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Conserved domains on  [gi|1046888122|ref|XP_017448799|]
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ubiquitin conjugation factor E4 B isoform X2 [Rattus norvegicus]

Protein Classification

ubiquitin conjugation factor E4 family protein( domain architecture ID 12105735)

ubiquitin conjugation factor E4 family protein such as UBE4B, a U-box-type ubiquitin-protein ligase that functions as an E3 ubiquitin ligase and an E4 polyubiquitin chain elongation factor, which catalyzes formation of Lys27- and Lys33-linked polyubiquitin chains rather than the Lys48-linked chain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ufd2P_core pfam10408
Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ...
 631-1251 0e+00

Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ubiquitin elongating factor or E4, running from helix alpha-11 to alpha-38. It consists of 31 helices of variable length connected by loops of variable size forming a compact unit; the helical packing pattern of the compact unit consists of five structural repeats that resemble tandem Armadillo (ARM) repeats. This domain is involved in ubiquitination as it binds Cdc48p and escorts ubiquitinated proteins from Cdc48p to the proteasome for degradation. The core is structurally similar to the nuclear transporter protein importin-alpha. The core is associated with the U-box at the C-terminus, pfam04564, which has ligase activity.


:

Pssm-ID: 463080  Cd Length: 594  Bit Score: 743.24  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  631 LGAFFSFSVFAeDDAKVVEKYFSGPAITLENTRVVSQ-SLQHYLELGRQELFKILHSILLNG-ETREAALSYMAAIVNAN 708
Cdd:pfam10408    1 LGPFLRLSPLP-DDPEVAKKYFSNPKTRSPADIESSQsSLRQELKTLQEQLFQIVNKLLRASpESRERVLDWFAQIINLN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  709 MKKAQMQADDRLVSTDGFMLNLLWVLQQLS------TKIKLETVDPTYIFHPRCRITLPnDETRINATMEDVNEWltelY 782
Cdd:pfam10408   80 HKRRKMQVDPNTVSSDGFMLNLTAVLLRLCepfldaTFSKIDKIDPDYLLPRSSRIDIS-DETRLNADQEEADEF----Y 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  783 GDQPPFSEPKFPTECFFLTLHAHHLSILPSCRRYIRRLRAIRELNRTvedlknnesqwkdsplatrhremlkrcktqlkk 862
Cdd:pfam10408  155 EQKAKEGEPNFITECFFLTLAALHLGILPAISKYKRLARELKRLQAE--------------------------------- 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  863 lvrcKACADAGLLDESFLRRCLNFYGLLIQLMLRVLDPA----YPDITLPLNSEVPKVFAALPEFYVEDVAEFLFFIVQY 938
Cdd:pfam10408  202 ----KLAYEAVLLDPSLLQRSLQFLRFVATWLLRVADPKhqypKKPLKLPLPAEPPEPFKYLPEYFIEDIVDFLLFVTRF 277

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  939 SPQVLY-EPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPSVQ-PRTQKFFEMIENHPLSTKLLVPSLMKFYTD 1016
Cdd:pfam10408  278 APDILEsLSQLDELITFCIVFLRSPEYIKNPHLKAKLVEVLFYGTPPRQnGRPGVLGDILESHPLALKHLLPALMKFYID 357

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122 1017 VEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFMEEFNSGKQ-FVRYINMLINDTTFLLDESLESLKRIHEVQEEM 1095
Cdd:pfam10408  358 VEKTGASSQFYDKFNIRYNISQILKYLWKNPSYREQLKKEAKENEDfFVRFVNLLLNDVTFLLDESLSKLKEIHELQEEM 437

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122 1096 KNQEQWDQLPRDQQQARQSQLAQDERVSRSYLALATETVDMFHLLTKQVQKPFLRPELGPRLAAMLNFNLQQLCGPKCRD 1175
Cdd:pfam10408  438 ADAAEWEALPEEERQEREEQLRSLERQAKSYLQLANETVKLLKLFTKEIPEPFLMPEIVDRLAAMLNYNLDQLVGPKCKN 517

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046888122 1176 LKVENPEKYGFEPKKLLDQLTDIYLQLDCA-RFAKAIADDQRSYSKELFEEVISKMRKAGIKSTIAIEKFKLLAEKV 1251
Cdd:pfam10408  518 LKVKNPEKYGFNPKELLSDIVDIYLNLSDQpEFVRAVARDGRSYSPELFEKAARILRRKGLKSPEEIEKFEELAQKV 594
RING-Ubox_UBE4B cd16658
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and ...
 1265-1338 1.70e-48

U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and similar proteins; UBE4B, also known as UFD2a, is a U-box-type ubiquitin-protein ligase that functions as an E3 ubiquitin ligase and an E4 polyubiquitin chain elongation factor, which catalyzes formation of Lys27- and Lys33-linked polyubiquitin chains rather than the Lys48-linked chain. It is a mammalian homolog of yeast UFD2 ubiquitination factor and it participates in the proteasomal degradation of misfolded or damaged proteins through association with chaperones. It is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. UBE4B has contradictory functions upon tumorigenesis as an oncogene or tumor suppressor in different types of cancers. It is essential for Hdm2 (also known as Mdm2)-mediated p53 degradation. It mediates p53 polyubiquitination and degradation, as well as inhibits p53-dependent transactivation and apoptosis, and thus plays an important role in regulating phosphorylated p53 following DNA damage. UBE4B is also associated with other pathways independent of the p53 family, such as polyglutamine aggregation and Wallerian degeneration, both of which are critical in neurodegenerative diseases. Moreover, UBE4B acts as a regulator of epidermal growth factor receptor (EGFR) degradation. It is recruited to endosomes in response to EGFR activation by binding to Hrs, a key component of endosomal sorting complex required for transport (ESCRT) 0, and then regulates endosomal sorting, affecting cellular levels of the EGFR and its downstream signaling. UBE4B contains a ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus.


:

Pssm-ID: 438320  Cd Length: 74  Bit Score: 166.68  E-value: 1.70e-48
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046888122 1265 YSDAPDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQMLTESMLEPVPELKEQIQAWMREKQ 1338
Cdd:cd16658      1 LGDAPDEFLDPLMDTLMTDPVILPSGTIMDRSIILRHLLNSQTDPFNRQPLTEDMLEPVPELKERIQAWIREKQ 74
PRK07003 super family cl35530
DNA polymerase III subunit gamma/tau;
287-450 7.98e-09

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK07003:

Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 60.25  E-value: 7.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  287 PGLSPSFASPSHTAPAASPHSSAPQGAVASQSLSPQSAATHPLSPHSVAP---------QAAVPSPSLSSHSTASVIATG 357
Cdd:PRK07003   383 PGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPpatadrgddAADGDAPVPAKANARASADSR 462

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  358 SQPSS--PRYRPYTVTHLWGSSPCPTPRSSilANPPGFPAHSSSPRAVPASSSRQRPRSRAPAfPPASPSAASRRPSSLR 435
Cdd:PRK07003   463 CDERDaqPPADSGSASAPASDAPPDAAFEP--APRAAAPSAATPAAVPDARAPAAASREDAPA-AAAPPAPEARPPTPAA 539

                          170
                   ....*....|....*
gi 1046888122  436 ISPSLGASGGASTWD 450
Cdd:PRK07003   540 AAPAARAGGAAAALD 554
 
Name Accession Description Interval E-value
Ufd2P_core pfam10408
Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ...
 631-1251 0e+00

Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ubiquitin elongating factor or E4, running from helix alpha-11 to alpha-38. It consists of 31 helices of variable length connected by loops of variable size forming a compact unit; the helical packing pattern of the compact unit consists of five structural repeats that resemble tandem Armadillo (ARM) repeats. This domain is involved in ubiquitination as it binds Cdc48p and escorts ubiquitinated proteins from Cdc48p to the proteasome for degradation. The core is structurally similar to the nuclear transporter protein importin-alpha. The core is associated with the U-box at the C-terminus, pfam04564, which has ligase activity.


Pssm-ID: 463080  Cd Length: 594  Bit Score: 743.24  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  631 LGAFFSFSVFAeDDAKVVEKYFSGPAITLENTRVVSQ-SLQHYLELGRQELFKILHSILLNG-ETREAALSYMAAIVNAN 708
Cdd:pfam10408    1 LGPFLRLSPLP-DDPEVAKKYFSNPKTRSPADIESSQsSLRQELKTLQEQLFQIVNKLLRASpESRERVLDWFAQIINLN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  709 MKKAQMQADDRLVSTDGFMLNLLWVLQQLS------TKIKLETVDPTYIFHPRCRITLPnDETRINATMEDVNEWltelY 782
Cdd:pfam10408   80 HKRRKMQVDPNTVSSDGFMLNLTAVLLRLCepfldaTFSKIDKIDPDYLLPRSSRIDIS-DETRLNADQEEADEF----Y 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  783 GDQPPFSEPKFPTECFFLTLHAHHLSILPSCRRYIRRLRAIRELNRTvedlknnesqwkdsplatrhremlkrcktqlkk 862
Cdd:pfam10408  155 EQKAKEGEPNFITECFFLTLAALHLGILPAISKYKRLARELKRLQAE--------------------------------- 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  863 lvrcKACADAGLLDESFLRRCLNFYGLLIQLMLRVLDPA----YPDITLPLNSEVPKVFAALPEFYVEDVAEFLFFIVQY 938
Cdd:pfam10408  202 ----KLAYEAVLLDPSLLQRSLQFLRFVATWLLRVADPKhqypKKPLKLPLPAEPPEPFKYLPEYFIEDIVDFLLFVTRF 277

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  939 SPQVLY-EPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPSVQ-PRTQKFFEMIENHPLSTKLLVPSLMKFYTD 1016
Cdd:pfam10408  278 APDILEsLSQLDELITFCIVFLRSPEYIKNPHLKAKLVEVLFYGTPPRQnGRPGVLGDILESHPLALKHLLPALMKFYID 357

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122 1017 VEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFMEEFNSGKQ-FVRYINMLINDTTFLLDESLESLKRIHEVQEEM 1095
Cdd:pfam10408  358 VEKTGASSQFYDKFNIRYNISQILKYLWKNPSYREQLKKEAKENEDfFVRFVNLLLNDVTFLLDESLSKLKEIHELQEEM 437

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122 1096 KNQEQWDQLPRDQQQARQSQLAQDERVSRSYLALATETVDMFHLLTKQVQKPFLRPELGPRLAAMLNFNLQQLCGPKCRD 1175
Cdd:pfam10408  438 ADAAEWEALPEEERQEREEQLRSLERQAKSYLQLANETVKLLKLFTKEIPEPFLMPEIVDRLAAMLNYNLDQLVGPKCKN 517

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046888122 1176 LKVENPEKYGFEPKKLLDQLTDIYLQLDCA-RFAKAIADDQRSYSKELFEEVISKMRKAGIKSTIAIEKFKLLAEKV 1251
Cdd:pfam10408  518 LKVKNPEKYGFNPKELLSDIVDIYLNLSDQpEFVRAVARDGRSYSPELFEKAARILRRKGLKSPEEIEKFEELAQKV 594
UFD2 COG5113
Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, ...
 536-1337 9.40e-131

Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227444 [Multi-domain]  Cd Length: 929  Bit Score: 426.32  E-value: 9.40e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  536 NLPYGFIQELVRTTHQDEEVFKQIFIPILQGLARaaKECSLDSDYFKYPLMALGELcetkFGKTHPMCNLVASLPLWLPk 615
Cdd:COG5113    129 LLPMIFLSSFKQRQLDEASNLDNLFTSALEALTG--LHGVLEEDTVLKNVMEIYWG----LVNTKPIADVILKFPIYSG- 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  616 SLSPGsgrELQRLSYLGAFFSFSVFAEDdakVVEKYFSGPAI-TLENTRVVSQSLQHYLELGRQELFKILHSILLNG-ET 693
Cdd:COG5113    202 TNFPC---GFEYKTLLGFIESLSYKKCD---VAARALDYLGIrSRQVVEKSRRSLRLTLSDHSDKLFQIIHSLVRSSkEL 275

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  694 REAALSYMAAIVNANMKKAQMQADDRLVSTDGFMLNLLWVLQQLSTKI------KLETVDPTYIFHPRCRITlpnDETRI 767
Cdd:COG5113    276 RANFMKYFAKVINVNHERSKTIFSWRENISDGFMYNMSMVLSRFSRPFldigcsKIDMVDKIYFNNPRVDIK---EETKL 352

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  768 NatmedVNEWLTELYGDQPPFSEPKFPTECFFLTLHAHHLSI---LPSCRRYIRRLRAIRELNRTVEDLKNNESQwkdsp 844
Cdd:COG5113    353 N-----VDEKSLDSFYTKPAEGSNNFISDIFFLYLTKIHYGVnatFTSCEKFGEYIRKLKESLEYECRLLDGSFQ----- 422

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  845 lATRHREMLKRCKTQLKKLVRCKACADAGLLDESFLRRCLNFYGLLIQLMLRVLDP--AYP--DITLPLNSEVPKVFAAL 920
Cdd:COG5113    423 -ATRLTAQLSRMEAYLKGIDSKMSALNGFLFMTSLFADEFPFTDFMTEYLARVEDPwpTYPfyYKTLPWMENAPMTFKLI 501

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  921 PEFYVEDVAEFLFFIVQYSPQVLYEPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPSVQPRTQKFF-EMIENH 999
Cdd:COG5113    502 PEATIENALNYVLESIKDWRSPIFKKELEPLCEFVKIVLHRSSAIKNPMLNRKLDYYLSLGRDEMRMESRSIIhDIFKEG 581

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122 1000 PLSTKLLVPSLMKFYTDVEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFM-EEFNSGKQFVRYINMLINDTTFLL 1078
Cdd:COG5113    582 KVFSRWLLPALMAFYIEIESTGQSTQFYDKFNIRFIICMMKDFEYKQPSYSEGLSsIKDTNLPFFVKFDAKMLNDLTRLL 661

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122 1079 DESLESLKRIHEVQEEMKNQEQWDQLPRDQQQArQSQLAQDERVSRSYLALATETVDMFHLLTKQVQKPFLRPELGPRLA 1158
Cdd:COG5113    662 DEALKELVEEHNIQSLLADAISNSNISERIGEL-QKSLAFAKRQARNSCLLVDGCFDLFTHILDEIPDAFLVDEIVSRLA 740

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122 1159 AMLNFNLQQLCGPKCRDLKVENPEKYGFEPKKLLDQLTDIYLQL-DCARFAKAIADDQRSYSKELFEEVISKMRKAGIKS 1237
Cdd:COG5113    741 RMLNYNLKILTGPKCTDLKVKDPEQYGFNAKNLLRRMVMVYINLrSESKFVEAVASDKRSFDIDFFRRALRICENKYLIS 820

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122 1238 TIAIEKFKLLAEKVEEIVAKNARAEIDYSDAPDEFRDPLMDTLMTDPVRLP-SGTIMDRSIILRHLLNSPTDPFNRQMLT 1316
Cdd:COG5113    821 ESQIEELRSFINRLEKVRVIEAVEEEDMGDVPDEFLDPLMFTIMKDPVKLPtSRITIDRSTIKAHLLSDGTDPFNRMPLT 900

                          810       820
                   ....*....|....*....|.
gi 1046888122 1317 ESMLEPVPELKEQIQAWMREK 1337
Cdd:COG5113    901 LDDVTPNAELREKINRFYKCK 921
RING-Ubox_UBE4B cd16658
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and ...
 1265-1338 1.70e-48

U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and similar proteins; UBE4B, also known as UFD2a, is a U-box-type ubiquitin-protein ligase that functions as an E3 ubiquitin ligase and an E4 polyubiquitin chain elongation factor, which catalyzes formation of Lys27- and Lys33-linked polyubiquitin chains rather than the Lys48-linked chain. It is a mammalian homolog of yeast UFD2 ubiquitination factor and it participates in the proteasomal degradation of misfolded or damaged proteins through association with chaperones. It is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. UBE4B has contradictory functions upon tumorigenesis as an oncogene or tumor suppressor in different types of cancers. It is essential for Hdm2 (also known as Mdm2)-mediated p53 degradation. It mediates p53 polyubiquitination and degradation, as well as inhibits p53-dependent transactivation and apoptosis, and thus plays an important role in regulating phosphorylated p53 following DNA damage. UBE4B is also associated with other pathways independent of the p53 family, such as polyglutamine aggregation and Wallerian degeneration, both of which are critical in neurodegenerative diseases. Moreover, UBE4B acts as a regulator of epidermal growth factor receptor (EGFR) degradation. It is recruited to endosomes in response to EGFR activation by binding to Hrs, a key component of endosomal sorting complex required for transport (ESCRT) 0, and then regulates endosomal sorting, affecting cellular levels of the EGFR and its downstream signaling. UBE4B contains a ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus.


Pssm-ID: 438320  Cd Length: 74  Bit Score: 166.68  E-value: 1.70e-48
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046888122 1265 YSDAPDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQMLTESMLEPVPELKEQIQAWMREKQ 1338
Cdd:cd16658      1 LGDAPDEFLDPLMDTLMTDPVILPSGTIMDRSIILRHLLNSQTDPFNRQPLTEDMLEPVPELKERIQAWIREKQ 74
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 1268-1338 4.82e-32

U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues.


Pssm-ID: 398320 [Multi-domain]  Cd Length: 73  Bit Score: 119.34  E-value: 4.82e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046888122 1268 APDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLN-SPTDPFNRQMLTESMLEPVPELKEQIQAWMREKQ 1338
Cdd:pfam04564    1 IPDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSvDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEKR 72
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 1271-1333 4.08e-22

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 90.76  E-value: 4.08e-22
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046888122  1271 EFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQMLTESMLEPVPELKEQIQAW 1333
Cdd:smart00504    1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLLSHGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
287-450 7.98e-09

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 60.25  E-value: 7.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  287 PGLSPSFASPSHTAPAASPHSSAPQGAVASQSLSPQSAATHPLSPHSVAP---------QAAVPSPSLSSHSTASVIATG 357
Cdd:PRK07003   383 PGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPpatadrgddAADGDAPVPAKANARASADSR 462

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  358 SQPSS--PRYRPYTVTHLWGSSPCPTPRSSilANPPGFPAHSSSPRAVPASSSRQRPRSRAPAfPPASPSAASRRPSSLR 435
Cdd:PRK07003   463 CDERDaqPPADSGSASAPASDAPPDAAFEP--APRAAAPSAATPAAVPDARAPAAASREDAPA-AAAPPAPEARPPTPAA 539

                          170
                   ....*....|....*
gi 1046888122  436 ISPSLGASGGASTWD 450
Cdd:PRK07003   540 AAPAARAGGAAAALD 554
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 220-457 2.45e-06

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 52.23  E-value: 2.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  220 NPFASLTaTSQPIAT----AARSPDRNLMLNTGSSsgTSPMFCSLGSFSASSLSSLYETSPAPSTSLWSfvpgLSPSFAS 295
Cdd:pfam05109  543 SPTSAVT-TPTPNATsptpAVTTPTPNATIPTLGK--TSPTSAVTTPTPNATSPTVGETSPQANTTNHT----LGGTSST 615

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  296 PSHTAPAASPHSSAPQGavaSQSLSPQSAATHPLSPHSVAPQAavpSPSLSSHSTASV-IATGSQPSS----PRYRPYTV 370
Cdd:pfam05109  616 PVVTSPPKNATSAVTTG---QHNITSSSTSSMSLRPSSISETL---SPSTSDNSTSHMpLLTSAHPTGgeniTQVTPAST 689

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  371 T--HLWGSSPCPTPRSSILANPPGFPAHSSSPRAVPASSSRQRPRSRAPAFPPASPSAAsrrpsslrisPSLGASGGAST 448
Cdd:pfam05109  690 SthHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAV----------PTVTSTGGKAN 759


                   ....*....
gi 1046888122  449 WDSYSDHFT 457
Cdd:pfam05109  760 STTGGKHTT 768
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 287-372 8.46e-03

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 40.24  E-value: 8.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  287 PGLSPSfASPSHTAPAASPHSSAPQGAVAS------QSLSPQSAAT----HPLSPHSVAPQAAVPSPSLSSHSTASVIAT 356
Cdd:cd23959    156 FGQHPP-PAKPLPAAAAAQQSSASPGEVASpfasgtVSASPFATATdtapSSGAPDGFPAEASAPSPFAAPASAASFPAA 234

                           90
                   ....*....|....*.
gi 1046888122  357 GSQPSspryRPYTVTH 372
Cdd:cd23959    235 PVANG----EAATPTH 246
 
Name Accession Description Interval E-value
Ufd2P_core pfam10408
Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ...
 631-1251 0e+00

Ubiquitin elongating factor core; This is the most conserved part of the core region of Ufd2P ubiquitin elongating factor or E4, running from helix alpha-11 to alpha-38. It consists of 31 helices of variable length connected by loops of variable size forming a compact unit; the helical packing pattern of the compact unit consists of five structural repeats that resemble tandem Armadillo (ARM) repeats. This domain is involved in ubiquitination as it binds Cdc48p and escorts ubiquitinated proteins from Cdc48p to the proteasome for degradation. The core is structurally similar to the nuclear transporter protein importin-alpha. The core is associated with the U-box at the C-terminus, pfam04564, which has ligase activity.


Pssm-ID: 463080  Cd Length: 594  Bit Score: 743.24  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  631 LGAFFSFSVFAeDDAKVVEKYFSGPAITLENTRVVSQ-SLQHYLELGRQELFKILHSILLNG-ETREAALSYMAAIVNAN 708
Cdd:pfam10408    1 LGPFLRLSPLP-DDPEVAKKYFSNPKTRSPADIESSQsSLRQELKTLQEQLFQIVNKLLRASpESRERVLDWFAQIINLN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  709 MKKAQMQADDRLVSTDGFMLNLLWVLQQLS------TKIKLETVDPTYIFHPRCRITLPnDETRINATMEDVNEWltelY 782
Cdd:pfam10408   80 HKRRKMQVDPNTVSSDGFMLNLTAVLLRLCepfldaTFSKIDKIDPDYLLPRSSRIDIS-DETRLNADQEEADEF----Y 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  783 GDQPPFSEPKFPTECFFLTLHAHHLSILPSCRRYIRRLRAIRELNRTvedlknnesqwkdsplatrhremlkrcktqlkk 862
Cdd:pfam10408  155 EQKAKEGEPNFITECFFLTLAALHLGILPAISKYKRLARELKRLQAE--------------------------------- 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  863 lvrcKACADAGLLDESFLRRCLNFYGLLIQLMLRVLDPA----YPDITLPLNSEVPKVFAALPEFYVEDVAEFLFFIVQY 938
Cdd:pfam10408  202 ----KLAYEAVLLDPSLLQRSLQFLRFVATWLLRVADPKhqypKKPLKLPLPAEPPEPFKYLPEYFIEDIVDFLLFVTRF 277

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  939 SPQVLY-EPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPSVQ-PRTQKFFEMIENHPLSTKLLVPSLMKFYTD 1016
Cdd:pfam10408  278 APDILEsLSQLDELITFCIVFLRSPEYIKNPHLKAKLVEVLFYGTPPRQnGRPGVLGDILESHPLALKHLLPALMKFYID 357

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122 1017 VEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFMEEFNSGKQ-FVRYINMLINDTTFLLDESLESLKRIHEVQEEM 1095
Cdd:pfam10408  358 VEKTGASSQFYDKFNIRYNISQILKYLWKNPSYREQLKKEAKENEDfFVRFVNLLLNDVTFLLDESLSKLKEIHELQEEM 437

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122 1096 KNQEQWDQLPRDQQQARQSQLAQDERVSRSYLALATETVDMFHLLTKQVQKPFLRPELGPRLAAMLNFNLQQLCGPKCRD 1175
Cdd:pfam10408  438 ADAAEWEALPEEERQEREEQLRSLERQAKSYLQLANETVKLLKLFTKEIPEPFLMPEIVDRLAAMLNYNLDQLVGPKCKN 517

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046888122 1176 LKVENPEKYGFEPKKLLDQLTDIYLQLDCA-RFAKAIADDQRSYSKELFEEVISKMRKAGIKSTIAIEKFKLLAEKV 1251
Cdd:pfam10408  518 LKVKNPEKYGFNPKELLSDIVDIYLNLSDQpEFVRAVARDGRSYSPELFEKAARILRRKGLKSPEEIEKFEELAQKV 594
UFD2 COG5113
Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, ...
 536-1337 9.40e-131

Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227444 [Multi-domain]  Cd Length: 929  Bit Score: 426.32  E-value: 9.40e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  536 NLPYGFIQELVRTTHQDEEVFKQIFIPILQGLARaaKECSLDSDYFKYPLMALGELcetkFGKTHPMCNLVASLPLWLPk 615
Cdd:COG5113    129 LLPMIFLSSFKQRQLDEASNLDNLFTSALEALTG--LHGVLEEDTVLKNVMEIYWG----LVNTKPIADVILKFPIYSG- 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  616 SLSPGsgrELQRLSYLGAFFSFSVFAEDdakVVEKYFSGPAI-TLENTRVVSQSLQHYLELGRQELFKILHSILLNG-ET 693
Cdd:COG5113    202 TNFPC---GFEYKTLLGFIESLSYKKCD---VAARALDYLGIrSRQVVEKSRRSLRLTLSDHSDKLFQIIHSLVRSSkEL 275

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  694 REAALSYMAAIVNANMKKAQMQADDRLVSTDGFMLNLLWVLQQLSTKI------KLETVDPTYIFHPRCRITlpnDETRI 767
Cdd:COG5113    276 RANFMKYFAKVINVNHERSKTIFSWRENISDGFMYNMSMVLSRFSRPFldigcsKIDMVDKIYFNNPRVDIK---EETKL 352

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  768 NatmedVNEWLTELYGDQPPFSEPKFPTECFFLTLHAHHLSI---LPSCRRYIRRLRAIRELNRTVEDLKNNESQwkdsp 844
Cdd:COG5113    353 N-----VDEKSLDSFYTKPAEGSNNFISDIFFLYLTKIHYGVnatFTSCEKFGEYIRKLKESLEYECRLLDGSFQ----- 422

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  845 lATRHREMLKRCKTQLKKLVRCKACADAGLLDESFLRRCLNFYGLLIQLMLRVLDP--AYP--DITLPLNSEVPKVFAAL 920
Cdd:COG5113    423 -ATRLTAQLSRMEAYLKGIDSKMSALNGFLFMTSLFADEFPFTDFMTEYLARVEDPwpTYPfyYKTLPWMENAPMTFKLI 501

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  921 PEFYVEDVAEFLFFIVQYSPQVLYEPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPSVQPRTQKFF-EMIENH 999
Cdd:COG5113    502 PEATIENALNYVLESIKDWRSPIFKKELEPLCEFVKIVLHRSSAIKNPMLNRKLDYYLSLGRDEMRMESRSIIhDIFKEG 581

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122 1000 PLSTKLLVPSLMKFYTDVEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFM-EEFNSGKQFVRYINMLINDTTFLL 1078
Cdd:COG5113    582 KVFSRWLLPALMAFYIEIESTGQSTQFYDKFNIRFIICMMKDFEYKQPSYSEGLSsIKDTNLPFFVKFDAKMLNDLTRLL 661

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122 1079 DESLESLKRIHEVQEEMKNQEQWDQLPRDQQQArQSQLAQDERVSRSYLALATETVDMFHLLTKQVQKPFLRPELGPRLA 1158
Cdd:COG5113    662 DEALKELVEEHNIQSLLADAISNSNISERIGEL-QKSLAFAKRQARNSCLLVDGCFDLFTHILDEIPDAFLVDEIVSRLA 740

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122 1159 AMLNFNLQQLCGPKCRDLKVENPEKYGFEPKKLLDQLTDIYLQL-DCARFAKAIADDQRSYSKELFEEVISKMRKAGIKS 1237
Cdd:COG5113    741 RMLNYNLKILTGPKCTDLKVKDPEQYGFNAKNLLRRMVMVYINLrSESKFVEAVASDKRSFDIDFFRRALRICENKYLIS 820

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122 1238 TIAIEKFKLLAEKVEEIVAKNARAEIDYSDAPDEFRDPLMDTLMTDPVRLP-SGTIMDRSIILRHLLNSPTDPFNRQMLT 1316
Cdd:COG5113    821 ESQIEELRSFINRLEKVRVIEAVEEEDMGDVPDEFLDPLMFTIMKDPVKLPtSRITIDRSTIKAHLLSDGTDPFNRMPLT 900

                          810       820
                   ....*....|....*....|.
gi 1046888122 1317 ESMLEPVPELKEQIQAWMREK 1337
Cdd:COG5113    901 LDDVTPNAELREKINRFYKCK 921
RING-Ubox_UBE4B cd16658
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and ...
 1265-1338 1.70e-48

U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and similar proteins; UBE4B, also known as UFD2a, is a U-box-type ubiquitin-protein ligase that functions as an E3 ubiquitin ligase and an E4 polyubiquitin chain elongation factor, which catalyzes formation of Lys27- and Lys33-linked polyubiquitin chains rather than the Lys48-linked chain. It is a mammalian homolog of yeast UFD2 ubiquitination factor and it participates in the proteasomal degradation of misfolded or damaged proteins through association with chaperones. It is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. UBE4B has contradictory functions upon tumorigenesis as an oncogene or tumor suppressor in different types of cancers. It is essential for Hdm2 (also known as Mdm2)-mediated p53 degradation. It mediates p53 polyubiquitination and degradation, as well as inhibits p53-dependent transactivation and apoptosis, and thus plays an important role in regulating phosphorylated p53 following DNA damage. UBE4B is also associated with other pathways independent of the p53 family, such as polyglutamine aggregation and Wallerian degeneration, both of which are critical in neurodegenerative diseases. Moreover, UBE4B acts as a regulator of epidermal growth factor receptor (EGFR) degradation. It is recruited to endosomes in response to EGFR activation by binding to Hrs, a key component of endosomal sorting complex required for transport (ESCRT) 0, and then regulates endosomal sorting, affecting cellular levels of the EGFR and its downstream signaling. UBE4B contains a ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus.


Pssm-ID: 438320  Cd Length: 74  Bit Score: 166.68  E-value: 1.70e-48
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046888122 1265 YSDAPDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQMLTESMLEPVPELKEQIQAWMREKQ 1338
Cdd:cd16658      1 LGDAPDEFLDPLMDTLMTDPVILPSGTIMDRSIILRHLLNSQTDPFNRQPLTEDMLEPVPELKERIQAWIREKQ 74
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 1268-1338 4.82e-32

U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues.


Pssm-ID: 398320 [Multi-domain]  Cd Length: 73  Bit Score: 119.34  E-value: 4.82e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046888122 1268 APDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLN-SPTDPFNRQMLTESMLEPVPELKEQIQAWMREKQ 1338
Cdd:pfam04564    1 IPDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSvDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEKR 72
RING-Ubox_UBE4A cd16657
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 A (UBE4A) and ...
 1270-1338 3.94e-28

U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 A (UBE4A) and similar proteins; This subfamily includes yeast ubiquitin fusion degradation protein 2 (UFD2p) and its mammalian homolog, UBE4A. Yeast UFD2p, also known as ubiquitin conjugation factor E4 or UB fusion protein 2, is a polyubiquitin chain conjugation factor (E4) in the ubiquitin fusion degradation (UFD) pathway which catalyzes elongation of the ubiquitin chain through Lys48 linkage. It binds to substrates conjugated with one to three ubiquitin molecules and catalyzes the addition of further ubiquitin moieties in the presence of ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2) and ubiquitin ligase (E3), yielding multiubiquitylated substrates that are targets for the 26S proteasome. UFD2p is implicated in cell survival under stress conditions and is essential for homoeostasis of unsaturated fatty acids. It interacts with UBL-UBA proteins Rad23 and Dsk2, which are involved in the endoplasmic reticulum-associated degradation, ubiquitin fusion degradation, and OLE-1 gene induction pathways. UBE4A is a U-box-type ubiquitin-protein ligase that is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. It may have a specific role in different biochemical processes other than ubiquitination, including growth or differentiation. Members of this family contain an N-terminal ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus.


Pssm-ID: 438319  Cd Length: 70  Bit Score: 108.13  E-value: 3.94e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122 1270 DEFRDPLMDTLMTDPVRLP-SGTIMDRSIILRHLLNSPTDPFNRQMLTESMLEPVPELKEQIQAWMREKQ 1338
Cdd:cd16657      1 DEFLDPIMYTLMKDPVILPsSKVTVDRSTIKRHLLSDQTDPFNRSPLTLDMVIPNEELKQKIEEFLAEKK 70
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 1271-1333 4.08e-22

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 90.76  E-value: 4.08e-22
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046888122  1271 EFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQMLTESMLEPVPELKEQIQAW 1333
Cdd:smart00504    1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLLSHGTDPVTGQPLTHEDLIPNLALKSAIQEW 63
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
 1272-1315 5.65e-15

U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that also includes the HECT family and the RING finger family. The E3 enzyme is ubiquitin-protein ligase that cooperates with a ubiquitin-activating enzyme (E1) and a ubiquitin-conjugating enzyme (E2), and plays a central role in determining the specificity of the ubiquitination system. It removes the ubiquitin molecule from the E2 enzyme and attaches it to the target substrate, forming a covalent bond between ubiquitin and the target. U-box proteins are characterized by the presence of a U-box domain of approximately 70 amino acids. The U-box is a modified form of the RING finger domain that lacks metal chelating cysteines and histidines. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms.


Pssm-ID: 438117 [Multi-domain]  Cd Length: 44  Bit Score: 69.89  E-value: 5.65e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1046888122 1272 FRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQML 1315
Cdd:cd16453      1 FLCPISGELMKDPVITPSGITYDRSAIERWLLSDNTDPFTREPL 44
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
 1268-1336 9.91e-12

U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein (CHIP) and similar proteins; CHIP, also known as STIP1 homology and U box-containing protein 1 (STUB1), CLL-associated antigen KW-8, or Antigen NY-CO-7, is a multifunctional protein that functions both as a co-chaperone and an E3 ubiquitin-protein ligase. It couples protein folding and proteasome mediated degradation by interacting with heat shock proteins (e.g. HSC70) and ubiquitinating their misfolded client proteins, thereby targeting them for proteasomal degradation. It is also important for cellular differentiation and survival (or apoptosis), as well as susceptibility to stress. It targets a wide range of proteins, such as expanded ataxin-1, ataxin-3, huntingtin, and androgen receptor, which play roles in glucocorticoid response, tau degradation, and both p53 and cAMP signaling. CHIP contains an N-terminal tetratricopeptide repeat (TPR) domain responsible for protein-protein interaction, a highly charged middle coiled-coil (CC), and a C-terminal RING-like U-box domain acting as an ubiquitin ligase.


Pssm-ID: 438316 [Multi-domain]  Cd Length: 71  Bit Score: 61.44  E-value: 9.91e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122 1268 APDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLL-NSPTDPFNRQMLTESMLEPVPELKEQIQAWMRE 1336
Cdd:cd16654      1 VPDYLCCKISFELMRDPVITPSGITYERKDIEEHLQrVGHFDPITREPLTQDQLIPNLALKEAIEAFLEE 70
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
287-450 7.98e-09

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 60.25  E-value: 7.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  287 PGLSPSFASPSHTAPAASPHSSAPQGAVASQSLSPQSAATHPLSPHSVAP---------QAAVPSPSLSSHSTASVIATG 357
Cdd:PRK07003   383 PGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPpatadrgddAADGDAPVPAKANARASADSR 462

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  358 SQPSS--PRYRPYTVTHLWGSSPCPTPRSSilANPPGFPAHSSSPRAVPASSSRQRPRSRAPAfPPASPSAASRRPSSLR 435
Cdd:PRK07003   463 CDERDaqPPADSGSASAPASDAPPDAAFEP--APRAAAPSAATPAAVPDARAPAAASREDAPA-AAAPPAPEARPPTPAA 539

                          170
                   ....*....|....*
gi 1046888122  436 ISPSLGASGGASTWD 450
Cdd:PRK07003   540 AAPAARAGGAAAALD 554
RING-Ubox_RNF37 cd16660
U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also ...
 1269-1310 9.25e-09

U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also known as KIAA0860, U-box domain-containing protein 5 (UBOX5), UbcM4-interacting protein 5 (UIP5), or ubiquitin-conjugating enzyme 7-interacting protein 5, is an E3 ubiquitin-protein ligase found exclusively in the nucleus as part of a nuclear dot-like structure. It interacts with the molecular chaperone VCP/p97 protein. RNF37 contains a U-box domain followed by a potential nuclear location signal (NLS), and a C-terminal C3HC4-type RING-HC finger. The U-box domain is a modified RING finger domain that lacks the hallmark metal-chelating cysteines and histidines of the latter, but is likely to adopt a RING finger-like conformation. The presence of the U-box, but not of the RING finger, is required for the E3 activity. The U-box domain can directly interact with several E2 enzymes, including UbcM2, UbcM3, UbcM4, UbcH5, and UbcH8, suggesting a similar function as the RING finger in the ubiquitination pathway. This model corresponds to the U-box domain.


Pssm-ID: 438322  Cd Length: 53  Bit Score: 52.70  E-value: 9.25e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1046888122 1269 PDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNS------PTDPF 1310
Cdd:cd16660      1 PEEFLDPITCELMTLPVLLPSGKVVDQSTLEKYIKEEatwgrlPSDPF 48
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 227-451 9.57e-08

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 57.10  E-value: 9.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  227 ATSQPIATAARSPDRNLMLNTGSSSGTSPMFCSLGSFSASSLSSLYET---SPAPS---TSLWSFVPGLSPSfASPSHTA 300
Cdd:PHA03307   208 RRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECplpRPAPItlpTRIWEASGWNGPS-SRPGPAS 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  301 PAASPHSSAPQgAVASQSLSPQSAATHPLSPHSVAPQAAVPSPSLSSHSTASviATGSQPSSPRYRPYTVTHLWGSSPCP 380
Cdd:PHA03307   287 SSSSPRERSPS-PSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSR--GAAVSPGPSPSRSPSPSRPPPPADPS 363

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  381 TPRSSILANP-PGFPAHSS----SPRAVPASSSRQRPRSRAPAF----PPASPSAASRRPSSLRISPSLGASGGASTWDS 451
Cdd:PHA03307   364 SPRKRPRPSRaPSSPAASAgrptRRRARAAVAGRARRRDATGRFpagrPRPSPLDAGAASGAFYARYPLLTPSGEPWPGS 443
RING-Ubox_LubX-like_rpt1 cd23149
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ...
 1275-1326 6.97e-07

first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the first one.


Pssm-ID: 438511 [Multi-domain]  Cd Length: 55  Bit Score: 47.48  E-value: 6.97e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1046888122 1275 PLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQMLTESMLEPVPEL 1326
Cdd:cd23149      4 PITSGFMEDPVITPSGFSYERSAIERWLETKPEDPQTREPLTAKDLQPNREL 55
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 227-461 7.58e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 54.02  E-value: 7.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  227 ATSQPIATAARS-PDRNLMLNTGSSSGTSPMFCSLGSFSASSLSSLYETSPAPSTSLWSFVPGLSPSFASPSHTAPaasP 305
Cdd:PHA03307   119 PTPPPASPPPSPaPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPP---P 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  306 HSSAPQGAVASQSLSPQSAATHPLSPHSVAPQAAVP---SPSLSSHSTASVIATGSQPSSPRYRPYTVTHLwgsspcPTP 382
Cdd:PHA03307   196 STPPAAASPRPPRRSSPISASASSPAPAPGRSAADDagaSSSDSSSSESSGCGWGPENECPLPRPAPITLP------TRI 269

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  383 RSSILANPPGFPAHSSSPRAVPAsssrqrprsraPAFPPASPSAASRR--PSSLRISPSLGASGGASTWDSYSDHFTIET 460
Cdd:PHA03307   270 WEASGWNGPSSRPGPASSSSSPR-----------ERSPSPSPSSPGSGpaPSSPRASSSSSSSRESSSSSTSSSSESSRG 338


                   .
gi 1046888122  461 C 461
Cdd:PHA03307   339 A 339
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 220-457 2.45e-06

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 52.23  E-value: 2.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  220 NPFASLTaTSQPIAT----AARSPDRNLMLNTGSSsgTSPMFCSLGSFSASSLSSLYETSPAPSTSLWSfvpgLSPSFAS 295
Cdd:pfam05109  543 SPTSAVT-TPTPNATsptpAVTTPTPNATIPTLGK--TSPTSAVTTPTPNATSPTVGETSPQANTTNHT----LGGTSST 615

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  296 PSHTAPAASPHSSAPQGavaSQSLSPQSAATHPLSPHSVAPQAavpSPSLSSHSTASV-IATGSQPSS----PRYRPYTV 370
Cdd:pfam05109  616 PVVTSPPKNATSAVTTG---QHNITSSSTSSMSLRPSSISETL---SPSTSDNSTSHMpLLTSAHPTGgeniTQVTPAST 689

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  371 T--HLWGSSPCPTPRSSILANPPGFPAHSSSPRAVPASSSRQRPRSRAPAFPPASPSAAsrrpsslrisPSLGASGGAST 448
Cdd:pfam05109  690 SthHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAV----------PTVTSTGGKAN 759


                   ....*....
gi 1046888122  449 WDSYSDHFT 457
Cdd:pfam05109  760 STTGGKHTT 768
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 273-448 4.47e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 51.33  E-value: 4.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  273 ETSPAPSTSLWSFVPGLSPSFASPSH-------TAPAASPHSSAPQGAVASQSLSPQSAATHPLSPHSVAPQAAVPSPSL 345
Cdd:PHA03307   181 ETARAPSSPPAEPPPSTPPAAASPRPprrsspiSASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRP 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  346 SSHSTASVIATGSQPSSPRYRPYTVThlwGSSPCPTPRSSILANPPGFPAHSSSPRAVPASSSRQRPRSRAPAF------ 419
Cdd:PHA03307   261 APITLPTRIWEASGWNGPSSRPGPAS---SSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSssessr 337

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1046888122  420 --------------------PPASPSAASRRPSSLRISPSLGASGGAST 448
Cdd:PHA03307   338 gaavspgpspsrspspsrppPPADPSSPRKRPRPSRAPSSPAASAGRPT 386
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
248-450 6.63e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 50.64  E-value: 6.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  248 GSSSGTSPMFCSLGSFSASSLSSLYETSPAPSTSLWSFVPGLSPSFASPSHTAPAA----SPHSSAPQGAVASQSLSPQS 323
Cdd:PRK12323   367 QSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAparrSPAPEALAAARQASARGPGG 446

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  324 AATHPLSPHSVaPQAAVPSPSLSSHSTASVIATGSQPSSPRYRPYTVTHL---WGSSPCPTPRSSILANPPGFPAHSSSP 400
Cdd:PRK12323   447 APAPAPAPAAA-PAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDpppWEELPPEFASPAPAQPDAAPAGWVAES 525

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1046888122  401 RAVPASSSRQRPRSRAPAFPPASPSAASRRPSSLRIS---PSLGASGGASTWD 450
Cdd:PRK12323   526 IPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAprpPRASASGLPDMFD 578
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 273-453 6.99e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.94  E-value: 6.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  273 ETSPAPSTSLWSFVPGLSPSFA-SPSHTAPAASPHSSAPqGAVASQSLSPQSAATHPLSP-HSVAPQAAVP---SPSLSS 347
Cdd:PHA03307    68 PTGPPPGPGTEAPANESRSTPTwSLSTLAPASPAREGSP-TPPGPSSPDPPPPTPPPASPpPSPAPDLSEMlrpVGSPGP 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  348 HSTASVIATGSQPSSPryrpytvthlwGSSPCPTPRSSILANPPGFPAHSSSPRAVPASSSRQRPRSRAPAFPPASPSAA 427
Cdd:PHA03307   147 PPAASPPAAGASPAAV-----------ASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISA 215

                          170       180
                   ....*....|....*....|....*.
gi 1046888122  428 SRRPSSLRISPSLGASGGASTWDSYS 453
Cdd:PHA03307   216 SASSPAPAPGRSAADDAGASSSDSSS 241
PHA03247 PHA03247
large tegument protein UL36; Provisional
 276-450 1.49e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  276 PAPSTSLWSFVPGLSPSFASPSHTAPA-------ASPHSSAPQGAVASQSLSPQSAATHPLSPHSVAPQAAV-----PSP 343
Cdd:PHA03247  2627 PPPSPSPAANEPDPHPPPTVPPPERPRddpapgrVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLadpppPPP 2706

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  344 SLSSHSTASVIATGSQPSSPRYRPYTVTHLWGSSPCPTPRSSIL---ANPPGFPAHSSSPRAvPAsssrqrprsrAPAFP 420
Cdd:PHA03247  2707 TPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATpggPARPARPPTTAGPPA-PA----------PPAAP 2775

                          170       180       190
                   ....*....|....*....|....*....|
gi 1046888122  421 PASPSAASRRPSSLRISPSLGASggASTWD 450
Cdd:PHA03247  2776 AAGPPRRLTRPAVASLSESRESL--PSPWD 2803
PHA03247 PHA03247
large tegument protein UL36; Provisional
 221-437 2.34e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 2.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  221 PFASLTATSQPIATAARSPDRNLMLNTGSSSGTSPMFCSLGSFSASSLSSLYETSPAPSTSLWSFVPGLSPSFASPSHTA 300
Cdd:PHA03247  2691 TVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPA 2770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  301 PAASPHSSAPQGAV--ASQSLSPqSAATHPLSPHSVAPQAAVPSPslsshstASVIATGSQPSSPryrpytvthlwgSSP 378
Cdd:PHA03247  2771 PPAAPAAGPPRRLTrpAVASLSE-SRESLPSPWDPADPPAAVLAP-------AAALPPAASPAGP------------LPP 2830

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1046888122  379 CPTPRSSILANPPGFPAHSSSPRAvpASSSRQRPRSRAPAFPPASPSAASRRPSSLRIS 437
Cdd:PHA03247  2831 PTSAQPTAPPPPPGPPPPSLPLGG--SVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLA 2887
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 287-425 3.88e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 48.22  E-value: 3.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  287 PGLSPSFASPSHTAPAASP--------------HSSAPQGAVASQSLSPqSAATHP--LSPHSVAPQAAVPSPSLSSHST 350
Cdd:pfam03154  394 PALKPLSSLSTHHPPSAHPpplqlmpqsqqlppPPAQPPVLTQSQSLPP-PAASHPptSGLHQVPSQSPFPQHPFVPGGP 472

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046888122  351 ASVI-ATGSQPSSPRYRPytvthlwGSSPCPTPRSSILANPPGFPAHSSSPRAVPASSSRQRPRSRAPAFPPASPS 425
Cdd:pfam03154  473 PPITpPSGPPTSTSSAMP-------GIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPS 541
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
277-450 4.64e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 47.92  E-value: 4.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  277 APSTSLWSFVPGLSPsfASPSHTAPAASPHSSAPQGAVASQSLSPQSAA-THPLSPHSVAPQAAVPSPSLSSHSTASVIA 355
Cdd:PRK07003   359 EPAVTGGGAPGGGVP--ARVAGAVPAPGARAAAAVGASAVPAVTAVTGAaGAALAPKAAAAAAATRAEAPPAAPAPPATA 436

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  356 TGSQPSSPryrpytvthlwGSSPCPTPRSSILANPPGFPAHSSSPRAVPASSSRQRPRSRAPAFPPASPSAASRRPSSLR 435
Cdd:PRK07003   437 DRGDDAAD-----------GDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPA 505

                          170
                   ....*....|....*
gi 1046888122  436 ISPSLGASGGASTWD 450
Cdd:PRK07003   506 AVPDARAPAAASRED 520
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
 1269-1322 5.72e-05

U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing protein 1 (WDSUB1) and similar proteins; WDSUB1 is an uncharacterized protein containing seven WD40 repeats and a SAM domain in addition to the U-box. Its biological role remains unclear. This subfamily also includes many uncharacterized kinase domain-containing U-box (AtPUB) proteins and several MIF4G motif-containing AtPUB proteins from Arabidopsis.


Pssm-ID: 438317 [Multi-domain]  Cd Length: 55  Bit Score: 42.10  E-value: 5.72e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1046888122 1269 PDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQMLTESMLEP 1322
Cdd:cd16655      1 PDEFLCPITQELMRDPVVAADGHTYERSAIEEWLETHNTSPMTRLPLSSTDLVP 54
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 218-404 6.11e-05

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: 47.26  E-value: 6.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  218 DENPFASLTATSQPIATAARSPDRNLMLNTGSSSGT----------SPMFCSLGSFSASSLSSLYETSPAPSTSLWSfvp 287
Cdd:pfam17823   45 DAVPRADNKSSEQ*NFCAATAAPAPVTLTKGTSAAHlnstevtaehTPHGTDLSEPATREGAADGAASRALAAAASS--- 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  288 glSPSFASPSHTAPAASPHS---SAPQGAVASqslSPQSAATHPLSPHSVAPQAAVPSPSLSSHSTASVIATGSQPSSPR 364
Cdd:pfam17823  122 --SPSSAAQSLPAAIAALPSeafSAPRAAACR---ANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPT 196

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1046888122  365 YRPYTVThlwgSSPCPTPRSSILANPPGFPAHSSSPRAVP 404
Cdd:pfam17823  197 TAASSAP----ATLTPARGISTAATATGHPAAGTALAAVG 232
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
 1269-1320 6.53e-05

U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and similar proteins; The plant PUB proteins, also known as U-box domain-containing proteins, are much more numerous in Arabidopsis which has 62 in comparison with the typical 6 in most animals. The majority of AtPUBs in this subfamily are known as ARM domain-containing PUB proteins, containing a C-terminally-located, tandem ARM (armadillo) repeat protein-interaction region in addition to the U-box domain. They have been implicated in the regulation of cell death and defense. They also play important roles in other plant-specific pathways, such as controlling both self-incompatibility and pseudo-self-incompatibility, as well as acting in abiotic stress. A subgroup of ARM domain-containing PUB proteins harbors a plant-specific U-box N-terminal domain.


Pssm-ID: 438326 [Multi-domain]  Cd Length: 53  Bit Score: 41.78  E-value: 6.53e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1046888122 1269 PDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHL-LNSPTDPFNRQMLTESML 1320
Cdd:cd16664      1 PEEFICPISLELMKDPVILATGQTYERAAIEKWLdSGNNTCPITGQPLTHTDL 53
RING-Ubox_LubX-like_rpt2 cd23150
second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein ...
 1269-1337 8.65e-05

second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the second one.


Pssm-ID: 438512 [Multi-domain]  Cd Length: 69  Bit Score: 42.07  E-value: 8.65e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046888122 1269 PDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQMLTESMLEPVPELKEQIQAWMREK 1337
Cdd:cd23150      1 PDIFLCPISKTLIKTPVITAQGKVYDQEALSNFLIATGNKDETGKKLSIDDVVVFDELYQQIKVYNFYR 69
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 278-434 1.16e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 46.63  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  278 PSTSLWSFVPGLSPSFASPSHTAPAASPhssAPQGAVASQSLSPQSAAThplsphSVAPQAAVPSPSLSSHSTASVIATG 357
Cdd:PRK14951   366 PAAAAEAAAPAEKKTPARPEAAAPAAAP---VAQAAAAPAPAAAPAAAA------SAPAAPPAAAPPAPVAAPAAAAPAA 436

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046888122  358 SQPSSPryrpytvthlwgsspcptprSSILANPPGFPAHSSSPRAVPASSSRQRPRSRAPAFPPASPSAASRRPSSL 434
Cdd:PRK14951   437 APAAAP--------------------AAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEE 493
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 287-432 2.39e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 2.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  287 PGLSPSFASPSHTAPAASPHSSAPQGAVASQSLSPQSAATHPLSPHSVAPQAAVPSPSLSSHSTASVIATGSQPSSPRYR 366
Cdd:PRK07764   390 GAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPA 469

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046888122  367 PytvthlwGSSPCPTPRSSilanPPGFPAHSSSPRAVPAsssrqrprsRAPAFPPASPSAASRRPS 432
Cdd:PRK07764   470 P-------AAAPEPTAAPA----PAPPAAPAPAAAPAAP---------AAPAAPAGADDAATLRER 515
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
302-438 2.43e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 45.64  E-value: 2.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  302 AASPHSSAPQGAVASQSLSPQSAATHPLSPHSVAPQAAVPSPSLSSHSTASVIATGSQPSSPRYRPYTVTHLWGSSPCPT 381
Cdd:PRK12323   362 AFRPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASA 441

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1046888122  382 PRSSILANPPGFPAHSSSPRAVPASSSRQRPRSRAPAFPPASPSAASRRPSSLRISP 438
Cdd:PRK12323   442 RGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPP 498
PHA03247 PHA03247
large tegument protein UL36; Provisional
 273-448 2.62e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 2.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  273 ETSP-APSTSLWSFVPGlSPSFASPSHTAPAASPHSSAPQGAVASqslSPQSAATHPLSPHSVA------PQAAVPSPSL 345
Cdd:PHA03247  2586 ARRPdAPPQSARPRAPV-DDRGDPRGPAPPSPLPPDTHAPDPPPP---SPSPAANEPDPHPPPTvppperPRDDPAPGRV 2661

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  346 SSHSTASVIATGSQPSSP--RYRPYTVTHLWGS--------------SPCPTPRSSILANPPGFPAHSSSPRAVPAsssr 409
Cdd:PHA03247  2662 SRPRRARRLGRAAQASSPpqRPRRRAARPTVGSltsladpppppptpEPAPHALVSATPLPPGPAAARQASPALPA---- 2737

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1046888122  410 qrprsrAPAFPPASPSAASRRPSSLRISPSLGASGGAST 448
Cdd:PHA03247  2738 ------APAPPAVPAGPATPGGPARPARPPTTAGPPAPA 2770
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 276-446 3.11e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 3.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  276 PAPSTSLWSFVPGLSPSFASPSHTAPAASPHSSAPQGAvasqslSPQSAATHPLSPHSVAPQAAVPSPSLSSHSTASVIA 355
Cdd:PRK07764   590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAP------APAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAS 663

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  356 TGSQPSSPRYRPYTvthlwGSSPCPTPRSSILANPPGFPAHSSSPRAVPAsssrqrprsrAPAFPPASPSAASRRPSSLR 435
Cdd:PRK07764   664 DGGDGWPAKAGGAA-----PAAPPPAPAPAAPAAPAGAAPAQPAPAPAAT----------PPAGQADDPAAQPPQAAQGA 728

                          170
                   ....*....|.
gi 1046888122  436 ISPSLGASGGA 446
Cdd:PRK07764   729 SAPSPAADDPV 739
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 287-455 3.13e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.55  E-value: 3.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  287 PGLSPSFASPSHTAPAASP-HSSAPQGAVASQSLSPQSAATHPLSPHSVAPQAAVPSPSLSSHSTASVIATGSQ----PS 361
Cdd:PHA03307   108 PPGPSSPDPPPPTPPPASPpPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEEtaraPS 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  362 SPRYRPYTVTHLWGSSPCPTPRSSILANP-----------PGFPAHSSS-------------------PRAVPASSSRQR 411
Cdd:PHA03307   188 SPPAEPPPSTPPAAASPRPPRRSSPISASasspapapgrsAADDAGASSsdssssessgcgwgpenecPLPRPAPITLPT 267

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1046888122  412 PRSRA------PAFPPASPSAASRRPSSLRISPSLGASGGASTWDSYSDH 455
Cdd:PHA03307   268 RIWEAsgwngpSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSS 317
PHA03247 PHA03247
large tegument protein UL36; Provisional
 219-442 3.70e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 3.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  219 ENPFASLTATSQPIATA-----ARSPDRNLMLNTGSSSgtSPMFCSLGSFSASSLSSLYETSPAPSTSLWSFVPGLSPSF 293
Cdd:PHA03247  2754 PARPARPPTTAGPPAPAppaapAAGPPRRLTRPAVASL--SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP 2831

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  294 ASPSHTAPAA----SPHSSAPQGAVA-----SQSLSPQSAATHPLSP-HSVAPQAAVPSPSLSSHSTAsviatgsQPSSP 363
Cdd:PHA03247  2832 TSAQPTAPPPppgpPPPSLPLGGSVApggdvRRRPPSRSPAAKPAAPaRPPVRRLARPAVSRSTESFA-------LPPDQ 2904

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046888122  364 RYRPytvthlwgsspcPTPRSSilanPPGFPAHSSSPRAVPASSSRQRPRSRAPAFPPASPSAASrRPSSLRISPSLGA 442
Cdd:PHA03247  2905 PERP------------PQPQAP----PPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAG-EPSGAVPQPWLGA 2966
PHA03378 PHA03378
EBNA-3B; Provisional
 276-446 5.72e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.29  E-value: 5.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  276 PAPSTSLWSFVPGLSPSFA-----SPSHTA-PAASPHSSAPQGAVASQSLSPQSAA----THPLSPHSVAPQAAVPSP-- 343
Cdd:PHA03378   565 PAPGLGPLQIQPLTSPTTSqlassAPSYAQtPWPVPHPSQTPEPPTTQSHIPETSAprqwPMPLRPIPMRPLRMQPITfn 644

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  344 ---SLSSHSTASVIATGSQPS--SPRYRPYtvthlwgsSPCPTPRSSILAnPPGFPAHSSSPRAVPAsssrqrprsraPA 418
Cdd:PHA03378   645 vlvFPTPHQPPQVEITPYKPTwtQIGHIPY--------QPSPTGANTMLP-IQWAPGTMQPPPRAPT-----------PM 704

                          170       180       190
                   ....*....|....*....|....*....|
gi 1046888122  419 FPPASPSAASRRP--SSLRISPSLGASGGA 446
Cdd:PHA03378   705 RPPAAPPGRAQRPaaATGRARPPAAAPGRA 734
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 274-443 7.69e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.14  E-value: 7.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  274 TSPAPSTS-LWSFVPGLSPSFASPshTAPAASPHSSAPQGAvASQSLSPQSAATHPlSPHSVAPQAAVP-------SPSL 345
Cdd:pfam05109  464 TGPTVSTAdVTSPTPAGTTSGASP--VTPSPSPRDNGTESK-APDMTSPTSAVTTP-TPNATSPTPAVTtptpnatSPTL 539

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  346 SSHSTASVIATGSqPSSPRYRPYTVThlwgsspcPTPRSSIlanppgfpahssspravpasssrqrprsraPAFPPASPS 425
Cdd:pfam05109  540 GKTSPTSAVTTPT-PNATSPTPAVTT--------PTPNATI------------------------------PTLGKTSPT 580

                          170
                   ....*....|....*...
gi 1046888122  426 AASRRPSSLRISPSLGAS 443
Cdd:pfam05109  581 SAVTTPTPNATSPTVGET 598
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 226-431 8.68e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 8.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  226 TATSQPIATAARSPDrnlmlnTGSSSGTSPMFCSLGSFSASSLSSLYETSPAPSTSLWSfVPGLSPSFASPSHTAPAASP 305
Cdd:PRK07764   616 AAPAAPAAPAAPAPA------GAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDG-WPAKAGGAAPAAPPPAPAPA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  306 HSSAPQGAVAsqslsPQSAATHPLSPHSVAPQAAVPSPSLSSHSTASViatgsQPSSPRYRPytvthlwgssPCPTPRss 385
Cdd:PRK07764   689 APAAPAGAAP-----AQPAPAPAATPPAGQADDPAAQPPQAAQGASAP-----SPAADDPVP----------LPPEPD-- 746

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1046888122  386 ilaNPPGFPAHSSSPRAVPAsssrqrprsRAPAFPPASPSAASRRP 431
Cdd:PRK07764   747 ---DPPDPAGAPAQPPPPPA---------PAPAAAPAAAPPPSPPS 780
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 277-427 1.03e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 43.38  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  277 APSTSLWSFVPGLSPSFASPSHTAPAASPHSSAPQGAVASQSLSPQSAA--------------THPLSPHSVAPQ---AA 339
Cdd:PLN03209   372 SPYTAYEDLKPPTSPIPTPPSSSPASSKSVDAVAKPAEPDVVPSPGSASnvpevepaqveakkTRPLSPYARYEDlkpPT 451

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  340 VPSPSLSSHSTASVIATGSQPSSPRYRPYTV--THLWGSSPCPTPRSSILANPPGFPAHSSSPRAVPASSSRQRPRSRAP 417
Cdd:PLN03209   452 SPSPTAPTGVSPSVSSTSSVPAVPDTAPATAatDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVK 531

                          170
                   ....*....|
gi 1046888122  418 AFPPASPSAA 427
Cdd:PLN03209   532 VGNSAPPTAL 541
PHA03247 PHA03247
large tegument protein UL36; Provisional
 276-445 1.16e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  276 PAPSTSLWSFV--PGLSPSFASPSHTAPAASPHSSAPQGAVASQ-----SLSPQSAATHPLSPHSVAPQAAVPSPSLSSH 348
Cdd:PHA03247  2689 RPTVGSLTSLAdpPPPPPTPEPAPHALVSATPLPPGPAAARQASpalpaAPAPPAVPAGPATPGGPARPARPPTTAGPPA 2768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  349 STA-SVIATGSQPSSPRYRpytvthlwGSSPCPTPRSSILANPPGFPAHSSSPRAvPASSSRQRPRSRAPafPPASPSAA 427
Cdd:PHA03247  2769 PAPpAAPAAGPPRRLTRPA--------VASLSESRESLPSPWDPADPPAAVLAPA-AALPPAASPAGPLP--PPTSAQPT 2837

                          170
                   ....*....|....*...
gi 1046888122  428 SRRPSSLRISPSLGASGG 445
Cdd:PHA03247  2838 APPPPPGPPPPSLPLGGS 2855
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 286-438 1.21e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.54  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  286 VPGLSPSFASPS-HTAPAASPHSSAPQGAVASQSLSPQSAATHPLSPHSVAPQAAVPSPSLSSHSTASviatgSQPSSPR 364
Cdd:PRK10263   346 VASVDVPPAQPTvAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAE-----QPAQQPY 420

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046888122  365 YRPYTVTHLWGSSPCPTPRSSILANPPGFPAHSSSPRAVPASSSRQRPRSRAPAFPPASPSAASRRPSSLRISP 438
Cdd:PRK10263   421 YAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEP 494
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 288-434 1.42e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 42.16  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  288 GLSPSFASPSHTAPAASPHSSAPQGAVASQSLSPQSAATHPLSPHSVAPQAAVPSPslSSHSTASVIATGSQPSSPRyrp 367
Cdd:PHA02682    78 GQSPLAPSPACAAPAPACPACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAP--ARPAPACPPSTRQCPPAPP--- 152

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  368 ytvthLWGSSPCPTPRSSILAN---PPGFPAhSSSPRAVPAsssrqrprsrapafPPASPSAASRRPSSL 434
Cdd:PHA02682   153 -----LPTPKPAPAAKPIFLHNqlpPPDYPA-ASCPTIETA--------------PAASPVLEPRIPDKI 202
PHA03247 PHA03247
large tegument protein UL36; Provisional
 223-448 1.80e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  223 ASLTATSQPIATAARSPDRNLMLNTGSS-SGTSPMFCSLGSFSASSLSSLYETSPAPSTSLwsfVPGLSPSFASPSHTA- 300
Cdd:PHA03247  2796 ESLPSPWDPADPPAAVLAPAAALPPAASpAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSV---APGGDVRRRPPSRSPa 2872

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  301 --PAASPHSSAPQGAVASQSLSPQSAATHPLSPHSVAPQAAVPSPSLSSHSTASVIATGSQPSSPRYRPytvthlwgsSP 378
Cdd:PHA03247  2873 akPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQP---------PL 2943

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  379 CPTPRSSILANPPGFPAHSSSPRAVPASSSRQRPRSRAPAfpPASPSAASrRPSSLRISPSLGASGGAST 448
Cdd:PHA03247  2944 APTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPA--PSREAPAS-STPPLTGHSLSRVSSWASS 3010
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 291-531 2.52e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.22  E-value: 2.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  291 PSFASPSHTAPAASPHSSAPQGAVASQS----LSPQSAATHPLSPHSV-----APQAAVPSPSLSSHSTASVIATGSQPS 361
Cdd:PLN03209   329 PPKESDAADGPKPVPTKPVTPEAPSPPIeeepPQPKAVVPRPLSPYTAyedlkPPTSPIPTPPSSSPASSKSVDAVAKPA 408

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  362 SPRyrpytvthlwgSSPCPTPRSSILANPPGfPAHSSSPRavPASSSRQRPRSRAPAFPpaSPSAASRRPSSLRISPSLG 441
Cdd:PLN03209   409 EPD-----------VVPSPGSASNVPEVEPA-QVEAKKTR--PLSPYARYEDLKPPTSP--SPTAPTGVSPSVSSTSSVP 472

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  442 ASGGASTWDSYSDHFTIETCKETDMLNYLIECFDRVGIEEKKAPKMCSQPAVSQLLSNIRSQCISHTALVLQGSLTQPrs 521
Cdd:PLN03209   473 AVPDTAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQP-- 550

                          250
                   ....*....|
gi 1046888122  522 lqQPSFLVPY 531
Cdd:PLN03209   551 --KPRPLSPY 558
PHA03247 PHA03247
large tegument protein UL36; Provisional
 286-447 3.38e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 3.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  286 VPGLSPSfASPSHTAPAASPHSSAPQGAVASQSLSPqSAATHPLSPHS-VAPQAAVPSPSLSSHSTASVIATGSQPSSPR 364
Cdd:PHA03247  2555 LPPAAPP-AAPDRSVPPPRPAPRPSEPAVTSRARRP-DAPPQSARPRApVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPS 2632

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  365 YRPYTVTHLWGSSPCPTPRSSILANPP-----------GFPAHSSSP------RAVPASSSRQRPRSRAPAfPPASPSAA 427
Cdd:PHA03247  2633 PAANEPDPHPPPTVPPPERPRDDPAPGrvsrprrarrlGRAAQASSPpqrprrRAARPTVGSLTSLADPPP-PPPTPEPA 2711

                          170       180
                   ....*....|....*....|
gi 1046888122  428 SRRPSSLRISPSLGASGGAS 447
Cdd:PHA03247  2712 PHALVSATPLPPGPAAARQA 2731
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 285-447 5.03e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 5.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  285 FVPGLSPSFASPSHTAPAASPHSSAPQGAVASQSlspqsaaTHPLSPHSVAPQAAVPSPSLSSHSTASVIATGSQPSSP- 363
Cdd:PHA03307    55 VVAGAAACDRFEPPTGPPPGPGTEAPANESRSTP-------TWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPp 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  364 ----------RYRPYTVTHLW-GSSPCPTPRSSILANPPGFPAHSSSPRAVPASSSRQRPRSRAPAFPPASPSAASRRPS 432
Cdd:PHA03307   128 pspapdlsemLRPVGSPGPPPaASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPP 207

                          170
                   ....*....|....*
gi 1046888122  433 SLRISPSLGASGGAS 447
Cdd:PHA03307   208 RRSSPISASASSPAP 222
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
273-428 6.69e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.99  E-value: 6.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  273 ETSPAPSTSLWSFVPGLSPSFASPshtaPAASPHSSAPQGAVASQSLSPQSAATHPLSPHSVAPQAAVPSPSLSSHSTAS 352
Cdd:PRK07003   471 PADSGSASAPASDAPPDAAFEPAP----RAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARA 546

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  353 VIAT---------GSQPSSPRYRPYTVTHLWGSSPCPTPRSSilanPPGFPAHSSSPRAvPASSSRQRPRSRAPAFPPAS 423
Cdd:PRK07003   547 GGAAaaldvlrnaGMRVSSDRGARAAAAAKPAAAPAAAPKPA----APRVAVQVPTPRA-RAATGDAPPNGAARAEQAAE 621


                   ....*
gi 1046888122  424 PSAAS 428
Cdd:PRK07003   622 SRGAP 626
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 287-372 8.46e-03

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 40.24  E-value: 8.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888122  287 PGLSPSfASPSHTAPAASPHSSAPQGAVAS------QSLSPQSAAT----HPLSPHSVAPQAAVPSPSLSSHSTASVIAT 356
Cdd:cd23959    156 FGQHPP-PAKPLPAAAAAQQSSASPGEVASpfasgtVSASPFATATdtapSSGAPDGFPAEASAPSPFAAPASAASFPAA 234

                           90
                   ....*....|....*.
gi 1046888122  357 GSQPSspryRPYTVTH 372
Cdd:cd23959    235 PVANG----EAATPTH 246
 
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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