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Conserved domains on  [gi|2059440167|gb|KAG7228375|]
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hypothetical protein INR49_009239 [Caranx melampygus]

Protein Classification

DUF913 and UBA_HUWE1 domain-containing protein( domain architecture ID 11003803)

protein containing domains DUF908, DUF913, UBA_HUWE1, and WWE

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF913 pfam06025
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ...
431-853 4.46e-101

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


:

Pssm-ID: 461803  Cd Length: 369  Bit Score: 329.96  E-value: 4.46e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  431 RAVRVVD-LITNLD--MAAFQSHSGLSIFICRLEHEVDLSRKECPFVIKPKIQRPSAAVESEdmdtdmemsevamesspg 507
Cdd:pfam06025    1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALELAEAGKGTPSEYKSSVVDYE------------------ 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  508 pstssgsrpegdhraqssaantpragmqcIP-QRAALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGS-LPTSLKHIISNA 583
Cdd:pfam06025   63 -----------------------------IPyYRQQLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENA 113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  584 EYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLTDVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLHSFVQCQPF 663
Cdd:pfam06025  114 KVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAGLSKAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNAL 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  664 ERLFKVLLSPDYLPAMRrrrssdPLGDTASNLGSAVDELMRHQPTLKTDATTAIIKLLEEICNLGRAPEY---ICQKPSI 740
Cdd:pfam06025  194 ESFFEIFESPDHVKAME------TDGELASNLGSSFDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEpdgWGAKLWV 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  741 QKADGTVAVPPARSShaaeeassEDEEEEEALHTFSQQQGEPESNRQSVPLELVVGTEERIPIPLMDYILNVMKFVESIL 820
Cdd:pfam06025  268 GCSSSSSFSPASSGS--------LPMETDGESGDESSSDEDVEMEDAPDTDSTEETEPESHGNSLTDYIDNVARFLEAFF 339
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2059440167  821 SNNTtddHCQEFVNQKGLLPLVSILGLPNLPID 853
Cdd:pfam06025  340 SNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
DUF908 super family cl20318
Domain of Unknown Function (DUF908);
90-367 4.55e-24

Domain of Unknown Function (DUF908);


The actual alignment was detected with superfamily member pfam06012:

Pssm-ID: 428721  Cd Length: 351  Bit Score: 106.26  E-value: 4.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167   90 KALLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASCDMQVVLSVLNLLYVFSKR-SNYITRLGSDKRT---PLLA---- 161
Cdd:pfam06012    3 RELVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLLRLAQRySASNSRRGSAPRHiqqSLLAnhyn 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  162 ----RLQHLAESWG------------------GKENGFGLAECCRDLPmTKYPPSATTLHFEFYAEPGPEVKVERKTSSN 219
Cdd:pfam06012   83 idldRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKEDS-KVLPSEWGSVKFTYYPSSSSDEAPTSSKSST 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  220 T-----------------------------------------LHYIHIEQLDKISESPSEIMESltAMYNIPKDKQTLLF 258
Cdd:pfam06012  162 SsnsspstptplrrsstlgtspdspsspststpssaadsdegLRTFEIPESKVASKSLEDILAK--AIEDLPKESRFELL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  259 THIRLAHGFSNHK--KRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQITDKQLVDIKAASLRTLTSI 334
Cdd:pfam06012  240 HRIRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEAL 319
                          330       340       350
                   ....*....|....*....|....*....|...
gi 2059440167  335 VHleRTPKLSNIIDCTGTASYHGFLPVLVRNCI 367
Cdd:pfam06012  320 AR--HRAKLSDVLSALGANVNHGILLYVLRKAV 350
UBA_HUWE1 cd14288
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ...
1398-1437 1.77e-19

UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, also called ARF-binding protein 1 (ARF-BP1), HECT, UBA and WWE domain-containing protein 1, homologous to E6AP carboxyl terminus homologs protein 9 (HectH9), large structure of UREB1 (LASU1), Mcl-1 ubiquitin ligase E3 (Mule), upstream regulatory element-binding protein 1 (URE-B1), or URE-binding protein 1, may function as a ubiquitin-protein ligase that involves in the ubiquitination cascade that targets specific substrate proteins in proteolysis. It can ubiquitylate DNA polymerase beta (Pol beta), the major BER DNA polymerase and modulates base excision repair (BER). HUWE1 also acts as a critical mediator of both the p53-independent and p53-dependent tumor suppressor functions of ARF tumor suppressor in p53 regulation. Moreover, HUWE1 is both required and sufficient for the polyubiquitination of Mcl-1, an anti-apoptotic Bcl-2 family member involving in DNA damage-induced apoptosis. Furthermore, HUWE1 plays an important role in the regulation of Cdc6 stability after DNA damage. In addition, HUWE1 works as a partner of N-Myc oncoprotein in neural cells. It ubiquitinates N-Myc and primes it for proteasomal-mediated degradation. HUWE1 contains a ubiquitin-associated (UBA) domain, a WWE domain, and a Bcl-2 homology region 3 (BH3) domain at the N-terminus and a HECT domain at the C-terminus. WWE domain plays a role in the regulation of specific protein-protein interactions in a ubiquitin conjugation system. BH3 domain is responsible for the specific binding to Mcl-1. HECT domain involves in the inhibition of the transcriptional activity of p53 via a ubiquitin-dependent degradation pathway. It also controls neural differentiation and proliferation by destabilizing the N-Myc oncoprotein.


:

Pssm-ID: 270474  Cd Length: 40  Bit Score: 83.22  E-value: 1.77e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2059440167 1398 VNQAQLTQLMDMGFSREHAMEALLNTSTMEQATEYLLTHP 1437
Cdd:cd14288      1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP 40
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
1698-1759 2.67e-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: 2.67e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2059440167 1698 WRWFDDRsGRWCSYSASNNSTIDAAWRAGESSV--RFTAGRRRYTVQFNTMVQVNEETANRRPV 1759
Cdd:pfam02825    2 WEWEDDN-GGWHPYDPEVSSLIEEAYQKGKPSVdlSITTAGFPYTIDFKSMTQTNKDTGTTRPV 64
rad23 super family cl36702
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
1346-1438 2.11e-04

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]


The actual alignment was detected with superfamily member TIGR00601:

Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 46.04  E-value: 2.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167 1346 EAASTGSLGPSGAPGASATAGEAPAPTGT----------------TSGGPAGGSADDSTNSTPRREPQVNQAqLTQLMDM 1409
Cdd:TIGR00601   88 AATPTSAPTPTPSPPASPASGMSAAPASAveekspseesatatapESPSTSVPSSGSDAASTLVVGSERETT-IEEIMEM 166
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2059440167 1410 GFSREH---AMEALLNTStmEQATEYLLTHPP 1438
Cdd:TIGR00601  167 GYEREEverALRAAFNNP--DRAVEYLLTGIP 196
 
Name Accession Description Interval E-value
DUF913 pfam06025
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ...
431-853 4.46e-101

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


Pssm-ID: 461803  Cd Length: 369  Bit Score: 329.96  E-value: 4.46e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  431 RAVRVVD-LITNLD--MAAFQSHSGLSIFICRLEHEVDLSRKECPFVIKPKIQRPSAAVESEdmdtdmemsevamesspg 507
Cdd:pfam06025    1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALELAEAGKGTPSEYKSSVVDYE------------------ 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  508 pstssgsrpegdhraqssaantpragmqcIP-QRAALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGS-LPTSLKHIISNA 583
Cdd:pfam06025   63 -----------------------------IPyYRQQLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENA 113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  584 EYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLTDVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLHSFVQCQPF 663
Cdd:pfam06025  114 KVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAGLSKAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNAL 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  664 ERLFKVLLSPDYLPAMRrrrssdPLGDTASNLGSAVDELMRHQPTLKTDATTAIIKLLEEICNLGRAPEY---ICQKPSI 740
Cdd:pfam06025  194 ESFFEIFESPDHVKAME------TDGELASNLGSSFDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEpdgWGAKLWV 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  741 QKADGTVAVPPARSShaaeeassEDEEEEEALHTFSQQQGEPESNRQSVPLELVVGTEERIPIPLMDYILNVMKFVESIL 820
Cdd:pfam06025  268 GCSSSSSFSPASSGS--------LPMETDGESGDESSSDEDVEMEDAPDTDSTEETEPESHGNSLTDYIDNVARFLEAFF 339
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2059440167  821 SNNTtddHCQEFVNQKGLLPLVSILGLPNLPID 853
Cdd:pfam06025  340 SNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
DUF908 pfam06012
Domain of Unknown Function (DUF908);
90-367 4.55e-24

Domain of Unknown Function (DUF908);


Pssm-ID: 428721  Cd Length: 351  Bit Score: 106.26  E-value: 4.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167   90 KALLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASCDMQVVLSVLNLLYVFSKR-SNYITRLGSDKRT---PLLA---- 161
Cdd:pfam06012    3 RELVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLLRLAQRySASNSRRGSAPRHiqqSLLAnhyn 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  162 ----RLQHLAESWG------------------GKENGFGLAECCRDLPmTKYPPSATTLHFEFYAEPGPEVKVERKTSSN 219
Cdd:pfam06012   83 idldRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKEDS-KVLPSEWGSVKFTYYPSSSSDEAPTSSKSST 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  220 T-----------------------------------------LHYIHIEQLDKISESPSEIMESltAMYNIPKDKQTLLF 258
Cdd:pfam06012  162 SsnsspstptplrrsstlgtspdspsspststpssaadsdegLRTFEIPESKVASKSLEDILAK--AIEDLPKESRFELL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  259 THIRLAHGFSNHK--KRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQITDKQLVDIKAASLRTLTSI 334
Cdd:pfam06012  240 HRIRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEAL 319
                          330       340       350
                   ....*....|....*....|....*....|...
gi 2059440167  335 VHleRTPKLSNIIDCTGTASYHGFLPVLVRNCI 367
Cdd:pfam06012  320 AR--HRAKLSDVLSALGANVNHGILLYVLRKAV 350
UBA_HUWE1 cd14288
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ...
1398-1437 1.77e-19

UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, also called ARF-binding protein 1 (ARF-BP1), HECT, UBA and WWE domain-containing protein 1, homologous to E6AP carboxyl terminus homologs protein 9 (HectH9), large structure of UREB1 (LASU1), Mcl-1 ubiquitin ligase E3 (Mule), upstream regulatory element-binding protein 1 (URE-B1), or URE-binding protein 1, may function as a ubiquitin-protein ligase that involves in the ubiquitination cascade that targets specific substrate proteins in proteolysis. It can ubiquitylate DNA polymerase beta (Pol beta), the major BER DNA polymerase and modulates base excision repair (BER). HUWE1 also acts as a critical mediator of both the p53-independent and p53-dependent tumor suppressor functions of ARF tumor suppressor in p53 regulation. Moreover, HUWE1 is both required and sufficient for the polyubiquitination of Mcl-1, an anti-apoptotic Bcl-2 family member involving in DNA damage-induced apoptosis. Furthermore, HUWE1 plays an important role in the regulation of Cdc6 stability after DNA damage. In addition, HUWE1 works as a partner of N-Myc oncoprotein in neural cells. It ubiquitinates N-Myc and primes it for proteasomal-mediated degradation. HUWE1 contains a ubiquitin-associated (UBA) domain, a WWE domain, and a Bcl-2 homology region 3 (BH3) domain at the N-terminus and a HECT domain at the C-terminus. WWE domain plays a role in the regulation of specific protein-protein interactions in a ubiquitin conjugation system. BH3 domain is responsible for the specific binding to Mcl-1. HECT domain involves in the inhibition of the transcriptional activity of p53 via a ubiquitin-dependent degradation pathway. It also controls neural differentiation and proliferation by destabilizing the N-Myc oncoprotein.


Pssm-ID: 270474  Cd Length: 40  Bit Score: 83.22  E-value: 1.77e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2059440167 1398 VNQAQLTQLMDMGFSREHAMEALLNTSTMEQATEYLLTHP 1437
Cdd:cd14288      1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP 40
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
1698-1759 2.67e-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: 2.67e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2059440167 1698 WRWFDDRsGRWCSYSASNNSTIDAAWRAGESSV--RFTAGRRRYTVQFNTMVQVNEETANRRPV 1759
Cdd:pfam02825    2 WEWEDDN-GGWHPYDPEVSSLIEEAYQKGKPSVdlSITTAGFPYTIDFKSMTQTNKDTGTTRPV 64
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
1698-1773 7.00e-13

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 65.82  E-value: 7.00e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2059440167  1698 WRW-FDDRSGRWCSYSASNNSTIDAAWRAGESSVRFTAGRRRYTVQFNTMVQVNEETANRRPvmltVQRVPRVPKPK 1773
Cdd:smart00678    1 YVWeYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRK----VRRVTYSPYSK 73
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
1398-1433 1.88e-05

UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.


Pssm-ID: 395502 [Multi-domain]  Cd Length: 37  Bit Score: 43.58  E-value: 1.88e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2059440167 1398 VNQAQLTQLMDMGFSREHAMEALLNTST-MEQATEYL 1433
Cdd:pfam00627    1 EDEEAIQRLVEMGFDREQVREALRATGNnVERAAEYL 37
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
1346-1438 2.11e-04

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: 46.04  E-value: 2.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167 1346 EAASTGSLGPSGAPGASATAGEAPAPTGT----------------TSGGPAGGSADDSTNSTPRREPQVNQAqLTQLMDM 1409
Cdd:TIGR00601   88 AATPTSAPTPTPSPPASPASGMSAAPASAveekspseesatatapESPSTSVPSSGSDAASTLVVGSERETT-IEEIMEM 166
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2059440167 1410 GFSREH---AMEALLNTStmEQATEYLLTHPP 1438
Cdd:TIGR00601  167 GYEREEverALRAAFNNP--DRAVEYLLTGIP 196
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
1399-1434 1.25e-03

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.


Pssm-ID: 197551 [Multi-domain]  Cd Length: 37  Bit Score: 38.24  E-value: 1.25e-03
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2059440167  1399 NQAQLTQLMDMGFSREHAMEALLNTSTMEQ-ATEYLL 1434
Cdd:smart00165    1 DEEKIDQLLEMGFSREEALKALRAANGNVErAAEYLL 37
 
Name Accession Description Interval E-value
DUF913 pfam06025
Domain of Unknown Function (DUF913); Members of this family are found in various ubiquitin ...
431-853 4.46e-101

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


Pssm-ID: 461803  Cd Length: 369  Bit Score: 329.96  E-value: 4.46e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  431 RAVRVVD-LITNLD--MAAFQSHSGLSIFICRLEHEVDLSRKECPFVIKPKIQRPSAAVESEdmdtdmemsevamesspg 507
Cdd:pfam06025    1 RAVQFLDtLIYNFQdaFQAFRNAGGLDAIIDRIVHEVDSALELAEAGKGTPSEYKSSVVDYE------------------ 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  508 pstssgsrpegdhraqssaantpragmqcIP-QRAALLKSMLNFLKKAIQ--DPAFSDGIRHVMDGS-LPTSLKHIISNA 583
Cdd:pfam06025   63 -----------------------------IPyYRQQLLKWLLKFIHHMMQhsGGGTDRLLRNLIDSSqLLGSLRKIIENA 113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  584 EYYGPSLFLLATEVVTVFVFQEPSLLSSLQDNGLTDVMLHALLIKDVPATREVLGSLPNVFSALCLNARGLHSFVQCQPF 663
Cdd:pfam06025  114 KVFGSSVWSLAVNILSDFIHNEPTSFAVIQEAGLSKAFLEAVLAKGILPSSEAINSIPNAFGAICLNNAGLELFKSSNAL 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  664 ERLFKVLLSPDYLPAMRrrrssdPLGDTASNLGSAVDELMRHQPTLKTDATTAIIKLLEEICNLGRAPEY---ICQKPSI 740
Cdd:pfam06025  194 ESFFEIFESPDHVKAME------TDGELASNLGSSFDELVRHHPSLKPAIINAVIDMLARVVELGSTKAEpdgWGAKLWV 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  741 QKADGTVAVPPARSShaaeeassEDEEEEEALHTFSQQQGEPESNRQSVPLELVVGTEERIPIPLMDYILNVMKFVESIL 820
Cdd:pfam06025  268 GCSSSSSFSPASSGS--------LPMETDGESGDESSSDEDVEMEDAPDTDSTEETEPESHGNSLTDYIDNVARFLEAFF 339
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2059440167  821 SNNTtddHCQEFVNQKGLLPLVSILGLPNLPID 853
Cdd:pfam06025  340 SNNS---HCSDFIEKGGIELLLDLATLPSLPYD 369
DUF908 pfam06012
Domain of Unknown Function (DUF908);
90-367 4.55e-24

Domain of Unknown Function (DUF908);


Pssm-ID: 428721  Cd Length: 351  Bit Score: 106.26  E-value: 4.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167   90 KALLLAVLNFTALLIEYSFSRHLYSSIEHLTTLLASCDMQVVLSVLNLLYVFSKR-SNYITRLGSDKRT---PLLA---- 161
Cdd:pfam06012    3 RELVEAILRFTRLLLENCGNRSIYNSSEHLNDLLNTTSLDVLLAALRLLLRLAQRySASNSRRGSAPRHiqqSLLAnhyn 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  162 ----RLQHLAESWG------------------GKENGFGLAECCRDLPmTKYPPSATTLHFEFYAEPGPEVKVERKTSSN 219
Cdd:pfam06012   83 idldRLLKLAQPFPkppppdstdpapsttknsANEYANDLVSLAKEDS-KVLPSEWGSVKFTYYPSSSSDEAPTSSKSST 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  220 T-----------------------------------------LHYIHIEQLDKISESPSEIMESltAMYNIPKDKQTLLF 258
Cdd:pfam06012  162 SsnsspstptplrrsstlgtspdspsspststpssaadsdegLRTFEIPESKVASKSLEDILAK--AIEDLPKESRFELL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167  259 THIRLAHGFSNHK--KRLQAVQARLHAISILVYSNALQESANSILY--NGLIEELVDVLQITDKQLVDIKAASLRTLTSI 334
Cdd:pfam06012  240 HRIRIAKALNSSSeeSRQQLLAIRLLAIANLAYIHPESTFQTKLFEydPDLVYQLAELIHPDTEVPLELQTAALYALEAL 319
                          330       340       350
                   ....*....|....*....|....*....|...
gi 2059440167  335 VHleRTPKLSNIIDCTGTASYHGFLPVLVRNCI 367
Cdd:pfam06012  320 AR--HRAKLSDVLSALGANVNHGILLYVLRKAV 350
UBA_HUWE1 cd14288
UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, ...
1398-1437 1.77e-19

UBA domain found in eukaryotic E3 ubiquitin-protein ligase HUWE1 and similar proteins; HUWE1, also called ARF-binding protein 1 (ARF-BP1), HECT, UBA and WWE domain-containing protein 1, homologous to E6AP carboxyl terminus homologs protein 9 (HectH9), large structure of UREB1 (LASU1), Mcl-1 ubiquitin ligase E3 (Mule), upstream regulatory element-binding protein 1 (URE-B1), or URE-binding protein 1, may function as a ubiquitin-protein ligase that involves in the ubiquitination cascade that targets specific substrate proteins in proteolysis. It can ubiquitylate DNA polymerase beta (Pol beta), the major BER DNA polymerase and modulates base excision repair (BER). HUWE1 also acts as a critical mediator of both the p53-independent and p53-dependent tumor suppressor functions of ARF tumor suppressor in p53 regulation. Moreover, HUWE1 is both required and sufficient for the polyubiquitination of Mcl-1, an anti-apoptotic Bcl-2 family member involving in DNA damage-induced apoptosis. Furthermore, HUWE1 plays an important role in the regulation of Cdc6 stability after DNA damage. In addition, HUWE1 works as a partner of N-Myc oncoprotein in neural cells. It ubiquitinates N-Myc and primes it for proteasomal-mediated degradation. HUWE1 contains a ubiquitin-associated (UBA) domain, a WWE domain, and a Bcl-2 homology region 3 (BH3) domain at the N-terminus and a HECT domain at the C-terminus. WWE domain plays a role in the regulation of specific protein-protein interactions in a ubiquitin conjugation system. BH3 domain is responsible for the specific binding to Mcl-1. HECT domain involves in the inhibition of the transcriptional activity of p53 via a ubiquitin-dependent degradation pathway. It also controls neural differentiation and proliferation by destabilizing the N-Myc oncoprotein.


Pssm-ID: 270474  Cd Length: 40  Bit Score: 83.22  E-value: 1.77e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2059440167 1398 VNQAQLTQLMDMGFSREHAMEALLNTSTMEQATEYLLTHP 1437
Cdd:cd14288      1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP 40
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
1698-1759 2.67e-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: 2.67e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2059440167 1698 WRWFDDRsGRWCSYSASNNSTIDAAWRAGESSV--RFTAGRRRYTVQFNTMVQVNEETANRRPV 1759
Cdd:pfam02825    2 WEWEDDN-GGWHPYDPEVSSLIEEAYQKGKPSVdlSITTAGFPYTIDFKSMTQTNKDTGTTRPV 64
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
1698-1773 7.00e-13

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 65.82  E-value: 7.00e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2059440167  1698 WRW-FDDRSGRWCSYSASNNSTIDAAWRAGESSVRFTAGRRRYTVQFNTMVQVNEETANRRPvmltVQRVPRVPKPK 1773
Cdd:smart00678    1 YVWeYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRK----VRRVTYSPYSK 73
UBA_atUPL1_2_like cd14327
UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 ...
1401-1436 5.72e-07

UBA domain found in Arabidopsis thaliana E3 ubiquitin-protein ligase UPL1 (atUPL1), UPL2 (atUPL2) and similar proteins; The family includes two highly similar 405-kDa HECT E3 ubiquitin-protein ligases (UPLs), UPL1 and UPL2, from Arabidopsis thaliana. The HECT E3 UPL family plays a prominent role in the ubiquitination of plant proteins. The biological functions of UPL1 and UPL2 remain unclear. Both of them contain a ubiquitin-associated (UBA) domain and a C-terminal HECT domain. UBA domain may be involved in ubiquitin metabolism. HECT domain is necessary and sufficient for their E3 catalytic activity, but requires ATP, E1 and an E2 of the Arabidopsis UBC8 family to ubiquitinate proteins.


Pssm-ID: 270512 [Multi-domain]  Cd Length: 38  Bit Score: 47.68  E-value: 5.72e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2059440167 1401 AQLTQLMDMGFSREHAMEAL--LNTSTMEQATEYLLTH 1436
Cdd:cd14327      1 EAVAQLVEMGFSRERAEEALraVGTNSVELAMEWLFTN 38
UBA1_atUBP14 cd14295
UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) ...
1399-1436 2.11e-06

UBA1 domain found in Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 14 (atUBP14) and similar proteins; atUBP14, also called deubiquitinating enzyme 14, TITAN-6 protein, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is related to the isopeptidase T class of deubiquitinating enzymes that recycle polyubiquitin chains following protein degradation. atUBP14 is essential for early plant development. It can disassemble multi-ubiquitin chains linked internally via epsilon-amino isopeptide bonds using Lys48 and can process some, but not all, translational fusions of ubiquitin linked via alpha-amino peptide bonds. atUBP14 contains two ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270481 [Multi-domain]  Cd Length: 45  Bit Score: 46.60  E-value: 2.11e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2059440167 1399 NQAQLTQLMDMGFSREHAMEALLNTSTM--EQATEYLLTH 1436
Cdd:cd14295      1 DQELVAQLMEMGFPKVRAEKALFFTQNKglEEAMEWLEEH 40
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
1400-1436 1.10e-05

UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270482 [Multi-domain]  Cd Length: 39  Bit Score: 44.16  E-value: 1.10e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2059440167 1400 QAQLTQLMDMGFSREHAMEALLNT--STMEQATEYLLTH 1436
Cdd:cd14296      1 EEAVSQLMSMGFSENAAKRALYYTgnSSVEAAMNWLFEH 39
UBA1_NUB1_like cd14291
UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called ...
1399-1433 1.22e-05

UBA1 domain found in NEDD8 ultimate buster 1 (NUB1) and similar proteins; NUB1, also called negative regulator of ubiquitin-like proteins 1, renal carcinoma antigen NY-REN-18, or protein BS4, is a NEDD8-interacting protein that can be induced by interferon. It functions as a strong post-transcriptional down-regulator of the NEDD8 expression and plays critical roles in regulating many biological events, such as cell growth, NF-kappaB signaling, and biological responses to hypoxia. NUB1 can also interact with aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) which may function in the regulation of cell cycle progression. NUB1 contains three ubiquitin-associated domains (UBA), a bipartite nuclear localization signal (NLS) and a PEST motif. This model corresponds to UBA1 domain.


Pssm-ID: 270477 [Multi-domain]  Cd Length: 36  Bit Score: 43.98  E-value: 1.22e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2059440167 1399 NQAQLTQLMDMGFSREHAMEALLNTS-TMEQATEYL 1433
Cdd:cd14291      1 DEDKLQQLMEMGFSEAEARLALRACNgNVERAVDYI 36
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
1398-1433 1.88e-05

UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.


Pssm-ID: 395502 [Multi-domain]  Cd Length: 37  Bit Score: 43.58  E-value: 1.88e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2059440167 1398 VNQAQLTQLMDMGFSREHAMEALLNTST-MEQATEYL 1433
Cdd:pfam00627    1 EDEEAIQRLVEMGFDREQVREALRATGNnVERAAEYL 37
UBA_TNR6C cd14283
UBA domain found in trinucleotide repeat-containing gene 6C protein (TNRC6C) and similar ...
1402-1435 2.23e-05

UBA domain found in trinucleotide repeat-containing gene 6C protein (TNRC6C) and similar proteins; TNRC6C is one of three GW182 paralogs in mammalian genomes. It is enriched in P-bodies and important for efficient miRNA-mediated repression. TNRC6C is composed of an N-terminal glycine/tryptophan (G/W)-rich region containing an Ago hook responsible for Ago protein-binding; a ubiquitin-associated (UBA) domain and a glutamine (Q)-rich region in the middle region; a middle G/W-rich region, a RNA recognition motif (RRM), also called RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal G/W-rich region, at the C-terminus. A bipartite C-terminal region including the middle and C-terminal G/W-rich regions is referred as silencing domain that triggers silencing of bound transcripts by inhibiting protein expression and promoting mRNA decay via deadenylation. The C-terminal half containing the RRM domain functions as a key effector domain mediating protein synthesis repression by TNRC6C.


Pssm-ID: 270469  Cd Length: 38  Bit Score: 43.26  E-value: 2.23e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2059440167 1402 QLTQLMDMGFSREHAMEAL-LNTSTMEQATEYLLT 1435
Cdd:cd14283      3 LLKQLTDMGFKREPAEEALkSNNMNLEQAVSALLS 37
UBA2_UBP5 cd14386
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called ...
1398-1437 9.34e-05

UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 5 (UBP5); UBP5, also called deubiquitinating enzyme 5, Isopeptidase T (IsoT), ubiquitin thioesterase 5, or ubiquitin-specific-processing protease 5, is a deubiquitinating enzyme largely responsible for the disassembly of the majority of unanchored polyubiquitin in the cell. Zinc is required for its catalytic activity. UBP5 contains four ubiquitin (Ub)-binding sites including an N-terminal zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. ZnF domain binds the proximal ubiquitin. UBP domain forms the active site. UBA domains are involved in binding linear or K48-linked polyubiquitin. This model corresponds to the UBA2 domain.


Pssm-ID: 270569 [Multi-domain]  Cd Length: 43  Bit Score: 41.55  E-value: 9.34e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2059440167 1398 VNQAQLTQLMDMGFSREHAMEALLNTS-TMEQATEYLLTHP 1437
Cdd:cd14386      1 VPEEAVAMLVSMGFTRDQAIKALKATDnNVERAADWIFSHP 41
UBA cd14270
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ...
1403-1431 1.65e-04

UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ubiquitin-associated (UBA) domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only the bind UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains.


Pssm-ID: 270456 [Multi-domain]  Cd Length: 30  Bit Score: 40.80  E-value: 1.65e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2059440167 1403 LTQLMDMGFSREHAMEALLNTS-TMEQATE 1431
Cdd:cd14270      1 LAQLVEMGFSREQARRALRATNgDVEAAVE 30
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
1395-1437 1.71e-04

UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270483 [Multi-domain]  Cd Length: 39  Bit Score: 40.93  E-value: 1.71e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2059440167 1395 EPQVNQaqltqLMDMGFSREHAMEALLNT-STMEQATEYLLTHP 1437
Cdd:cd14297      1 EDLVKQ-----LVDMGFTEAQARKALRKTnNNVERAVDWLFEGP 39
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
1346-1438 2.11e-04

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: 46.04  E-value: 2.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2059440167 1346 EAASTGSLGPSGAPGASATAGEAPAPTGT----------------TSGGPAGGSADDSTNSTPRREPQVNQAqLTQLMDM 1409
Cdd:TIGR00601   88 AATPTSAPTPTPSPPASPASGMSAAPASAveekspseesatatapESPSTSVPSSGSDAASTLVVGSERETT-IEEIMEM 166
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2059440167 1410 GFSREH---AMEALLNTStmEQATEYLLTHPP 1438
Cdd:TIGR00601  167 GYEREEverALRAAFNNP--DRAVEYLLTGIP 196
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
1403-1436 3.47e-04

UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required.


Pssm-ID: 270491  Cd Length: 36  Bit Score: 39.73  E-value: 3.47e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2059440167 1403 LTQLMDMGFSREHAMEALLNTS-TMEQATEYLLTH 1436
Cdd:cd14306      1 VAKLMELGFPEEDCIRALRACGgNVEEAANWLLEN 35
UBA_UBXN1 cd14302
UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also ...
1403-1436 3.86e-04

UBA domain found in UBX domain-containing protein 1 (UBXN1) and similar proteins; UBXN1, also called SAPK substrate protein 1 (SAKS1) or UBA/UBX 33.3 kDa protein, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (UBX) domain. It binds polyubiquitin and valosin-containing protein (VCP), and has been identified as a substrate for stress-activated protein kinases (SAPKs). Moreover, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and may be involved in the Ub-proteasome proteolytic pathways. In addition, UBXN1 can associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domain.


Pssm-ID: 270487 [Multi-domain]  Cd Length: 41  Bit Score: 39.97  E-value: 3.86e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2059440167 1403 LTQLMDMGFSREHAMEALLNTST--MEQATEYLLTH 1436
Cdd:cd14302      3 LQTLIEMGFSRNRAEKALAKTGNqgVEAAMEWLLAH 38
UBA1_KPC2 cd14303
UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
1398-1436 1.10e-03

UBA1 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar proteins; KPC2, also called ubiquitin-associated domain-containing protein 1 (UBAC1), or glialblastoma cell differentiation-related protein 1, is one of two subunits of Kip1 ubiquitination-promoting complex (KPC), a novel E3 ubiquitin-protein ligase that also contains KPC1 subunit and regulates the ubiquitin-dependent degradation of the cyclin-dependent kinase (CDK) inhibitor p27 at G1 phase. KPC2 contains a ubiquitin-like (UBL) domain and two ubiquitin-associated (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270488 [Multi-domain]  Cd Length: 41  Bit Score: 38.53  E-value: 1.10e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2059440167 1398 VNQAQLTQLMDMGFSREHAMEAL-LNTSTMEQATEYLLTH 1436
Cdd:cd14303      1 VDPEALKQLTEMGFPEARATKALlLNRMSPTQAMEWLLEH 40
UBA_UBAC2 cd14305
UBA domain found in ubiquitin-associated domain-containing protein 2 (UBAC2) and similar ...
1398-1434 1.21e-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: 38.48  E-value: 1.21e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2059440167 1398 VNQAQLTQLMDMGFSREHAMEALL--NTSTMEqATEYLL 1434
Cdd:cd14305      1 PSEEQVQQLVDMGFSREDVLEALRqsNNDVNA-ATNLLL 38
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
1399-1434 1.25e-03

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.


Pssm-ID: 197551 [Multi-domain]  Cd Length: 37  Bit Score: 38.24  E-value: 1.25e-03
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 2059440167  1399 NQAQLTQLMDMGFSREHAMEALLNTSTMEQ-ATEYLL 1434
Cdd:smart00165    1 DEEKIDQLLEMGFSREEALKALRAANGNVErAAEYLL 37
UBA2_UBP13 cd14387
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ...
1405-1433 2.47e-03

UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13 is an ortholog of UBP5 implicated in catalyzing hydrolysis of various ubiquitin (Ub)-chains. It contains a zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. Due to the non-activating catalysis for K63-polyubiquitin chains, UBP13 may function differently from USP5 in cellular deubiquitination processes. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270570  Cd Length: 35  Bit Score: 37.35  E-value: 2.47e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2059440167 1405 QLMDMGFSREHAMEALLNT-STMEQATEYL 1433
Cdd:cd14387      6 ILMSMGFPRNRAIEALKRTnNNLDRALDWL 35
UBA1_spUBP14_like cd14385
UBA1 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
1399-1436 2.66e-03

UBA1 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 UBA1 domain.


Pssm-ID: 270568 [Multi-domain]  Cd Length: 47  Bit Score: 37.78  E-value: 2.66e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2059440167 1399 NQAQLTQLMDMGFSREHAMEALLNT--STMEQATEYLLTH 1436
Cdd:cd14385      1 NAEALAQLLGMGFPEVRCKKALLATgnSDAEAAMNWLFEH 40
UBA2_KPC2 cd14304
UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
1399-1434 3.45e-03

UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar proteins; KPC2, also called ubiquitin-associated domain-containing protein 1 (UBAC1), or glialblastoma cell differentiation-related protein 1, is one of two subunits of Kip1 ubiquitination-promoting complex (KPC), a novel E3 ubiquitin-protein ligase that also contains KPC1 subunit and regulates the ubiquitin-dependent degradation of the cyclin-dependent kinase (CDK) inhibitor p27 at G1 phase. KPC2 contains a ubiquitin-like (UBL) domain and two ubiquitin-associated (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270489  Cd Length: 39  Bit Score: 37.24  E-value: 3.45e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2059440167 1399 NQAQLTQLMDMGFSREHAMEAL-LNTSTMEQATEYLL 1434
Cdd:cd14304      2 NPRAVQSLMEMGFEEEDVLEALrVTRNNQNAACEWLL 38
UBA_AAA_plant cd14389
UBA domain found in plant AAA-type ATPase-like proteins; This family includes some ...
1403-1436 6.79e-03

UBA domain found in plant AAA-type ATPase-like proteins; This family includes some uncharacterized AAA-type ATPase-like proteins found in plant. The AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. Members in this family contains an N-terminal ubiquitin-association (UBA) domain, a AAA-type ATPase domain and a C-terminal MgsA AAA+ ATPase domain. This model corresponds to the UBA domain which show a high level of sequence similarity with mammalian ubiquitin-associated and SH3 domain-containing protein A (UBS3A).


Pssm-ID: 270572  Cd Length: 37  Bit Score: 36.56  E-value: 6.79e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2059440167 1403 LTQLMDMGFSREHAMEALLNT--STMEQATEYLLTH 1436
Cdd:cd14389      1 MEQLVDMGFSSDLAAEALAATggKSTQKATEWILSH 36
UBA_TDRD3 cd14282
UBA domain of Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a ...
1398-1435 7.26e-03

UBA domain of Tudor domain-containing protein 3 (TDRD3) and similar proteins; TDRD3 is a modular protein containing Tudor domain, a DUF/OB-fold motif and a ubiquitin-associated (UBA) domain. It shows both nucleic acid- and methyl-binding properties and can interact with methylated RNA-binding proteins, such as fragile X mental retardation protein (FMRP) and DEAD/H box-3 (also known as DDX3X/Y, DBX/Y, HLP2 and DDX14) which is implicated in human genetic diseases. At this point, TDRD3 may play a central role in RNA processing regulatory pathways involving arginine methylation. TDRD3 localizes predominantly to the cytoplasm stress granules (SGs). The Tudor domain is essential and sufficient for its recruitment to SGs.


Pssm-ID: 270468  Cd Length: 39  Bit Score: 36.37  E-value: 7.26e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2059440167 1398 VNQAQLTQLMDMGFSREHAMEALL-NTSTMEQATEYLLT 1435
Cdd:cd14282      1 VDEKALRHITEMGFSKEAARQALMdNNNNLEAALNFLLT 39
UBA_II_E2_UBE2K_like cd14313
UBA domain found in vertebrate ubiquitin-conjugating enzyme E2 K (UBE2K), Drosophila ...
1400-1434 8.26e-03

UBA domain found in vertebrate ubiquitin-conjugating enzyme E2 K (UBE2K), Drosophila melanogaster ubiquitin-conjugating enzyme E2-22 kDa (UbcD4) and similar proteins; UBE2K, also called Huntingtin-interacting protein 2 (HIP-2), ubiquitin carrier protein, ubiquitin-conjugating enzyme E2-25 kDa (E2-25K), or ubiquitin-protein ligase, is a multi-ubiquitinating enzyme with the ability to synthesize Lys48-linked polyubiquitin chains which is involved in the ubiquitin (Ub)-dependent proteolytic pathway. It interacts with the frameshift mutant of ubiquitin B and functions as a crucial factor regulating amyloid-beta neurotoxicity. It has also been characterized as Huntingtin-interacting protein that modulates the neurotoxicity of Amyloid-beta (Abeta), the principal protein involved in Alzheimer's disease pathogenesis. Moreover, E2-25K increases aggregate the formation of expanded polyglutamine proteins and polyglutamine-induced cell death in the pathology of polyglutamine diseases. UbcD4, also called ubiquitin carrier protein, or ubiquitin-protein ligase, is encoded by Drosophila E2 gene which is only expressed in pole cells in embryos. It is a putative E2 enzyme homologous to the Huntingtin interacting protein-2 (HIP2) of human. UbcD4 specifically interacts with the polyubiquitin-binding subunit of the proteasome. This family also includes a putative ubiquitin conjugating enzyme from plasmodium Yoelii (pyUCE). It shows a high level of sequence similarity with UBE2K and may also plays a role in the ubiquitin-mediated protein degradation pathway. All family members are class II E2 conjugating enzymes which contain a C-terminal ubiquitin-associated (UBA) domain in addition to an N-terminal catalytic ubiquitin-conjugating enzyme E2 (UBCc) domain.


Pssm-ID: 270498  Cd Length: 36  Bit Score: 36.15  E-value: 8.26e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2059440167 1400 QAQLTQLMDMGFSREHAMEALLNTS-TMEQATEYLL 1434
Cdd:cd14313      1 KKKVDKLVDMGFDRDEAIVALSSNNwNLERATEYLF 36
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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