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

                           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

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2059440167 1398 VNQAQLTQLMDMGFSREHAMEALLNTSTMEQATEYLLTHP 1437
Cdd:cd14288      1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP 40

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]

                           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

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

                           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

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2059440167 1398 VNQAQLTQLMDMGFSREHAMEALLNTSTMEQATEYLLTHP 1437
Cdd:cd14288      1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP 40

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

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2059440167  1698 WRW-FDDRSGRWCSYSASNNSTIDAAWRAGESSVRFTAGRRRYTVQFNTMVQVNEETANRRPvmltVQRVPRVPKPK 1773
Cdd:smart00678    1 YVWeYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRK----VRRVTYSPYSK 73

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]

                           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

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

                           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

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2059440167 1398 VNQAQLTQLMDMGFSREHAMEALLNTSTMEQATEYLLTHP 1437
Cdd:cd14288      1 VNEAHLQQLMDMGFTREHALEALLHTSTLEQATEYLLTHP 40

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

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2059440167  1698 WRW-FDDRSGRWCSYSASNNSTIDAAWRAGESSVRFTAGRRRYTVQFNTMVQVNEETANRRPvmltVQRVPRVPKPK 1773
Cdd:smart00678    1 YVWeYEGRNGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRK----VRRVTYSPYSK 73

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2059440167 1399 NQAQLTQLMDMGFSREHAMEALLNTSTM--EQATEYLLTH 1436
Cdd:cd14295      1 DQELVAQLMEMGFPKVRAEKALFFTQNKglEEAMEWLEEH 40

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.

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2059440167 1399 NQAQLTQLMDMGFSREHAMEALLNTS-TMEQATEYL 1433
Cdd:cd14291      1 DEDKLQQLMEMGFSEAEARLALRACNgNVERAVDYI 36

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.

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2059440167 1402 QLTQLMDMGFSREHAMEAL-LNTSTMEQATEYLLT 1435
Cdd:cd14283      3 LLKQLTDMGFKREPAEEALkSNNMNLEQAVSALLS 37

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.

                           10        20        30
                   ....*....|....*....|....*....|
gi 2059440167 1403 LTQLMDMGFSREHAMEALLNTS-TMEQATE 1431
Cdd:cd14270      1 LAQLVEMGFSREQARRALRATNgDVEAAVE 30

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]

                           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 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.

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2059440167 1403 LTQLMDMGFSREHAMEALLNTST--MEQATEYLLTH 1436
Cdd:cd14302      3 LQTLIEMGFSRNRAEKALAKTGNqgVEAAMEWLLAH 38

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.

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2059440167 1398 VNQAQLTQLMDMGFSREHAMEALL--NTSTMEqATEYLL 1434
Cdd:cd14305      1 PSEEQVQQLVDMGFSREDVLEALRqsNNDVNA-ATNLLL 38

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.

                           10        20        30
                   ....*....|....*....|....*....|
gi 2059440167 1405 QLMDMGFSREHAMEALLNT-STMEQATEYL 1433
Cdd:cd14387      6 ILMSMGFPRNRAIEALKRTnNNLDRALDWL 35

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.

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2059440167 1399 NQAQLTQLMDMGFSREHAMEAL-LNTSTMEQATEYLL 1434
Cdd:cd14304      2 NPRAVQSLMEMGFEEEDVLEALrVTRNNQNAACEWLL 38

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.

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2059440167 1398 VNQAQLTQLMDMGFSREHAMEALL-NTSTMEQATEYLLT 1435
Cdd:cd14282      1 VDEKALRHITEMGFSKEAARQALMdNNNNLEAALNFLLT 39