.56e-05 |
|
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.
Pssm-ID: 395502 [Multi-domain] Cd Length: 37 Bit Score: 42.43 E-value: 8.56e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2038296688 1361 VNQQHLQQvLMDMGFTREHALEALLNTST-MEQATEYL 1397
Cdd:pfam00627 1 EDEEAIQR-LVEMGFDREQVREALRATGNnVERAAEYL 37
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
2973-2991 |
6.28e-03 |
|
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen.
Pssm-ID: 412037 Cd Length: 36 Bit Score: 37.20 E-value: 6.28e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
3998-4351 |
4.32e-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: 4.32e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 3998 VHVRRDHVFEDSYRELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSH 4077
Cdd:cd00078 3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4078 CNPNHLSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEV 4157
Cdd:cd00078 83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4158 QE-FGVCEVRDLKPNGANILVTEENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTI 4236
Cdd:cd00078 163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4237 DIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEgmngiQKFQIHRDDRSTDRLP 4315
Cdd:cd00078 243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 2038296688 4316 SAHTCFNQLDLPAYESYEKLRHMLLLAIQECsEGFG 4351
Cdd:cd00078 318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
4022-4350 |
4.01e-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: 4.01e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4022 KNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGRIVAKAVYDNR 4101
Cdd:smart00119 4 KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHLSYFRFIGRVLGKALYDNR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4102 LLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYL-LENDVSTLgYDLTFSTEVQE-FGVCEVRDLKPNGANILVTE 4179
Cdd:smart00119 84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSIVLTSeFGQVKVVELKPGGSNIPVTE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4180 ENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKSNTEY-HKYQSNSIQIQ 4258
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYkGGYSANSQTIK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4259 WFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGmngiqKFQIHRDDRSTDRLPSAHTCFNQLDLPAYESYEKLRHM 4338
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317
|
330
....*....|..
gi 2038296688 4339 LLLAIQECsEGF 4350
Cdd:smart00119 318 LLLAINEG-KGF 328
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
3936-4353 |
3.02e-148 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 486.58 E-value: 3.02e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 3936 RFAETHRTVLNQILRQSTTHL--ADGPFAVLVDYIRVLDFDVKRKYFRQeleRLDEGLRKEDMAVH--VRRDHVFEDSYR 4011
Cdd:COG5021 454 RLNNLYRFYFVEHRKKTLTKNdsRLGSFISLNKLDIRRIKEDKRRKLFY---SLKQKAKIFDPYLHikVRRDRVFEDSYR 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4012 ELHRKSPEEMKNRLYIVFEGEEGQDAGGLLREWYMIISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNHLSYFKFVGR 4091
Cdd:COG5021 531 EIMDESGDDLKKTLEIEFVGEEGIDAGGLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGR 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4092 IVAKAVYDNRLLECYFTRSFYKHILGKSVRYTDMESEDYHFYQGLVYLLENDVSTLGYDLTFSTEVQEFGVCEVRDLKPN 4171
Cdd:COG5021 611 VIGKAIYDSRILDVQFSKAFYKKLLGKPVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPN 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4172 GANILVTEENKKEYVHLVCQMKMTGAIRKQLAAFLEGFYEIIPKRLISIFTEQELELLISGLPT-IDIDDLKSNTEYHKY 4250
Cdd:COG5021 691 GRNISVTNENKKEYVKKVVDYKLNKRVEKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGY 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4251 QSNSIQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFAALEGMNGIQKFQIHRDDRSTDRLPSAHTCFNQLDLPAYE 4330
Cdd:COG5021 771 TEDSPIIVWFWEIISEFDFEERAKLLQFVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYS 850
|
410 420
....*....|....*....|...
gi 2038296688 4331 SYEKLRHMLLLAIQECSeGFGLA 4353
Cdd:COG5021 851 SKEKLRSKLLTAINEGA-GFGLL 872
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
4047-4353 |
1.28e-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: 384.27 E-value: 1.28e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4047 IISREMFNPMYALFRTSPGDRVTYTINPSSHCNPNH--LSYFKFVGRIVAKAVYDNRLLECYFTRSFYKHILGKSVRYTD 4124
Cdd:pfam00632 2 LLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4125 MESEDYHFYQGLVYLLENDVSTLG-YDLTFSteVQEFGVCEVRDLKPNGANILVTEENKKEYVHLVCQMKMTGAIRKQLA 4203
Cdd:pfam00632 82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 4204 AFLEGFYEIIPKRLISIFTEQELELLISGLPTIDIDDLKSNTEY-HKYQSNSIQIQWFWRALRSFDQADRAKFLQFVTGT 4282
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYdGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038296688 4283 SKVPLQGFAALegmngiQKFQIHR-DDRSTDRLPSAHTCFNQLDLPAYESYEKLRHMLLLAIQECsEGFGLA 4353
Cdd:pfam00632 240 SRLPVGGFKSL------PKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
|
|
| DUF913 |
pfam06025 |
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ... |
431-859 |
7.54e-102 |
|
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin protein ligases.
Pssm-ID: 461803 Cd Length: 369 Bit Score: 333.04 E-value: 7.54e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 431 RAVRVVD-LITNLD--MAAFQSHSGLSIFIYRLEHEVDLCRKecpfvikpkiqrpaNVQEGEEMETDMevsdvamescpg 507
Cdd:pfam06025 1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALE--------------LAEAGKGTPSEY------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 508 PSTSSDHRpslstssssssivvprtgvqcIP-QRAALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGT-LPTSLKHIISNA 583
Cdd:pfam06025 55 KSSVVDYE---------------------IPyYRQQLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 584 EYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLTDVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLQSFVQCQPF 663
Cdd:pfam06025 114 KVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAGLSKAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNAL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 664 ERLFKVLLSPDYLPAMRrrrssdplaltslrsPAGDTASNLGSAVDELMRHQPTLKTDATTAIIKLLEEICNLGRDPKY- 742
Cdd:pfam06025 194 ESFFEIFESPDHVKAME---------------TDGELASNLGSSFDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEp 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 743 --ICQKPSIQKADGTATAPPPRTNHAAEEASSEDEEEEE---VQAMQSFSTNQQSEVEPSQHvvgteeriPIPLMDYILN 817
Cdd:pfam06025 259 dgWGAKLWVGCSSSSSFSPASSGSLPMETDGESGDESSSdedVEMEDAPDTDSTEETEPESH--------GNSLTDYIDN 330
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2038296688 818 VMKFVESILSNNTtddHCQEFVSQKGLLPLVTILGLPNLPID 859
Cdd:pfam06025 331 VARFLEAFFSNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
|
|
| DUF908 |
pfam06012 |
Domain of Unknown Function (DUF908); |
90-367 |
7.01e-24 |
|
Domain of Unknown Function (DUF908);
Pssm-ID: 428721 Cd Length: 351 Bit Score: 106.65 E-value: 7.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 90 KALLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASSDMQVVLAVLNLL------YVFSKRSNYITRLASDKRTP----- 158
Cdd:pfam06012 3 RELVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLlrlaqrYSASNSRRGSAPRHIQQSLLanhyn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 159 -LLSRLQHLAESWG------------------GKENGFGLAECCKDMHmLKYPPSATTLHFEFYAELGSEVKVEK----- 214
Cdd:pfam06012 83 iDLDRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKEDS-KVLPSEWGSVKFTYYPSSSSDEAPTSsksst 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 215 ------------------------------------RTSSNTLHYIHIEQLDKISESPSEIMESLtkMYSIPKDKQMLLF 258
Cdd:pfam06012 162 ssnsspstptplrrsstlgtspdspsspststpssaADSDEGLRTFEIPESKVASKSLEDILAKA--IEDLPKESRFELL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 259 THIRLAHGFSNHK--KRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQIADKQLMEIKAASLRTLTSI 334
Cdd:pfam06012 240 HRIRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEAL 319
|
330 340 350
....*....|....*....|....*....|...
gi 2038296688 335 VHleRTPKLSSIIDCTGTASYHGFLPVLVRNCI 367
Cdd:pfam06012 320 AR--HRAKLSDVLSALGANVNHGILLYVLRKAV 350
|
|
| UBA_HUWE1 |
cd14288 |
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ... |
1361-1401 |
8.47e-19 |
|
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, also called ARF-binding protein 1 (ARF-BP1), HECT, UBA and WWE domain-containing protein 1, homologous to E6AP carboxyl terminus homologs protein 9 (HectH9), large structure of UREB1 (LASU1), Mcl-1 ubiquitin ligase E3 (Mule), upstream regulatory element-binding protein 1 (URE-B1), or URE-binding protein 1, may function as a ubiquitin-protein ligase that involves in the ubiquitination cascade that targets specific substrate proteins in proteolysis. It can ubiquitylate DNA polymerase beta (Pol beta), the major BER DNA polymerase and modulates base excision repair (BER). HUWE1 also acts as a critical mediator of both the p53-independent and p53-dependent tumor suppressor functions of ARF tumor suppressor in p53 regulation. Moreover, HUWE1 is both required and sufficient for the polyubiquitination of Mcl-1, an anti-apoptotic Bcl-2 family member involving in DNA damage-induced apoptosis. Furthermore, HUWE1 plays an important role in the regulation of Cdc6 stability after DNA damage. In addition, HUWE1 works as a partner of N-Myc oncoprotein in neural cells. It ubiquitinates N-Myc and primes it for proteasomal-mediated degradation. HUWE1 contains a ubiquitin-associated (UBA) domain, a WWE domain, and a Bcl-2 homology region 3 (BH3) domain at the N-terminus and a HECT domain at the C-terminus. WWE domain plays a role in the regulation of specific protein-protein interactions in a ubiquitin conjugation system. BH3 domain is responsible for the specific binding to Mcl-1. HECT domain involves in the inhibition of the transcriptional activity of p53 via a ubiquitin-dependent degradation pathway. It also controls neural differentiation and proliferation by destabilizing the N-Myc oncoprotein.
Pssm-ID: 270474 Cd Length: 40 Bit Score: 82.06 E-value: 8.47e-19
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2038296688 1361 VNQQHLQQvLMDMGFTREHALEALLNTSTMEQATEYLLTHP 1401
Cdd:cd14288 1 VNEAHLQQ-LMDMGFTREHALEALLHTSTLEQATEYLLTHP 40
|
|
| WWE |
pfam02825 |
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ... |
1631-1692 |
2.11e-13 |
|
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: 67.71 E-value: 2.11e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038296688 1631 WRWFDDRsGRWCSYSASNNNTIDAAWKAGET--CVRFTAGRRRYTVQFTTMVQVNEETGNRRPV 1692
Cdd:pfam02825 2 WEWEDDN-GGWHPYDPEVSSLIEEAYQKGKPsvDLSITTAGFPYTIDFKSMTQTNKDTGTTRPV 64
|
|
| WWE |
smart00678 |
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ... |
1631-1692 |
1.52e-11 |
|
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;
Pssm-ID: 128922 [Multi-domain] Cd Length: 73 Bit Score: 62.74 E-value: 1.52e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038296688 1631 WRW-FDDRSGRWCSYSASNNNTIDAAWKAGE-TCVRFTAGRRrYTVQFTTMVQVNEETGNRRPV 1692
Cdd:smart00678 1 YVWeYEGRNGKWWPYDPRVSEDIEEAYAAGKkLCELSICGFP-YTIDFNAMTQYNQATGTTRKV 63
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
3016-3049 |
2.26e-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: 49.42 E-value: 2.26e-07
10 20 30
....*....|....*....|....*....|....
gi 2038296688 3016 ANAGVTEVSPEFLAALPPAIQEEVLAQQRAEQQR 3049
Cdd:pfam14377 1 AAPPPEGIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
2970-2997 |
9.62e-07 |
|
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT E3 ubiquitin ligases and the Y-family translesion polymerases, including human HUWE1 and Arabidopsis UPL1. Each of these repetitive elements are approximately 20 amino acids in length and contain two predicted helical segments separated by a Leu-Pro motif. The REs from the Y-family polymerases were shown to bind ubiquitin and were the basis for a novel ubiquitin-binding domain called the ubiquitin-binding motif (UBM).
Pssm-ID: 464159 [Multi-domain] Cd Length: 34 Bit Score: 47.88 E-value: 9.62e-07
10 20
....*....|....*....|....*...
gi 2038296688 2970 PEGVDPSFLAALPEDIRREVLQNQLGIR 2997
Cdd:pfam14377 5 PEGIDPSFLAALPPDLRQEVLAQQDDER 32
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2751-3094 |
1.11e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 55.33 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2751 PENFPTAPSSAEGTPTSPEivrldpTLRAHPPEATLAQLPQGLPADSGTeDAGLQLMSSHQEDSGPGHPSTEGD--ATQM 2828
Cdd:PHA03247 2708 PEPAPHALVSATPLPPGPA------AARQASPALPAAPAPPAVPAGPAT-PGGPARPARPPTTAGPPAPAPPAApaAGPP 2780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2829 ELSPAPTITSLSPERAedsdaltavSSQLEGSPMDTSSLASGPledgVGEIPGIVNPEQPLVVGSSIavgqQPVEPPTTG 2908
Cdd:PHA03247 2781 RRLTRPAVASLSESRE---------SLPSPWDPADPPAAVLAP----AAALPPAASPAGPLPPPTSA----QPTAPPPPP 2843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2909 EAQPVVSQHSDESSPIAPSSELPSLRESAVTLLATDSSGI--LEEPLPSTSSED----EDPLAGINLPEGVDPsflaALP 2982
Cdd:PHA03247 2844 GPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVrrLARPAVSRSTESfalpPDQPERPPQPQAPPP----PQP 2919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2983 EDIRREVLQNQLGIRPPSRPPPTAAPVIPPPVVANAGVTEVSPEfLAALPPAIQEEVLAQQRAEQQRRELTQSITS---- 3058
Cdd:PHA03247 2920 QPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPW-LGALVPGRVAVPRFRVPQPAPSREAPASSTPpltg 2998
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038296688 3059 -----------------DTPMDPVTFIQTL-PSD---------LRRSVLEDMEESVLAVMPPD 3094
Cdd:PHA03247 2999 hslsrvsswasslalheETDPPPVSLKQTLwPPDdtedsdadsLFDSDSERSDLEALDPLPPE 3061
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
2757-3053 |
2.52e-06 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 53.78 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2757 APSSAEGTPTSPEIVRLdPTLRAHPPEATLAQLPQGLPADSGTEDAglqlmSSHQEDSGPGH----------PSTEGDAT 2826
Cdd:PLN03209 307 AETTAPLTPMEELLAKI-PSQRVPPKESDAADGPKPVPTKPVTPEA-----PSPPIEEEPPQpkavvprplsPYTAYEDL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2827 QMELSPAPTITSLSPERAEDSDALTAVSSQlegSPMDTSSLASGPLEDGVGEIPgiVNPEQPLvvgsSIAVGQQPVEPPT 2906
Cdd:PLN03209 381 KPPTSPIPTPPSSSPASSKSVDAVAKPAEP---DVVPSPGSASNVPEVEPAQVE--AKKTRPL----SPYARYEDLKPPT 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2907 TgeaqpvvsqhsdeSSPIAPSSELPSLRESAVTllatdsSGILEEPLPSTSSEDEDPlaginLPEGVDPSFLAALPEDir 2986
Cdd:PLN03209 452 S-------------PSPTAPTGVSPSVSSTSSV------PAVPDTAPATAATDAAAP-----PPANMRPLSPYAVYDD-- 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038296688 2987 revlqnqlgIRPPSRPPPTAapviPPPVVANAGVTEVSPEFLAALPPAIQEEvlaQQRAEQQRRELT 3053
Cdd:PLN03209 506 ---------LKPPTSPSPAA----PVGKVAPSSTNEVVKVGNSAPPTALADE---QHHAQPKPRPLS 556
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2758-3072 |
3.43e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.79 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2758 PSSAEGTPTSPEIVRLDP---TLRAHPPEATLAQLPQGLPADSGTEDAGLQLMSSHQEDSGPGHPSTEGDATQMELSPA- 2833
Cdd:PHA03247 2609 RGPAPPSPLPPDTHAPDPpppSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAa 2688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2834 -PTITSLS------PERAEDSDALTAVSSQLEGSPMDTSSLASGPLEDGVGEIPGIvnPEQPLVVGSSIAVGQQ------ 2900
Cdd:PHA03247 2689 rPTVGSLTsladppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAV--PAGPATPGGPARPARPpttagp 2766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2901 --------PVEPPTTGEAQPVVSQHSdESSPIAPSSELPSLRESAVT----LLATDSSGILEEPLPSTSSEDEDPLAGIN 2968
Cdd:PHA03247 2767 papappaaPAAGPPRRLTRPAVASLS-ESRESLPSPWDPADPPAAVLapaaALPPAASPAGPLPPPTSAQPTAPPPPPGP 2845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2969 LPEGVDPSFLAALPEDIRRevlqnqlgiRPPSRPPPT--AAPVIPPPVVANAGVTEVSPEFLAALP--------PAIQEE 3038
Cdd:PHA03247 2846 PPPSLPLGGSVAPGGDVRR---------RPPSRSPAAkpAAPARPPVRRLARPAVSRSTESFALPPdqperppqPQAPPP 2916
|
330 340 350
....*....|....*....|....*....|....*..
gi 2038296688 3039 VLAQQRAEQQRRELTQSIT---SDTPMDPVTFIQTLP 3072
Cdd:PHA03247 2917 PQPQPQPPPPPQPQPPPPPpprPQPPLAPTTDPAGAG 2953
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
2744-3013 |
5.79e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 52.87 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2744 DQDGSGHPENFPTAPSSAEGTPTSPEIVR-LDPTLRAHPPEATLAQLPQGLPADSGTEDAG--------LQLMSSHQEDS 2814
Cdd:PHA03307 107 TPPGPSSPDPPPPTPPPASPPPSPAPDLSeMLRPVGSPGPPPAASPPAAGASPAAVASDAAssrqaalpLSSPEETARAP 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2815 GPGHPSTEGDATQMELSPAP----TITSLSPERAEDSDALTAVSSQLEGSPMDTSSLASGPLEDGVGEIPgiVNPEQPLV 2890
Cdd:PHA03307 187 SSPPAEPPPSTPPAAASPRPprrsSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECP--LPRPAPIT 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2891 VGSSIAVGQQPVEP---PTTGEAQPVVSQHSDESSPIAPSSELPSLRESAVTLLATDSSGILEEPLPStSSEDEDPLAGI 2967
Cdd:PHA03307 265 LPTRIWEASGWNGPssrPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSS-SESSRGAAVSP 343
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2038296688 2968 NLPEGVDPSflAALPEDIRRevlqnqlGIRPPSRPPPTAAPVIPPP 3013
Cdd:PHA03307 344 GPSPSRSPS--PSRPPPPAD-------PSSPRKRPRPSRAPSSPAA 380
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
2752-3008 |
2.01e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 51.33 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2752 ENFPTAPSSAEGTPTSP-----------EIVRLDPTLRAHPPEATLAQLPQGLPADSGTEDAGLQLM-------SSHQED 2813
Cdd:PHA03307 19 EFFPRPPATPGDAADDLlsgsqgqlvsdSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRstptwslSTLAPA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2814 SGPGHPSTEGDATQMELSPAPTITSLSPERAEDSDAltavssqlegSPMDTSSLASGPLEDGVGEIPGIVNPEQPLVVGS 2893
Cdd:PHA03307 99 SPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDL----------SEMLRPVGSPGPPPAASPPAAGASPAAVASDAAS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2894 S------IAVGQQPVEPPTTGEAQPVVSQH--------SDESSPIAPSSELPS---LRESAVTLLATDSSgileeplpST 2956
Cdd:PHA03307 169 SrqaalpLSSPEETARAPSSPPAEPPPSTPpaaasprpPRRSSPISASASSPApapGRSAADDAGASSSD--------SS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2038296688 2957 SSEDEDPLAGINLPEGVDPSFLAALPEDIRREVLQNQLGIRPPSRPPPTAAP 3008
Cdd:PHA03307 241 SSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPR 292
|
|
| UBA_atUPL1_2_like |
cd14327 |
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ... |
1366-1400 |
2.32e-05 |
|
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: 43.83 E-value: 2.32e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2038296688 1366 LQQVLMDMGFTREHALEAL--LNTSTMEQATEYLLTH 1400
Cdd:cd14327 2 AVAQLVEMGFSRERAEEALraVGTNSVELAMEWLFTN 38
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
2813-3054 |
4.78e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 49.49 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2813 DSGPGHPSTEGDATQMELSPAPTITSLSPERAEDSDALTAVSSQLEGSPMDTSSLASGPLEdgvgeipGIVNPEQPLVVG 2892
Cdd:PRK12323 371 GAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPE-------ALAAARQASARG 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2893 SSIAVGQQPVEPPTTGEAQPVVSQHSDESSPIAPSSelPSLRESAVTLLATDSSGILEEPLPSTSSEDEdplaginlPEG 2972
Cdd:PRK12323 444 PGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAA--PARAAPAAAPAPADDDPPPWEELPPEFASPA--------PAQ 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2973 VDPSFLAALPEDIRREVLQNQLGIRPPSRPPPTAAPVIP------------PPVVANAGVTEVS----PEFLAALPPaiq 3036
Cdd:PRK12323 514 PDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRaaaatepvvaprPPRASASGLPDMFdgdwPALAARLPV--- 590
|
250
....*....|....*...
gi 2038296688 3037 eEVLAQQRAEQQrrELTQ 3054
Cdd:PRK12323 591 -RGLAQQLARQS--ELAG 605
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2737-3101 |
7.68e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.17 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2737 PFELS-LADQDGSGHP-------ENFPTAPSSAEGTPTSPEIVRLDPTLRAHPPEATLAQLPQG--LPADSGTEDAGLQL 2806
Cdd:PHA03247 2463 PFSLSlLLGELFPGAPvyrrpaeARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGepVHPRMLTWIRGLEE 2542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2807 MSShqEDSGpghpstegdatqmelSPAPTITSLSPERAEDSDALTavsSQLEGSPmdtsslaSGPLEDGVGEIPGIvnPE 2886
Cdd:PHA03247 2543 LAS--DDAG---------------DPPPPLPPAAPPAAPDRSVPP---PRPAPRP-------SEPAVTSRARRPDA--PP 2593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2887 QPlvvgssiAVGQQPVEPPTTGEAQPvvsqhsdESSPIAPSSELPSLRESAVTLLATDSSGILEEPLPSTSSEDEDPLAG 2966
Cdd:PHA03247 2594 QS-------ARPRAPVDDRGDPRGPA-------PPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPG 2659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2967 -INLPEGVD----PSFLAALPEDIRREVLQNQLG-----IRPP-------SRPPPTAAPVIPPPVVANAGVTEVSPEFLA 3029
Cdd:PHA03247 2660 rVSRPRRARrlgrAAQASSPPQRPRRRAARPTVGsltslADPPpppptpePAPHALVSATPLPPGPAAARQASPALPAAP 2739
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038296688 3030 ALPPAIQEEVLAQQRAEQQRRELTQSITSDT-PMDPVTfiqTLPSDLRRSVLEDMEESVLAVMPPDIAAEAQA 3101
Cdd:PHA03247 2740 APPAVPAGPATPGGPARPARPPTTAGPPAPApPAAPAA---GPPRRLTRPAVASLSESRESLPSPWDPADPPA 2809
|
|
| UBA |
pfam00627 |
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ... |
1361-1397 |
8.56e-05 |
|
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.
Pssm-ID: 395502 [Multi-domain] Cd Length: 37 Bit Score: 42.43 E-value: 8.56e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2038296688 1361 VNQQHLQQvLMDMGFTREHALEALLNTST-MEQATEYL 1397
Cdd:pfam00627 1 EDEEAIQR-LVEMGFDREQVREALRATGNnVERAAEYL 37
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
2755-3027 |
1.19e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 48.54 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2755 PTAPSSAEGTPTSPEIVRLDPTLRAHPPEATLAQLPQGLPADSGTEDAGLQLMSSHQEdsgPGHPSTEGDATQMELSPAP 2834
Cdd:PRK10263 342 QTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQ---PVQPQQPYYAPAAEQPAQQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2835 TITSLSPERAEDSDALTAVSSQlegsPMDTSSLASGPLEDGVGEIPgIVNPEQPL---VVGSSIAVGQQPVEPPTTGEAQ 2911
Cdd:PRK10263 419 PYYAPAPEQPAQQPYYAPAPEQ----PVAGNAWQAEEQQSTFAPQS-TYQTEQTYqqpAAQEPLYQQPQPVEQQPVVEPE 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2912 PVVSQHSDESSPIAPSSELPSLRESAVTLLATdssgiLEEPLPSTSSEdedplaginlPEGVDPSFLAALPEDIrrevlq 2991
Cdd:PRK10263 494 PVVEETKPARPPLYYFEEVEEKRAREREQLAA-----WYQPIPEPVKE----------PEPIKSSLKAPSVAAV------ 552
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2038296688 2992 nqlgirPPSRPPPTAAPVIP----PPVVANAGVTEVSPEF 3027
Cdd:PRK10263 553 ------PPVEAAAAVSPLASgvkkATLATGAAATVAAPVF 586
|
|
| UBA2_spUBP14_like |
cd14297 |
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ... |
1358-1401 |
4.49e-04 |
|
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.
Pssm-ID: 270483 [Multi-domain] Cd Length: 39 Bit Score: 40.54 E-value: 4.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2038296688 1358 EPQVNQqhlqqvLMDMGFTREHALEALLNT-STMEQATEYLLTHP 1401
Cdd:cd14297 1 EDLVKQ------LVDMGFTEAQARKALRKTnNNVERAVDWLFEGP 39
|
|
| UBA1_NUB1_like |
cd14291 |
UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called ... |
1362-1397 |
1.18e-03 |
|
UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called negative regulator of ubiquitin-like proteins 1, renal carcinoma antigen NY-REN-18, or protein BS4, is a NEDD8-interacting protein that can be induced by interferon. It functions as a strong post-transcriptional down-regulator of the NEDD8 expression and plays critical roles in regulating many biological events, such as cell growth, NF-kappaB signaling, and biological responses to hypoxia. NUB1 can also interact with aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) which may function in the regulation of cell cycle progression. NUB1 contains three ubiquitin-associated domains (UBA), a bipartite nuclear localization signal (NLS) and a PEST motif. This model corresponds to UBA1 domain.
Pssm-ID: 270477 [Multi-domain] Cd Length: 36 Bit Score: 38.97 E-value: 1.18e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2038296688 1362 NQQHLQQvLMDMGFTREHALEALLNTS-TMEQATEYL 1397
Cdd:cd14291 1 DEDKLQQ-LMEMGFSEAEARLALRACNgNVERAVDYI 36
|
|
| UBA |
cd14270 |
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ... |
1368-1395 |
2.11e-03 |
|
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ubiquitin-associated (UBA) domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only the bind UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains.
Pssm-ID: 270456 [Multi-domain] Cd Length: 30 Bit Score: 38.10 E-value: 2.11e-03
10 20
....*....|....*....|....*....
gi 2038296688 1368 QVLMDMGFTREHALEALLNTS-TMEQATE 1395
Cdd:cd14270 2 AQLVEMGFSREQARRALRATNgDVEAAVE 30
|
|
| UBA_VP13D |
cd14306 |
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ... |
1368-1400 |
2.29e-03 |
|
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required.
Pssm-ID: 270491 Cd Length: 36 Bit Score: 38.19 E-value: 2.29e-03
10 20 30
....*....|....*....|....*....|....
gi 2038296688 1368 QVLMDMGFTREHALEALLNTS-TMEQATEYLLTH 1400
Cdd:cd14306 2 AKLMELGFPEEDCIRALRACGgNVEEAANWLLEN 35
|
|
| UBA_UBXN1 |
cd14302 |
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ... |
1368-1400 |
2.56e-03 |
|
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also called SAPK substrate protein 1 (SAKS1) or UBA/UBX 33.3 kDa protein, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (UBX) domain. It binds polyubiquitin and valosin-containing protein (VCP), and has been identified as a substrate for stress-activated protein kinases (SAPKs). Moreover, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and may be involved in the Ub-proteasome proteolytic pathways. In addition, UBXN1 can associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domain.
Pssm-ID: 270487 [Multi-domain] Cd Length: 41 Bit Score: 38.43 E-value: 2.56e-03
10 20 30
....*....|....*....|....*....|....*
gi 2038296688 1368 QVLMDMGFTREHALEALLNTST--MEQATEYLLTH 1400
Cdd:cd14302 4 QTLIEMGFSRNRAEKALAKTGNqgVEAAMEWLLAH 38
|
|
| UBA1_scUBP14_like |
cd14296 |
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ... |
1364-1400 |
2.57e-03 |
|
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.
Pssm-ID: 270482 [Multi-domain] Cd Length: 39 Bit Score: 38.38 E-value: 2.57e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2038296688 1364 QHLQQVLMDMGFTREHALEALLNT--STMEQATEYLLTH 1400
Cdd:cd14296 1 EEAVSQLMSMGFSENAAKRALYYTgnSSVEAAMNWLFEH 39
|
|
| PRK14949 |
PRK14949 |
DNA polymerase III subunits gamma and tau; Provisional |
2795-3066 |
2.76e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237863 [Multi-domain] Cd Length: 944 Bit Score: 43.95 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2795 ADSGTEDAGLQLMSSHQEDSGPGHPSTEGDATQMELSPAPTITSLSPeRAEDSDALTAVssqlegspmdtssLAS-GPLE 2873
Cdd:PRK14949 558 AFSSESYNALSDDEQHSANVQSAQSAAEAQPSSQSLSPISAVTTAAA-SLADDDILDAV-------------LAArDSLL 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2874 DGVGEIpgivNPEQPLvvGSSIAVGQQPVEPPttgEAQPVVSQHSDESSPiaPSSELPSLRESAVTLLATDSSGILEEPL 2953
Cdd:PRK14949 624 SDLDAL----SPKEGD--GKKSSADRKPKTPP---SRAPPASLSKPASSP--DASQTSASFDLDPDFELATHQSVPEAAL 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038296688 2954 PSTSSEDEDPlaginlpegvdpsflAALPEDirrevlqnqlgiRPPSRPPPTAAPVIPPPVVANAGVTEVSPEF-----L 3028
Cdd:PRK14949 693 ASGSAPAPPP---------------VPDPYD------------RPPWEEAPEVASANDGPNNAAEGNLSESVEDasnseL 745
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2038296688 3029 AALPPAI--QEEVLAQQRAEQQRRELTQSITSDTPMDPVT 3066
Cdd:PRK14949 746 QAVEQQAthQPQVQAEAQSPASTTALTQTSSEVQDTELNL 785
|
|
| UBA_TNR6C |
cd14283 |
UBA domain found in trinucleotide repeat-containing gene 6C protein (TNRC6C) and similar ... |
1364-1399 |
3.30e-03 |
|
UBA domain found in trinucleotide repeat-containing gene 6C protein (TNRC6C) and similar proteins; TNRC6C is one of three GW182 paralogs in mammalian genomes. It is enriched in P-bodies and important for efficient miRNA-mediated repression. TNRC6C is composed of an N-terminal glycine/tryptophan (G/W)-rich region containing an Ago hook responsible for Ago protein-binding; a ubiquitin-associated (UBA) domain and a glutamine (Q)-rich region in the middle region; a middle G/W-rich region, a RNA recognition motif (RRM), also called RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal G/W-rich region, at the C-terminus. A bipartite C-terminal region including the middle and C-terminal G/W-rich regions is referred as silencing domain that triggers silencing of bound transcripts by inhibiting protein expression and promoting mRNA decay via deadenylation. The C-terminal half containing the RRM domain functions as a key effector domain mediating protein synthesis repression by TNRC6C.
Pssm-ID: 270469 Cd Length: 38 Bit Score: 37.87 E-value: 3.30e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2038296688 1364 QHLQQvLMDMGFTREHALEAL-LNTSTMEQATEYLLT 1399
Cdd:cd14283 2 RLLKQ-LTDMGFKREPAEEALkSNNMNLEQAVSALLS 37
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
2973-2991 |
6.28e-03 |
|
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, the second ubiquitin-binding motif of Rev1, a DNA damage tolerance protein. Rev1 acts as a translesion synthesis (TLS) DNA polymerase and may also recruit other TLS polymerases to the site of DNA damage; in that process the UBMs are essential for Rev1 function, triggering TLS activation via recognition of ubiquitin moieties in PCNA, the proliferating cell nuclear antigen.
Pssm-ID: 412037 Cd Length: 36 Bit Score: 37.20 E-value: 6.28e-03
|
| UBA1_atUBP14 |
cd14295 |
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ... |
1362-1400 |
6.86e-03 |
|
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and similar proteins; atUBP14, also called deubiquitinating enzyme 14, TITAN-6 protein, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is related to the isopeptidase T class of deubiquitinating enzymes that recycle polyubiquitin chains following protein degradation. atUBP14 is essential for early plant development. It can disassemble multi-ubiquitin chains linked internally via epsilon-amino isopeptide bonds using Lys48 and can process some, but not all, translational fusions of ubiquitin linked via alpha-amino peptide bonds. atUBP14 contains two ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.
Pssm-ID: 270481 [Multi-domain] Cd Length: 45 Bit Score: 37.35 E-value: 6.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2038296688 1362 NQQHLQQvLMDMGFTREHALEALLNTSTM--EQATEYLLTH 1400
Cdd:cd14295 1 DQELVAQ-LMEMGFPKVRAEKALFFTQNKglEEAMEWLEEH 40
|
|
| |
