|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
4772-5125 |
2.18e-148 |
|
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: 466.27 E-value: 2.18e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4772 VSVRRVTVFEDSFRVLYRLGPEEWKNRFYIVFEDEEGQDAGGLLREWYVIISREIFNPMYALFCVSPGDRVTYMINPSSH 4851
Cdd:cd00078 3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4852 ANPNHLSYFKFVGRVIAKAVHDNKLLECYFTRSFYKHILGKQVKHTDMESQDYEFYKGLDYLMKNDISTLGYELTFSTEV 4931
Cdd:cd00078 83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4932 QE-FGVTQIRDLKPNGRDTAVTEENKFEYVQLVCQLKMSGSIRQQLDAFLEGFYDIIPKHLISIFNEQELELLISGLPDI 5010
Cdd:cd00078 163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 5011 DIEDLKANTEY-HKYTSKSAQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFGSLEgmngiQKFQIHRDDRSTDRLP 5089
Cdd:cd00078 243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 599138015 5090 CAHTCFNQLDLPMYKSYDKLRSCLLKAIHECsEGFG 5125
Cdd:cd00078 318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
|
|
| DUF913 |
pfam06025 |
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ... |
622-990 |
1.40e-77 |
|
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin protein ligases.
:
Pssm-ID: 461803 Cd Length: 369 Bit Score: 263.71 E-value: 1.40e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 622 QRAALLKSMLNFLKKSIQDHA-HFSN-MRNIMETS-LTQSLRHIIANAEYYGPSLFLLATDVVTVYVFNEPSLLSSLQDL 698
Cdd:pfam06025 66 YRQQLLKWLLKFIHHMMQHSGgGTDRlLRNLIDSSqLLGSLRKIIENAKVFGSSVWSLAVNILSDFIHNEPTSFAVIQEA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 699 GITSVMLKALLQKDVPATREVLGSLPNVFSALCLNERGLFEFLSYDPFDKVLKVLLSPDYLVAMRrrrssdPLGDTATNL 778
Cdd:pfam06025 146 GLSKAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNALESFFEIFESPDHVKAME------TDGELASNL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 779 GNAMDDLIKHHPYLRADATEAIVRLLNELVRLGSDPSficwrankessgsgsgsgshggghhVASTPSPMVMVAGTGSAS 858
Cdd:pfam06025 220 GSSFDELVRHHPSLKPAIINAVIDMLARVVELGSTKA-------------------------EPDGWGAKLWVGCSSSSS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 859 SVLQGAAdtndssgdddddddemssasqqqqqpttpgqgggPSTPRTQQAGGVVGSGAGATGTPAAASQAVKVVTPPERE 938
Cdd:pfam06025 275 FSPASSG----------------------------------SLPMETDGESGDESSSDEDVEMEDAPDTDSTEETEPESH 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 599138015 939 AIPLIDYILNVMKFIEAIFSNSPngdHCREFVLHGGLKPILQLLSLPNLPVD 990
Cdd:pfam06025 321 GNSLTDYIDNVARFLEAFFSNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
|
|
| WWE |
smart00678 |
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ... |
1757-1829 |
4.78e-22 |
|
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;
:
Pssm-ID: 128922 [Multi-domain] Cd Length: 73 Bit Score: 92.79 E-value: 4.78e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 599138015 1757 VWRWYDAStGKWNAYSEANNELIRNAYAAGERWLYINIGRQRCTVSLNCMTQVSEASGTHRPVCPALKLSEAI 1829
Cdd:smart00678 2 VWEYEGRN-GKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYSPYSK 73
|
|
| DUF908 super family |
cl20318 |
Domain of Unknown Function (DUF908); |
90-326 |
2.99e-09 |
|
Domain of Unknown Function (DUF908);
The actual alignment was detected with superfamily member pfam06012:
Pssm-ID: 428721 Cd Length: 351 Bit Score: 62.35 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 90 DVTLLLHVLNFTTLLIEHSFSRHLYNSIEHLTVLLSSQNMDIVLAVLNLL------Y------MFSKRSNFIPRLPFEKK 157
Cdd:pfam06012 2 DRELVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLlrlaqrYsasnsrRGSAPRHIQQSLLANHY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 158 ELLIVKLFNIAERWGDPN------------------YGLSLKDCCIGEPK--------LEFLY----------------- 194
Cdd:pfam06012 82 NIDLDRLLKLAQPFPKPPppdstdpapsttknsaneYANDLVSLAKEDSKvlpsewgsVKFTYypssssdeaptssksst 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 195 ------------------------------QLCIDYVDEHGHAAQLEIPDMmdlcHTASAP--EVIKTIAGQIskPSEAi 242
Cdd:pfam06012 162 ssnsspstptplrrsstlgtspdspsspstSTPSSAADSDEGLRTFEIPES----KVASKSleDILAKAIEDL--PKES- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 243 KMRIAHRVRLISGFNN--YKLRLQFVQARLQAVSILIYSNALQDNTDKVLYA--GFGEELCELIDKEDVHLVEIRAAVLR 318
Cdd:pfam06012 235 RFELLHRIRIAKALNSssEESRQQLLAIRLLAIANLAYIHPESTFQTKLFEYdpDLVYQLAELIHPDTEVPLELQTAALY 314
|
....*...
gi 599138015 319 TLTSMLHF 326
Cdd:pfam06012 315 ALEALARH 322
|
|
| UBA_like_SF super family |
cl21463 |
UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains ... |
1468-1507 |
7.59e-09 |
|
UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains alpha-helical structural homology ubiquitin-binding domains, including UBA domains and coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domains which share a common three-helical bundle architecture. 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 bind the 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. CUE domain containing proteins are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. This superfamily also includes many UBA-like domains found in AMP-activated protein kinase (AMPK) related kinases, the NXF family of mRNA nuclear export factors, elongation factor Ts (EF-Ts), nascent polypeptide-associated complex subunit alpha (NACA) and similar proteins. Although many UBA-like domains may have a conserved TG but not GF/Y-loop, they still show a high level of structural and sequence similarity with three-helical ubiquitin binding domains.
The actual alignment was detected with superfamily member cd14288:
Pssm-ID: 473871 Cd Length: 40 Bit Score: 54.33 E-value: 7.59e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 599138015 1468 LNADHIKTLTDMGFMHYHVIEALRTNASLEEATDYLLNNP 1507
Cdd:cd14288 1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP 40
|
|
| DUF5585 super family |
cl39316 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
3264-3648 |
7.21e-07 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
The actual alignment was detected with superfamily member pfam17823:
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 55.74 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3264 ATSDATTTTGGPTRNFSSvdSNVSSET---QTTTRPPRQRGGlrqqsqlpfniyaeidltnEQDSEGDRSTSTTTgtaad 3340
Cdd:pfam17823 66 APAPVTLTKGTSAAHLNS--TEVTAEHtphGTDLSEPATREG-------------------AADGAASRALAAAA----- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3341 gAESQSQHNSSSTAAQVAVPQHQRHPP---VPLLPSSGRPSRPHTRLDETELLLLQLTDRQIRNRLQGSSGHTNSSRTSG 3417
Cdd:pfam17823 120 -SSSPSSAAQSLPAAIAALPSEAFSAPraaACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3418 --SALINARPNRDLPACLQRHDHPAGSIFPRPSANRTPAP-TLVSMPTPMSNAALEQL--------------NVTAPDVV 3480
Cdd:pfam17823 199 asSAPATLTPARGISTAATATGHPAAGTALAAVGNSSPAAgTVTAAVGTVTPAALATLaaaagtvasaagtiNMGDPHAR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3481 RTDRNFALPSSLEVDVDVLPGivdlpQQEAQPEDDQLLLPPPPPPPPSDTTPlVHAEDDLWPGTVVSAGTreeSSAPAVA 3560
Cdd:pfam17823 279 RLSPAKHMPSDTMARNPAAPM-----GAQAQGPIIQVSTDQPVHNTAGEPTP-SPSNTTLEPNTPKSVAS---TNLAVVT 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3561 TESTEAVNESNQPEPTPESSESTSPNPQAPSAEPTPLEPgaaVDASVGAQTPATTEEAASTAGAsGTTATitdmSPEVRA 3640
Cdd:pfam17823 350 TTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSPLLP---TQGAAGPGILLAPEQVATEATA-GTASA----GPTPRS 421
|
....*...
gi 599138015 3641 AlGDLEVP 3648
Cdd:pfam17823 422 S-GDPKTL 428
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
3646-3676 |
9.78e-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: 9.78e-07
10 20 30
....*....|....*....|....*....|.
gi 599138015 3646 EVPEGVDPSFLAALPSEMREEVIQEHLRMQR 3676
Cdd:pfam14377 3 PPPEGIDPSFLAALPPDLRQEVLAQQDDERL 33
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
3695-3722 |
2.08e-05 |
|
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: 44.03 E-value: 2.08e-05
10 20
....*....|....*....|....*...
gi 599138015 3695 EVNPEFLAALPLNIQSEVLMQQRIEQQR 3722
Cdd:pfam14377 7 GIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
4772-5125 |
2.18e-148 |
|
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: 466.27 E-value: 2.18e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4772 VSVRRVTVFEDSFRVLYRLGPEEWKNRFYIVFEDEEGQDAGGLLREWYVIISREIFNPMYALFCVSPGDRVTYMINPSSH 4851
Cdd:cd00078 3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4852 ANPNHLSYFKFVGRVIAKAVHDNKLLECYFTRSFYKHILGKQVKHTDMESQDYEFYKGLDYLMKNDISTLGYELTFSTEV 4931
Cdd:cd00078 83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4932 QE-FGVTQIRDLKPNGRDTAVTEENKFEYVQLVCQLKMSGSIRQQLDAFLEGFYDIIPKHLISIFNEQELELLISGLPDI 5010
Cdd:cd00078 163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 5011 DIEDLKANTEY-HKYTSKSAQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFGSLEgmngiQKFQIHRDDRSTDRLP 5089
Cdd:cd00078 243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 599138015 5090 CAHTCFNQLDLPMYKSYDKLRSCLLKAIHECsEGFG 5125
Cdd:cd00078 318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
4796-5124 |
4.82e-140 |
|
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: 441.29 E-value: 4.82e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4796 KNRFYIVFEDEEGQDAGGLLREWYVIISREIFNPMYALFCVSPGDRVTYMINPSSHANPNHLSYFKFVGRVIAKAVHDNK 4875
Cdd:smart00119 4 KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHLSYFRFIGRVLGKALYDNR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4876 LLECYFTRSFYKHILGKQVKHTDMESQDYEFYKGLDYL-MKNDISTLgYELTFSTEVQE-FGVTQIRDLKPNGRDTAVTE 4953
Cdd:smart00119 84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSIVLTSeFGQVKVVELKPGGSNIPVTE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4954 ENKFEYVQLVCQLKMSGSIRQQLDAFLEGFYDIIPKHLISIFNEQELELLISGLPDIDIEDLKANTEY-HKYTSKSAQIQ 5032
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYkGGYSANSQTIK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 5033 WFWRALRSFDQADRAKFLQFVTGTSKVPLQGFGSLEGmngiqKFQIHRDDRSTDRLPCAHTCFNQLDLPMYKSYDKLRSC 5112
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317
|
330
....*....|..
gi 599138015 5113 LLKAIHECsEGF 5124
Cdd:smart00119 318 LLLAINEG-KGF 328
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
4733-5127 |
8.71e-137 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 453.45 E-value: 8.71e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4733 GPFAVLVDHTRILDFDVKRKYFQTELERLDEGIRREEHtVSVRRVTVFEDSFRVLYRLGPEEWKNRFYIVFEDEEGQDAG 4812
Cdd:COG5021 479 GSFISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDPYLH-IKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIDAG 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4813 GLLREWYVIISREIFNPMYALFCVSPGDRVTYMINPSSHANPNHLSYFKFVGRVIAKAVHDNKLLECYFTRSFYKHILGK 4892
Cdd:COG5021 558 GLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGK 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4893 QVKHTDMESQDYEFYKGLDYLMKNDISTLGYELTFSTEVQEFGVTQIRDLKPNGRDTAVTEENKFEYVQLVCQLKMSGSI 4972
Cdd:COG5021 638 PVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRV 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4973 RQQLDAFLEGFYDIIPKHLISIFNEQELELLISGLPD-IDIEDLKANTEYHKYTSKSAQIQWFWRALRSFDQADRAKFLQ 5051
Cdd:COG5021 718 EKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQ 797
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 599138015 5052 FVTGTSKVPLQGFGSLEGMNGIQKFQIHRDDRSTDRLPCAHTCFNQLDLPMYKSYDKLRSCLLKAIHECSeGFGFA 5127
Cdd:COG5021 798 FVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGA-GFGLL 872
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
4821-5127 |
6.26e-114 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 365.39 E-value: 6.26e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4821 IISREIFNPMYALFCVSPGDRVTYMINPSSHANPNH--LSYFKFVGRVIAKAVHDNKLLECYFTRSFYKHILGKQVKHTD 4898
Cdd:pfam00632 2 LLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4899 MESQDYEFYKGLDYLMKNDISTLG-YELTFSteVQEFGVTQIRDLKPNGRDTAVTEENKFEYVQLVCQLKMSGSIRQQLD 4977
Cdd:pfam00632 82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4978 AFLEGFYDIIPKHLISIFNEQELELLISGLPDIDIEDLKANTEY-HKYTSKSAQIQWFWRALRSFDQADRAKFLQFVTGT 5056
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYdGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 599138015 5057 SKVPLQGFGSLegmngiQKFQIHR-DDRSTDRLPCAHTCFNQLDLPMYKSYDKLRSCLLKAIHECsEGFGFA 5127
Cdd:pfam00632 240 SRLPVGGFKSL------PKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
|
|
| DUF913 |
pfam06025 |
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ... |
622-990 |
1.40e-77 |
|
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin protein ligases.
Pssm-ID: 461803 Cd Length: 369 Bit Score: 263.71 E-value: 1.40e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 622 QRAALLKSMLNFLKKSIQDHA-HFSN-MRNIMETS-LTQSLRHIIANAEYYGPSLFLLATDVVTVYVFNEPSLLSSLQDL 698
Cdd:pfam06025 66 YRQQLLKWLLKFIHHMMQHSGgGTDRlLRNLIDSSqLLGSLRKIIENAKVFGSSVWSLAVNILSDFIHNEPTSFAVIQEA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 699 GITSVMLKALLQKDVPATREVLGSLPNVFSALCLNERGLFEFLSYDPFDKVLKVLLSPDYLVAMRrrrssdPLGDTATNL 778
Cdd:pfam06025 146 GLSKAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNALESFFEIFESPDHVKAME------TDGELASNL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 779 GNAMDDLIKHHPYLRADATEAIVRLLNELVRLGSDPSficwrankessgsgsgsgshggghhVASTPSPMVMVAGTGSAS 858
Cdd:pfam06025 220 GSSFDELVRHHPSLKPAIINAVIDMLARVVELGSTKA-------------------------EPDGWGAKLWVGCSSSSS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 859 SVLQGAAdtndssgdddddddemssasqqqqqpttpgqgggPSTPRTQQAGGVVGSGAGATGTPAAASQAVKVVTPPERE 938
Cdd:pfam06025 275 FSPASSG----------------------------------SLPMETDGESGDESSSDEDVEMEDAPDTDSTEETEPESH 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 599138015 939 AIPLIDYILNVMKFIEAIFSNSPngdHCREFVLHGGLKPILQLLSLPNLPVD 990
Cdd:pfam06025 321 GNSLTDYIDNVARFLEAFFSNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
|
|
| WWE |
smart00678 |
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ... |
1757-1829 |
4.78e-22 |
|
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;
Pssm-ID: 128922 [Multi-domain] Cd Length: 73 Bit Score: 92.79 E-value: 4.78e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 599138015 1757 VWRWYDAStGKWNAYSEANNELIRNAYAAGERWLYINIGRQRCTVSLNCMTQVSEASGTHRPVCPALKLSEAI 1829
Cdd:smart00678 2 VWEYEGRN-GKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYSPYSK 73
|
|
| WWE |
pfam02825 |
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ... |
1757-1820 |
7.08e-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: 66.55 E-value: 7.08e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 599138015 1757 VWRWYDaSTGKWNAYSEANNELIRNAYAAGERW--LYINIGRQRCTVSLNCMTQVSEASGTHRPVC 1820
Cdd:pfam02825 1 VWEWED-DNGGWHPYDPEVSSLIEEAYQKGKPSvdLSITTAGFPYTIDFKSMTQTNKDTGTTRPVR 65
|
|
| DUF908 |
pfam06012 |
Domain of Unknown Function (DUF908); |
90-326 |
2.99e-09 |
|
Domain of Unknown Function (DUF908);
Pssm-ID: 428721 Cd Length: 351 Bit Score: 62.35 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 90 DVTLLLHVLNFTTLLIEHSFSRHLYNSIEHLTVLLSSQNMDIVLAVLNLL------Y------MFSKRSNFIPRLPFEKK 157
Cdd:pfam06012 2 DRELVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLlrlaqrYsasnsrRGSAPRHIQQSLLANHY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 158 ELLIVKLFNIAERWGDPN------------------YGLSLKDCCIGEPK--------LEFLY----------------- 194
Cdd:pfam06012 82 NIDLDRLLKLAQPFPKPPppdstdpapsttknsaneYANDLVSLAKEDSKvlpsewgsVKFTYypssssdeaptssksst 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 195 ------------------------------QLCIDYVDEHGHAAQLEIPDMmdlcHTASAP--EVIKTIAGQIskPSEAi 242
Cdd:pfam06012 162 ssnsspstptplrrsstlgtspdspsspstSTPSSAADSDEGLRTFEIPES----KVASKSleDILAKAIEDL--PKES- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 243 KMRIAHRVRLISGFNN--YKLRLQFVQARLQAVSILIYSNALQDNTDKVLYA--GFGEELCELIDKEDVHLVEIRAAVLR 318
Cdd:pfam06012 235 RFELLHRIRIAKALNSssEESRQQLLAIRLLAIANLAYIHPESTFQTKLFEYdpDLVYQLAELIHPDTEVPLELQTAALY 314
|
....*...
gi 599138015 319 TLTSMLHF 326
Cdd:pfam06012 315 ALEALARH 322
|
|
| UBA_HUWE1 |
cd14288 |
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ... |
1468-1507 |
7.59e-09 |
|
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: 54.33 E-value: 7.59e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 599138015 1468 LNADHIKTLTDMGFMHYHVIEALRTNASLEEATDYLLNNP 1507
Cdd:cd14288 1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP 40
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
3264-3648 |
7.21e-07 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 55.74 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3264 ATSDATTTTGGPTRNFSSvdSNVSSET---QTTTRPPRQRGGlrqqsqlpfniyaeidltnEQDSEGDRSTSTTTgtaad 3340
Cdd:pfam17823 66 APAPVTLTKGTSAAHLNS--TEVTAEHtphGTDLSEPATREG-------------------AADGAASRALAAAA----- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3341 gAESQSQHNSSSTAAQVAVPQHQRHPP---VPLLPSSGRPSRPHTRLDETELLLLQLTDRQIRNRLQGSSGHTNSSRTSG 3417
Cdd:pfam17823 120 -SSSPSSAAQSLPAAIAALPSEAFSAPraaACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3418 --SALINARPNRDLPACLQRHDHPAGSIFPRPSANRTPAP-TLVSMPTPMSNAALEQL--------------NVTAPDVV 3480
Cdd:pfam17823 199 asSAPATLTPARGISTAATATGHPAAGTALAAVGNSSPAAgTVTAAVGTVTPAALATLaaaagtvasaagtiNMGDPHAR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3481 RTDRNFALPSSLEVDVDVLPGivdlpQQEAQPEDDQLLLPPPPPPPPSDTTPlVHAEDDLWPGTVVSAGTreeSSAPAVA 3560
Cdd:pfam17823 279 RLSPAKHMPSDTMARNPAAPM-----GAQAQGPIIQVSTDQPVHNTAGEPTP-SPSNTTLEPNTPKSVAS---TNLAVVT 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3561 TESTEAVNESNQPEPTPESSESTSPNPQAPSAEPTPLEPgaaVDASVGAQTPATTEEAASTAGAsGTTATitdmSPEVRA 3640
Cdd:pfam17823 350 TTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSPLLP---TQGAAGPGILLAPEQVATEATA-GTASA----GPTPRS 421
|
....*...
gi 599138015 3641 AlGDLEVP 3648
Cdd:pfam17823 422 S-GDPKTL 428
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
3646-3676 |
9.78e-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: 9.78e-07
10 20 30
....*....|....*....|....*....|.
gi 599138015 3646 EVPEGVDPSFLAALPSEMREEVIQEHLRMQR 3676
Cdd:pfam14377 3 PPPEGIDPSFLAALPPDLRQEVLAQQDDERL 33
|
|
| UBA |
pfam00627 |
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ... |
1469-1503 |
1.58e-05 |
|
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.
Pssm-ID: 395502 [Multi-domain] Cd Length: 37 Bit Score: 44.74 E-value: 1.58e-05
10 20 30
....*....|....*....|....*....|....*.
gi 599138015 1469 NADHIKTLTDMGFMHYHVIEALR-TNASLEEATDYL 1503
Cdd:pfam00627 2 DEEAIQRLVEMGFDREQVREALRaTGNNVERAAEYL 37
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
3695-3722 |
2.08e-05 |
|
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: 44.03 E-value: 2.08e-05
10 20
....*....|....*....|....*...
gi 599138015 3695 EVNPEFLAALPLNIQSEVLMQQRIEQQR 3722
Cdd:pfam14377 7 GIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| PHA01929 |
PHA01929 |
putative scaffolding protein |
3555-3775 |
6.00e-05 |
|
putative scaffolding protein
Pssm-ID: 177328 Cd Length: 306 Bit Score: 48.51 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3555 SAPAVATESTEAVNESNQPEPTPESSESTSPNPQAPsAEPTPLEP---GAAVDASVGAQTPATTEEAASTAgasGTTATI 3631
Cdd:PHA01929 39 VQPGQPGAPQQLAIPTQQPQPVPTSAMTPHVVQQAP-AQPAPAAPpaaGAALPEALEVPPPPAFTPNGEIV---GTLAGN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3632 TDMSPEVRAALGDLEVPEGVDPSFLAALPSEMREE----VIQEHLRMQRIRQRAQQNAIQIAHDSLVEVNPEFLAALpln 3707
Cdd:PHA01929 115 LEGDPQLAPSVSYLEAFSGLDKLDTVRAFGKAAENrdprFIDTHYLKEVLGEAQAQHVINVAKGVLTYVDAQTKAVV--- 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 599138015 3708 iqsevlmqqrieqqRQAAQTANPEDPVDTAA--FFQNLPENLRQAILTDMEESQIASLppELAAE--AQFLR 3775
Cdd:PHA01929 192 --------------NETYAAVGGEAVWKQAAglFNQKADPATRAAIGRLMNSGDAQAM--QYAAKqvAAFAQ 247
|
|
| PRK12495 |
PRK12495 |
hypothetical protein; Provisional |
3542-3658 |
6.59e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 183558 [Multi-domain] Cd Length: 226 Bit Score: 47.56 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3542 PGTVVSAGTREESSAPAVATESTEAVNESNQPEPTPESSESTSPNPQAPSAEPTPLEPGAAVD--ASVGAQTPATTEEAA 3619
Cdd:PRK12495 67 PVTEDGAAGDDAGDGAEATAPSDAGSQASPDDDAQPAAEAEAADQSAPPEASSTSATDEAATDppATAAARDGPTPDPTA 146
|
90 100 110
....*....|....*....|....*....|....*....
gi 599138015 3620 STAGASGTTATITDMSPEVRAAlGDLEVPEGVDPSFLAA 3658
Cdd:PRK12495 147 QPATPDERRSPRQRPPVSGEPP-TPSTPDAHVAGTLQAA 184
|
|
| rad23 |
TIGR00601 |
UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
3546-3771 |
7.51e-05 |
|
UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273167 [Multi-domain] Cd Length: 378 Bit Score: 48.74 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3546 VSAGTREESSAPAVATESTeavnesNQPEPTPESSESTSPNPQAPSAEPTPLEPGAAVDASVGAQTPATTEEAAST--AG 3623
Cdd:TIGR00601 80 GTGKVAPPAATPTSAPTPT------PSPPASPASGMSAAPASAVEEKSPSEESATATAPESPSTSVPSSGSDAASTlvVG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3624 ASGTTAT--ITDM---SPEVRAAL-GDLEVPEGVDPSFLAALPSEMREEVIQEHLrmqrirQRAQQNAI--QIAHDSLVE 3695
Cdd:TIGR00601 154 SERETTIeeIMEMgyeREEVERALrAAFNNPDRAVEYLLTGIPEDPEQPEPVQQT------AASTAAATteTPQHGSVFE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3696 V-------NPEFLAALPLNIQSEVLMQQRIEQQRQAAQtANPEdpvDTAAFFQNL-PEN--LRQAILTDMEE-SQIASLP 3764
Cdd:TIGR00601 228 QaaqggteQPATEAAQGGNPLEFLRNQPQFQQLRQVVQ-QNPQ---LLPPLLQQIgQENpqLLQQISQHPEQfLQMLNEP 303
|
....*..
gi 599138015 3765 PELAAEA 3771
Cdd:TIGR00601 304 VGELASE 310
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
3651-3675 |
5.67e-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: 37.59 E-value: 5.67e-03
10 20
....*....|....*....|....*
gi 599138015 3651 VDPSFLAALPSEMREEVIQEHLRMQ 3675
Cdd:cd19318 12 VDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HECTc |
cd00078 |
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
4772-5125 |
2.18e-148 |
|
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: 466.27 E-value: 2.18e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4772 VSVRRVTVFEDSFRVLYRLGPEEWKNRFYIVFEDEEGQDAGGLLREWYVIISREIFNPMYALFCVSPGDRVTYMINPSSH 4851
Cdd:cd00078 3 ITVRRDRILEDALRQLSKVSSSDLKKVLEVEFVGEEGIDAGGVTREFFTLVSKELFNPSYGLFRYTPDDSGLLYPNPSSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4852 ANPNHLSYFKFVGRVIAKAVHDNKLLECYFTRSFYKHILGKQVKHTDMESQDYEFYKGLDYLMKNDISTLGYELTFSTEV 4931
Cdd:cd00078 83 ADEDHLKLFRFLGRLLGKALYEGRLLDLPFSRAFYKKLLGKPLSLEDLEELDPELYKSLKELLDNDGDEDDLELTFTIEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4932 QE-FGVTQIRDLKPNGRDTAVTEENKFEYVQLVCQLKMSGSIRQQLDAFLEGFYDIIPKHLISIFNEQELELLISGLPDI 5010
Cdd:cd00078 163 DSsFGGAVTVELKPGGRDIPVTNENKEEYVDLYVDYRLNKGIEEQVEAFRDGFSEVIPEELLSLFTPEELELLICGSEDI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 5011 DIEDLKANTEY-HKYTSKSAQIQWFWRALRSFDQADRAKFLQFVTGTSKVPLQGFGSLEgmngiQKFQIHRDDRSTDRLP 5089
Cdd:cd00078 243 DLEDLKKNTEYkGGYSSDSPTIQWFWEVLESFTNEERKKFLQFVTGSSRLPVGGFADLN-----PKFTIRRVGSPDDRLP 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 599138015 5090 CAHTCFNQLDLPMYKSYDKLRSCLLKAIHECsEGFG 5125
Cdd:cd00078 318 TAHTCFNLLKLPPYSSKEILREKLLYAINEG-AGFG 352
|
|
| HECTc |
smart00119 |
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
4796-5124 |
4.82e-140 |
|
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: 441.29 E-value: 4.82e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4796 KNRFYIVFEDEEGQDAGGLLREWYVIISREIFNPMYALFCVSPGDRVTYMINPSSHANPNHLSYFKFVGRVIAKAVHDNK 4875
Cdd:smart00119 4 KRVLEIEFEGEEGLDGGGVTREFFFLLSKELFNPDYGLFRYSPNDYLLYPNPRSGFANEEHLSYFRFIGRVLGKALYDNR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4876 LLECYFTRSFYKHILGKQVKHTDMESQDYEFYKGLDYL-MKNDISTLgYELTFSTEVQE-FGVTQIRDLKPNGRDTAVTE 4953
Cdd:smart00119 84 LLDLFFARPFYKKLLGKPVTLHDLESLDPELYKSLKWLlLNNDTSEE-LDLTFSIVLTSeFGQVKVVELKPGGSNIPVTE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4954 ENKFEYVQLVCQLKMSGSIRQQLDAFLEGFYDIIPKHLISIFNEQELELLISGLPDIDIEDLKANTEY-HKYTSKSAQIQ 5032
Cdd:smart00119 163 ENKKEYVHLVIEYRLNKGIEKQLEAFREGFSEVIPENLLKLFDPEELELLICGSPEIDVDDLKSNTEYkGGYSANSQTIK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 5033 WFWRALRSFDQADRAKFLQFVTGTSKVPLQGFGSLEGmngiqKFQIHRDDRSTDRLPCAHTCFNQLDLPMYKSYDKLRSC 5112
Cdd:smart00119 243 WFWEVVESFTNEERRKLLQFVTGSSRLPVGGFAALSP-----KFTIRKAGSDDERLPTAHTCFNRLKLPPYSSKEILREK 317
|
330
....*....|..
gi 599138015 5113 LLKAIHECsEGF 5124
Cdd:smart00119 318 LLLAINEG-KGF 328
|
|
| HUL4 |
COG5021 |
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
4733-5127 |
8.71e-137 |
|
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 453.45 E-value: 8.71e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4733 GPFAVLVDHTRILDFDVKRKYFQTELERLDEGIRREEHtVSVRRVTVFEDSFRVLYRLGPEEWKNRFYIVFEDEEGQDAG 4812
Cdd:COG5021 479 GSFISLNKLDIRRIKEDKRRKLFYSLKQKAKIFDPYLH-IKVRRDRVFEDSYREIMDESGDDLKKTLEIEFVGEEGIDAG 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4813 GLLREWYVIISREIFNPMYALFCVSPGDRVTYMINPSSHANPNHLSYFKFVGRVIAKAVHDNKLLECYFTRSFYKHILGK 4892
Cdd:COG5021 558 GLTREWLFLLSKEMFNPDYGLFEYITEDLYTLPINPLSSINPEHLSYFKFLGRVIGKAIYDSRILDVQFSKAFYKKLLGK 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4893 QVKHTDMESQDYEFYKGLDYLMKNDISTLGYELTFSTEVQEFGVTQIRDLKPNGRDTAVTEENKFEYVQLVCQLKMSGSI 4972
Cdd:COG5021 638 PVSLVDLESLDPELYRSLVWLLNNDIDETILDLTFTVEDDSFGESRTVELIPNGRNISVTNENKKEYVKKVVDYKLNKRV 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4973 RQQLDAFLEGFYDIIPKHLISIFNEQELELLISGLPD-IDIEDLKANTEYHKYTSKSAQIQWFWRALRSFDQADRAKFLQ 5051
Cdd:COG5021 718 EKQFSAFKSGFSEIIPPDLLQIFDESELELLIGGIPEdIDIDDWKSNTAYHGYTEDSPIIVWFWEIISEFDFEERAKLLQ 797
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 599138015 5052 FVTGTSKVPLQGFGSLEGMNGIQKFQIHRDDRSTDRLPCAHTCFNQLDLPMYKSYDKLRSCLLKAIHECSeGFGFA 5127
Cdd:COG5021 798 FVTGTSRIPINGFKDLQGSDGVRKFTIEKGGTDDDRLPSAHTCFNRLKLPEYSSKEKLRSKLLTAINEGA-GFGLL 872
|
|
| HECT |
pfam00632 |
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
4821-5127 |
6.26e-114 |
|
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus.
Pssm-ID: 459880 Cd Length: 304 Bit Score: 365.39 E-value: 6.26e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4821 IISREIFNPMYALFCVSPGDRVTYMINPSSHANPNH--LSYFKFVGRVIAKAVHDNKLLECYFTRSFYKHILGKQVKHTD 4898
Cdd:pfam00632 2 LLSKELFDPNYGLFEYETEDDRTYWFNPSSSESPDLelLDYFKFLGKLLGKAIYNGILLDLPFPPFFYKKLLGEPLTLED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4899 MESQDYEFYKGLDYLMKNDISTLG-YELTFSteVQEFGVTQIRDLKPNGRDTAVTEENKFEYVQLVCQLKMSGSIRQQLD 4977
Cdd:pfam00632 82 LESIDPELYKSLKSLLNMDNDDDEdLGLTFT--IPVFGESKTIELIPNGRNIPVTNENKEEYIRLYVDYRLNKSIEPQLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 4978 AFLEGFYDIIPKHLISIFNEQELELLISGLPDIDIEDLKANTEY-HKYTSKSAQIQWFWRALRSFDQADRAKFLQFVTGT 5056
Cdd:pfam00632 160 AFRKGFYSVIPKEALSLFTPEELELLICGSPEIDVEDLKKNTEYdGGYTKNSPTIQWFWEILEEFSPEQRRLFLKFVTGS 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 599138015 5057 SKVPLQGFGSLegmngiQKFQIHR-DDRSTDRLPCAHTCFNQLDLPMYKSYDKLRSCLLKAIHECsEGFGFA 5127
Cdd:pfam00632 240 SRLPVGGFKSL------PKFTIVRkGGDDDDRLPTAHTCFNRLKLPDYSSKEILKEKLLIAIEEG-EGFGLS 304
|
|
| DUF913 |
pfam06025 |
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ... |
622-990 |
1.40e-77 |
|
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin protein ligases.
Pssm-ID: 461803 Cd Length: 369 Bit Score: 263.71 E-value: 1.40e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 622 QRAALLKSMLNFLKKSIQDHA-HFSN-MRNIMETS-LTQSLRHIIANAEYYGPSLFLLATDVVTVYVFNEPSLLSSLQDL 698
Cdd:pfam06025 66 YRQQLLKWLLKFIHHMMQHSGgGTDRlLRNLIDSSqLLGSLRKIIENAKVFGSSVWSLAVNILSDFIHNEPTSFAVIQEA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 699 GITSVMLKALLQKDVPATREVLGSLPNVFSALCLNERGLFEFLSYDPFDKVLKVLLSPDYLVAMRrrrssdPLGDTATNL 778
Cdd:pfam06025 146 GLSKAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNALESFFEIFESPDHVKAME------TDGELASNL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 779 GNAMDDLIKHHPYLRADATEAIVRLLNELVRLGSDPSficwrankessgsgsgsgshggghhVASTPSPMVMVAGTGSAS 858
Cdd:pfam06025 220 GSSFDELVRHHPSLKPAIINAVIDMLARVVELGSTKA-------------------------EPDGWGAKLWVGCSSSSS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 859 SVLQGAAdtndssgdddddddemssasqqqqqpttpgqgggPSTPRTQQAGGVVGSGAGATGTPAAASQAVKVVTPPERE 938
Cdd:pfam06025 275 FSPASSG----------------------------------SLPMETDGESGDESSSDEDVEMEDAPDTDSTEETEPESH 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 599138015 939 AIPLIDYILNVMKFIEAIFSNSPngdHCREFVLHGGLKPILQLLSLPNLPVD 990
Cdd:pfam06025 321 GNSLTDYIDNVARFLEAFFSNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
|
|
| WWE |
smart00678 |
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ... |
1757-1829 |
4.78e-22 |
|
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;
Pssm-ID: 128922 [Multi-domain] Cd Length: 73 Bit Score: 92.79 E-value: 4.78e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 599138015 1757 VWRWYDAStGKWNAYSEANNELIRNAYAAGERWLYINIGRQRCTVSLNCMTQVSEASGTHRPVCPALKLSEAI 1829
Cdd:smart00678 2 VWEYEGRN-GKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVTYSPYSK 73
|
|
| WWE |
pfam02825 |
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ... |
1757-1820 |
7.08e-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: 66.55 E-value: 7.08e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 599138015 1757 VWRWYDaSTGKWNAYSEANNELIRNAYAAGERW--LYINIGRQRCTVSLNCMTQVSEASGTHRPVC 1820
Cdd:pfam02825 1 VWEWED-DNGGWHPYDPEVSSLIEEAYQKGKPSvdLSITTAGFPYTIDFKSMTQTNKDTGTTRPVR 65
|
|
| DUF908 |
pfam06012 |
Domain of Unknown Function (DUF908); |
90-326 |
2.99e-09 |
|
Domain of Unknown Function (DUF908);
Pssm-ID: 428721 Cd Length: 351 Bit Score: 62.35 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 90 DVTLLLHVLNFTTLLIEHSFSRHLYNSIEHLTVLLSSQNMDIVLAVLNLL------Y------MFSKRSNFIPRLPFEKK 157
Cdd:pfam06012 2 DRELVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLlrlaqrYsasnsrRGSAPRHIQQSLLANHY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 158 ELLIVKLFNIAERWGDPN------------------YGLSLKDCCIGEPK--------LEFLY----------------- 194
Cdd:pfam06012 82 NIDLDRLLKLAQPFPKPPppdstdpapsttknsaneYANDLVSLAKEDSKvlpsewgsVKFTYypssssdeaptssksst 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 195 ------------------------------QLCIDYVDEHGHAAQLEIPDMmdlcHTASAP--EVIKTIAGQIskPSEAi 242
Cdd:pfam06012 162 ssnsspstptplrrsstlgtspdspsspstSTPSSAADSDEGLRTFEIPES----KVASKSleDILAKAIEDL--PKES- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 243 KMRIAHRVRLISGFNN--YKLRLQFVQARLQAVSILIYSNALQDNTDKVLYA--GFGEELCELIDKEDVHLVEIRAAVLR 318
Cdd:pfam06012 235 RFELLHRIRIAKALNSssEESRQQLLAIRLLAIANLAYIHPESTFQTKLFEYdpDLVYQLAELIHPDTEVPLELQTAALY 314
|
....*...
gi 599138015 319 TLTSMLHF 326
Cdd:pfam06012 315 ALEALARH 322
|
|
| UBA_HUWE1 |
cd14288 |
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ... |
1468-1507 |
7.59e-09 |
|
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: 54.33 E-value: 7.59e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 599138015 1468 LNADHIKTLTDMGFMHYHVIEALRTNASLEEATDYLLNNP 1507
Cdd:cd14288 1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP 40
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
3264-3648 |
7.21e-07 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 55.74 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3264 ATSDATTTTGGPTRNFSSvdSNVSSET---QTTTRPPRQRGGlrqqsqlpfniyaeidltnEQDSEGDRSTSTTTgtaad 3340
Cdd:pfam17823 66 APAPVTLTKGTSAAHLNS--TEVTAEHtphGTDLSEPATREG-------------------AADGAASRALAAAA----- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3341 gAESQSQHNSSSTAAQVAVPQHQRHPP---VPLLPSSGRPSRPHTRLDETELLLLQLTDRQIRNRLQGSSGHTNSSRTSG 3417
Cdd:pfam17823 120 -SSSPSSAAQSLPAAIAALPSEAFSAPraaACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3418 --SALINARPNRDLPACLQRHDHPAGSIFPRPSANRTPAP-TLVSMPTPMSNAALEQL--------------NVTAPDVV 3480
Cdd:pfam17823 199 asSAPATLTPARGISTAATATGHPAAGTALAAVGNSSPAAgTVTAAVGTVTPAALATLaaaagtvasaagtiNMGDPHAR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3481 RTDRNFALPSSLEVDVDVLPGivdlpQQEAQPEDDQLLLPPPPPPPPSDTTPlVHAEDDLWPGTVVSAGTreeSSAPAVA 3560
Cdd:pfam17823 279 RLSPAKHMPSDTMARNPAAPM-----GAQAQGPIIQVSTDQPVHNTAGEPTP-SPSNTTLEPNTPKSVAS---TNLAVVT 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3561 TESTEAVNESNQPEPTPESSESTSPNPQAPSAEPTPLEPgaaVDASVGAQTPATTEEAASTAGAsGTTATitdmSPEVRA 3640
Cdd:pfam17823 350 TTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSPLLP---TQGAAGPGILLAPEQVATEATA-GTASA----GPTPRS 421
|
....*...
gi 599138015 3641 AlGDLEVP 3648
Cdd:pfam17823 422 S-GDPKTL 428
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
3646-3676 |
9.78e-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: 9.78e-07
10 20 30
....*....|....*....|....*....|.
gi 599138015 3646 EVPEGVDPSFLAALPSEMREEVIQEHLRMQR 3676
Cdd:pfam14377 3 PPPEGIDPSFLAALPPDLRQEVLAQQDDERL 33
|
|
| UBA |
pfam00627 |
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ... |
1469-1503 |
1.58e-05 |
|
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.
Pssm-ID: 395502 [Multi-domain] Cd Length: 37 Bit Score: 44.74 E-value: 1.58e-05
10 20 30
....*....|....*....|....*....|....*.
gi 599138015 1469 NADHIKTLTDMGFMHYHVIEALR-TNASLEEATDYL 1503
Cdd:pfam00627 2 DEEAIQRLVEMGFDREQVREALRaTGNNVERAAEYL 37
|
|
| UBM |
pfam14377 |
Ubiquitin binding region; This family contains repetitive element (RE) from a subgroup of HECT ... |
3695-3722 |
2.08e-05 |
|
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: 44.03 E-value: 2.08e-05
10 20
....*....|....*....|....*...
gi 599138015 3695 EVNPEFLAALPLNIQSEVLMQQRIEQQR 3722
Cdd:pfam14377 7 GIDPSFLAALPPDLRQEVLAQQDDERLR 34
|
|
| PHA01929 |
PHA01929 |
putative scaffolding protein |
3555-3775 |
6.00e-05 |
|
putative scaffolding protein
Pssm-ID: 177328 Cd Length: 306 Bit Score: 48.51 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3555 SAPAVATESTEAVNESNQPEPTPESSESTSPNPQAPsAEPTPLEP---GAAVDASVGAQTPATTEEAASTAgasGTTATI 3631
Cdd:PHA01929 39 VQPGQPGAPQQLAIPTQQPQPVPTSAMTPHVVQQAP-AQPAPAAPpaaGAALPEALEVPPPPAFTPNGEIV---GTLAGN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3632 TDMSPEVRAALGDLEVPEGVDPSFLAALPSEMREE----VIQEHLRMQRIRQRAQQNAIQIAHDSLVEVNPEFLAALpln 3707
Cdd:PHA01929 115 LEGDPQLAPSVSYLEAFSGLDKLDTVRAFGKAAENrdprFIDTHYLKEVLGEAQAQHVINVAKGVLTYVDAQTKAVV--- 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 599138015 3708 iqsevlmqqrieqqRQAAQTANPEDPVDTAA--FFQNLPENLRQAILTDMEESQIASLppELAAE--AQFLR 3775
Cdd:PHA01929 192 --------------NETYAAVGGEAVWKQAAglFNQKADPATRAAIGRLMNSGDAQAM--QYAAKqvAAFAQ 247
|
|
| PRK12495 |
PRK12495 |
hypothetical protein; Provisional |
3542-3658 |
6.59e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 183558 [Multi-domain] Cd Length: 226 Bit Score: 47.56 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3542 PGTVVSAGTREESSAPAVATESTEAVNESNQPEPTPESSESTSPNPQAPSAEPTPLEPGAAVD--ASVGAQTPATTEEAA 3619
Cdd:PRK12495 67 PVTEDGAAGDDAGDGAEATAPSDAGSQASPDDDAQPAAEAEAADQSAPPEASSTSATDEAATDppATAAARDGPTPDPTA 146
|
90 100 110
....*....|....*....|....*....|....*....
gi 599138015 3620 STAGASGTTATITDMSPEVRAAlGDLEVPEGVDPSFLAA 3658
Cdd:PRK12495 147 QPATPDERRSPRQRPPVSGEPP-TPSTPDAHVAGTLQAA 184
|
|
| rad23 |
TIGR00601 |
UV excision repair protein Rad23; All proteins in this family for which functions are known ... |
3546-3771 |
7.51e-05 |
|
UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273167 [Multi-domain] Cd Length: 378 Bit Score: 48.74 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3546 VSAGTREESSAPAVATESTeavnesNQPEPTPESSESTSPNPQAPSAEPTPLEPGAAVDASVGAQTPATTEEAAST--AG 3623
Cdd:TIGR00601 80 GTGKVAPPAATPTSAPTPT------PSPPASPASGMSAAPASAVEEKSPSEESATATAPESPSTSVPSSGSDAASTlvVG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3624 ASGTTAT--ITDM---SPEVRAAL-GDLEVPEGVDPSFLAALPSEMREEVIQEHLrmqrirQRAQQNAI--QIAHDSLVE 3695
Cdd:TIGR00601 154 SERETTIeeIMEMgyeREEVERALrAAFNNPDRAVEYLLTGIPEDPEQPEPVQQT------AASTAAATteTPQHGSVFE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3696 V-------NPEFLAALPLNIQSEVLMQQRIEQQRQAAQtANPEdpvDTAAFFQNL-PEN--LRQAILTDMEE-SQIASLP 3764
Cdd:TIGR00601 228 QaaqggteQPATEAAQGGNPLEFLRNQPQFQQLRQVVQ-QNPQ---LLPPLLQQIgQENpqLLQQISQHPEQfLQMLNEP 303
|
....*..
gi 599138015 3765 PELAAEA 3771
Cdd:TIGR00601 304 VGELASE 310
|
|
| UBA2_UBP13 |
cd14387 |
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ... |
1473-1503 |
1.52e-04 |
|
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13 is an ortholog of UBP5 implicated in catalyzing hydrolysis of various ubiquitin (Ub)-chains. It contains a zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. Due to the non-activating catalysis for K63-polyubiquitin chains, UBP13 may function differently from USP5 in cellular deubiquitination processes. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA2 domain.
Pssm-ID: 270570 Cd Length: 35 Bit Score: 41.98 E-value: 1.52e-04
10 20 30
....*....|....*....|....*....|..
gi 599138015 1473 IKTLTDMGFMHYHVIEAL-RTNASLEEATDYL 1503
Cdd:cd14387 4 IAILMSMGFPRNRAIEALkRTNNNLDRALDWL 35
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
3547-3648 |
8.02e-04 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 46.04 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3547 SAGTREESSAPAVATESTEAVNESNQPEPTPESSESTSPNPQAPSAEPTPLEPGAAVDASVGAQTPATTEEAASTAGASG 3626
Cdd:PRK12270 37 GPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDE 116
|
90 100
....*....|....*....|....*....
gi 599138015 3627 TT-------ATITDMSpevraalGDLEVP 3648
Cdd:PRK12270 117 VTplrgaaaAVAKNMD-------ASLEVP 138
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
3366-3625 |
9.66e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 9.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3366 PPVPLLPSSGRPS------RPHTRLDETELLLLQLTDRQIRNRLQGS--SGHTNSSRTSGSALINARPNRDLPACLQRHD 3437
Cdd:PHA03247 2613 PPSPLPPDTHAPDppppspSPAANEPDPHPPPTVPPPERPRDDPAPGrvSRPRRARRLGRAAQASSPPQRPRRRAARPTV 2692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3438 HPAGSIFPRPSANRTPAP----TLVSMPTPMSNAALEQLNVTAPDVVRTDRNFALPSslevdVDVLPGIVDLPQQEAQPE 3513
Cdd:PHA03247 2693 GSLTSLADPPPPPPTPEPaphaLVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA-----TPGGPARPARPPTTAGPP 2767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3514 DDQLLLPPPPPPPPSDTTPLVHAeddLWPGTVVSAGTREESSAPAVATESTEAVNESNQPEPTpeSSESTSPNPQAPSAE 3593
Cdd:PHA03247 2768 APAPPAAPAAGPPRRLTRPAVAS---LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP--LPPPTSAQPTAPPPP 2842
|
250 260 270
....*....|....*....|....*....|....*.
gi 599138015 3594 PTPLEPGAAVDASVGAQTP----ATTEEAASTAGAS 3625
Cdd:PHA03247 2843 PGPPPPSLPLGGSVAPGGDvrrrPPSRSPAAKPAAP 2878
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
3547-3656 |
1.31e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.70 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3547 SAGTREESSAPAVATESTEAVNESNQPE---PTPESSESTSPNPQAPSAEPTPLEPGAAVDASVGAQTPATTEEAASTAG 3623
Cdd:PHA03247 379 SLPTRKRRSARHAATPFARGPGGDDQTRpaaPVPASVPTPAPTPVPASAPPPPATPLPSAEPGSDDGPAPPPERQPPAPA 458
|
90 100 110
....*....|....*....|....*....|....*
gi 599138015 3624 ASGTTATITDMSPEVRAALGDLEVPE--GVDPSFL 3656
Cdd:PHA03247 459 TEPAPDDPDDATRKALDALRERRPPEppGADLAEL 493
|
|
| UBA2_UBP5 |
cd14386 |
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ... |
1469-1509 |
1.34e-03 |
|
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. This model corresponds to the UBA2 domain.
Pssm-ID: 270569 [Multi-domain] Cd Length: 43 Bit Score: 39.24 E-value: 1.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 599138015 1469 NADHIKTLTDMGFMHYHVIEALR-TNASLEEATDYLLNNPEA 1509
Cdd:cd14386 2 PEEAVAMLVSMGFTRDQAIKALKaTDNNVERAADWIFSHPDE 43
|
|
| UBA_UBAC2 |
cd14305 |
UBA domain found in ubiquitin-associated domain-containing protein 2 (UBAC2) and similar ... |
1471-1504 |
1.61e-03 |
|
UBA domain found in ubiquitin-associated domain-containing protein 2 (UBAC2) and similar proteins; UBAC2, also called phosphoglycerate dehydrogenase-like protein 1, is a ubiquitin-associated domain (UBA)-domain containing protein encoded by gene UBAC2 (or PHGDHL1), a risk gene for Behcet's disease (BD). It may play an important role in the development of BD through its transcriptional modulation. Members in this family contain an N-terminal rhomboid-like domain and a C-terminal UBA domain.
Pssm-ID: 270490 Cd Length: 38 Bit Score: 38.87 E-value: 1.61e-03
10 20 30
....*....|....*....|....*....|....*
gi 599138015 1471 DHIKTLTDMGFMHYHVIEALR-TNASLEEATDYLL 1504
Cdd:cd14305 4 EQVQQLVDMGFSREDVLEALRqSNNDVNAATNLLL 38
|
|
| UBA2_KPC2 |
cd14304 |
UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ... |
1469-1504 |
2.39e-03 |
|
UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar proteins; KPC2, also called ubiquitin-associated domain-containing protein 1 (UBAC1), or glialblastoma cell differentiation-related protein 1, is one of two subunits of Kip1 ubiquitination-promoting complex (KPC), a novel E3 ubiquitin-protein ligase that also contains KPC1 subunit and regulates the ubiquitin-dependent degradation of the cyclin-dependent kinase (CDK) inhibitor p27 at G1 phase. KPC2 contains a ubiquitin-like (UBL) domain and two ubiquitin-associated (UBA) domains. This model corresponds to the UBA2 domain.
Pssm-ID: 270489 Cd Length: 39 Bit Score: 38.39 E-value: 2.39e-03
10 20 30
....*....|....*....|....*....|....*..
gi 599138015 1469 NADHIKTLTDMGFMHYHVIEALR-TNASLEEATDYLL 1504
Cdd:cd14304 2 NPRAVQSLMEMGFEEEDVLEALRvTRNNQNAACEWLL 38
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
3573-3738 |
2.52e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 44.31 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3573 PEPT--PESSESTSPNPQAPSAepTPLEPGAAV---DASVGAQTPATTeEAASTAGASGTTATITDMSPEVRAALG-DLE 3646
Cdd:PRK10263 531 PEPVkePEPIKSSLKAPSVAAV--PPVEAAAAVsplASGVKKATLATG-AAATVAAPVFSLANSGGPRPQVKEGIGpQLP 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3647 VPEGVD-------PSFLAALPSE-MREEVIQEHLRMQrirqraQQNAIQIAHDSLVEVNPEFLAAlplniQSEVLMQQRI 3718
Cdd:PRK10263 608 RPKRIRvptrrelASYGIKLPSQrAAEEKAREAQRNQ------YDSGDQYNDDEIDAMQQDELAR-----QFAQTQQQRY 676
|
170 180
....*....|....*....|
gi 599138015 3719 EQQRQAAQTANPEDPvDTAA 3738
Cdd:PRK10263 677 GEQYQHDVPVNAEDA-DAAA 695
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
3542-3692 |
3.60e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.82 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3542 PGTVVSAGTREESSAPAVATESTEAVNESNQPEPTPESSESTSPNPQAPSAEPTPLEPGAAVDASVGAQTPATTEEAAST 3621
Cdd:PRK07764 406 PAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPP 485
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 599138015 3622 AGASGTTATITDMSPEVRAALGDLEVPEGVDPSFLAALPsEMREEVIQEHLRMQRIRQrAQQNAIQIAHDS 3692
Cdd:PRK07764 486 AAPAPAAAPAAPAAPAAPAGADDAATLRERWPEILAAVP-KRSRKTWAILLPEATVLG-VRGDTLVLGFST 554
|
|
| UBA2_spUBP14_like |
cd14297 |
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ... |
1471-1507 |
4.09e-03 |
|
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: 37.85 E-value: 4.09e-03
10 20 30
....*....|....*....|....*....|....*...
gi 599138015 1471 DHIKTLTDMGFMHYHVIEALR-TNASLEEATDYLLNNP 1507
Cdd:cd14297 2 DLVKQLVDMGFTEAQARKALRkTNNNVERAVDWLFEGP 39
|
|
| Rev1_UBM2 |
cd19318 |
Ubiquitin-Binding Motif 2 (UBM2) of Y-family polymerase Rev1; This model characterizes UBM2, ... |
3651-3675 |
5.67e-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: 37.59 E-value: 5.67e-03
10 20
....*....|....*....|....*
gi 599138015 3651 VDPSFLAALPSEMREEVIQEHLRMQ 3675
Cdd:cd19318 12 VDPSVLAALPPDLQEELEAAYAQRQ 36
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
3530-3662 |
6.82e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 42.91 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3530 TTPLVHAEDDLWPGTVVSAGTREESSAPAVATESTEAVNESNQPEPTPESSESTSPNPQaPSAEPTPLEPGAAVDASVGA 3609
Cdd:PRK07003 387 AAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADG-DAPVPAKANARASADSRCDE 465
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 599138015 3610 QTPATTEEAASTAGASGTTATITDMSPEVRAALGDLEVPEGV-DPSFLAALPSE 3662
Cdd:PRK07003 466 RDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVpDARAPAAASRE 519
|
|
| UBA |
cd14270 |
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ... |
1473-1501 |
7.18e-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: 36.95 E-value: 7.18e-03
10 20 30
....*....|....*....|....*....|
gi 599138015 1473 IKTLTDMGFMHYHVIEALR-TNASLEEATD 1501
Cdd:cd14270 1 LAQLVEMGFSREQARRALRaTNGDVEAAVE 30
|
|
| UBA_atUPL1_2_like |
cd14327 |
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ... |
1473-1506 |
9.28e-03 |
|
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: 36.89 E-value: 9.28e-03
10 20 30
....*....|....*....|....*....|....*.
gi 599138015 1473 IKTLTDMGFMHYHVIEALR--TNASLEEATDYLLNN 1506
Cdd:cd14327 3 VAQLVEMGFSRERAEEALRavGTNSVELAMEWLFTN 38
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
3542-3626 |
9.70e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 42.10 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 599138015 3542 PGTVVSAGTREESSAPAVA----TESTEAVNESNQPEPTPESSESTSPNPQAPSAEPTPLEpGAAVDASVGAQTPATTEE 3617
Cdd:PRK14950 374 AAPSPVRPTPAPSTRPKAAaaanIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTRA-AIPVDEKPKYTPPAPPKE 452
|
....*....
gi 599138015 3618 AASTAGASG 3626
Cdd:PRK14950 453 EEKALIADG 461
|
|
| |
