NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1622941541|ref|XP_028704617|]
View 

OTU domain-containing protein 4 isoform X7 [Macaca mulatta]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Tudor_SF super family cl02573
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
 163-222 1.11e-29

Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.


The actual alignment was detected with superfamily member cd20448:

Pssm-ID: 470623  Cd Length: 64  Bit Score: 112.28  E-value: 1.11e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622941541  163 DYSIAAGLQYEVGDKCQVRLDHNGKFLNADVQGVHSENGPVLV--EELGKKHTS--KNLKAPPP 222
Cdd:cd20448      1 DFSIAAGMQYSVGDKCKVRLDHNGKFYNAHIQEVSPENGPVVVfvEELGKKHTVplKNLKPPPQ 64
OTU super family cl45892
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
 1-43 6.03e-24

OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation.


The actual alignment was detected with superfamily member cd22794:

Pssm-ID: 459237 [Multi-domain]  Cd Length: 130  Bit Score: 98.21  E-value: 6.03e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622941541    1 MYRKDFIIYREPNVSPSQVTENNFPEKVLLCFSNGNHYDIVYP 43
Cdd:cd22794     88 MYKRDFIIYQEPGKPPSNVTENGFPDKILLCFSNGNHYDSVYP 130
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 431-774 4.93e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 4.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  431 TVSSPSKSKKLECPSPAEQKPAEHVSLSNPAPLLVSPEVHLTPavPSLPATVPAWPS--EPTTFGPTGVPAPIPILSVTq 508
Cdd:PHA03247  2643 PPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRR--RAARPTVGSLTSlaDPPPPPPTPEPAPHALVSAT- 2719

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  509 TLTTGPDSAVSQAHLTPSpVPVSIQAVNQPLMPL-------PQTLSLYQDPLYPGFPCNEKGDRAIVPPY-SLCQTGEDL 580
Cdd:PHA03247  2720 PLPPGPAAARQASPALPA-APAPPAVPAGPATPGgparparPPTTAGPPAPAPPAAPAAGPPRRLTRPAVaSLSESRESL 2798

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  581 PKDKNILRFFFNLGVKAYSCPMWAPHSYLYPLHQAYLAACRMYPKVPVP--------VYPHNPWFQEAPAAQNESDCAcT 652
Cdd:PHA03247  2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPpslplggsVAPGGDVRRRPPSRSPAAKPA-A 2877

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  653 DAHFPMQteasvngQMPQPEIGPPTFSSPLviPPSQVSESHGQLSYQADLESETPGQLLHADYEESLSGKnmfPQPSFGP 732
Cdd:PHA03247  2878 PARPPVR-------RLARPAVSRSTESFAL--PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR---PQPPLAP 2945

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1622941541  733 NPFLGPVPIAPPFFPHVWYGYPFQGFIENPVMRQNIVLPSDE 774
Cdd:PHA03247  2946 TTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSRE 2987
 
Name Accession Description Interval E-value
Tudor_OTUD4 cd20448
Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called ...
 163-222 1.11e-29

Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called HIV-1-induced protein HIN-1, is a phospho-activated K63 deubiquitinase that hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein. It may negatively regulate inflammatory and pathogen recognition signaling in innate immune response. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410519  Cd Length: 64  Bit Score: 112.28  E-value: 1.11e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622941541  163 DYSIAAGLQYEVGDKCQVRLDHNGKFLNADVQGVHSENGPVLV--EELGKKHTS--KNLKAPPP 222
Cdd:cd20448      1 DFSIAAGMQYSVGDKCKVRLDHNGKFYNAHIQEVSPENGPVVVfvEELGKKHTVplKNLKPPPQ 64
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
 1-43 6.03e-24

OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU domain-containing protein 4 (OTUD4), also called HIV-1-induced protein HIN-1, is a deubiquitinase that specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein upon phosphorylation, triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators. OTUD4 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438615 [Multi-domain]  Cd Length: 130  Bit Score: 98.21  E-value: 6.03e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622941541    1 MYRKDFIIYREPNVSPSQVTENNFPEKVLLCFSNGNHYDIVYP 43
Cdd:cd22794     88 MYKRDFIIYQEPGKPPSNVTENGFPDKILLCFSNGNHYDSVYP 130
PHA03247 PHA03247
large tegument protein UL36; Provisional
 431-774 4.93e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 4.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  431 TVSSPSKSKKLECPSPAEQKPAEHVSLSNPAPLLVSPEVHLTPavPSLPATVPAWPS--EPTTFGPTGVPAPIPILSVTq 508
Cdd:PHA03247  2643 PPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRR--RAARPTVGSLTSlaDPPPPPPTPEPAPHALVSAT- 2719

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  509 TLTTGPDSAVSQAHLTPSpVPVSIQAVNQPLMPL-------PQTLSLYQDPLYPGFPCNEKGDRAIVPPY-SLCQTGEDL 580
Cdd:PHA03247  2720 PLPPGPAAARQASPALPA-APAPPAVPAGPATPGgparparPPTTAGPPAPAPPAAPAAGPPRRLTRPAVaSLSESRESL 2798

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  581 PKDKNILRFFFNLGVKAYSCPMWAPHSYLYPLHQAYLAACRMYPKVPVP--------VYPHNPWFQEAPAAQNESDCAcT 652
Cdd:PHA03247  2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPpslplggsVAPGGDVRRRPPSRSPAAKPA-A 2877

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  653 DAHFPMQteasvngQMPQPEIGPPTFSSPLviPPSQVSESHGQLSYQADLESETPGQLLHADYEESLSGKnmfPQPSFGP 732
Cdd:PHA03247  2878 PARPPVR-------RLARPAVSRSTESFAL--PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR---PQPPLAP 2945

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1622941541  733 NPFLGPVPIAPPFFPHVWYGYPFQGFIENPVMRQNIVLPSDE 774
Cdd:PHA03247  2946 TTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSRE 2987
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 416-531 4.74e-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: 4.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  416 PEPSTLENITDDKYATVSSPSKSKKLECPSPAEQKPAehvsLSNPAPLLVSPEVHLTPavPSLPATVPAwpsePTTFGPT 495
Cdd:pfam05109  490 PSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPA----VTTPTPNATSPTLGKTS--PTSAVTTPT----PNATSPT 559

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1622941541  496 -GVPAPIPILSVTQTLTTGPDSAVSqahlTPSPVPVS 531
Cdd:pfam05109  560 pAVTTPTPNATIPTLGKTSPTSAVT----TPTPNATS 592
 
Name Accession Description Interval E-value
Tudor_OTUD4 cd20448
Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called ...
 163-222 1.11e-29

Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called HIV-1-induced protein HIN-1, is a phospho-activated K63 deubiquitinase that hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein. It may negatively regulate inflammatory and pathogen recognition signaling in innate immune response. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410519  Cd Length: 64  Bit Score: 112.28  E-value: 1.11e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622941541  163 DYSIAAGLQYEVGDKCQVRLDHNGKFLNADVQGVHSENGPVLV--EELGKKHTS--KNLKAPPP 222
Cdd:cd20448      1 DFSIAAGMQYSVGDKCKVRLDHNGKFYNAHIQEVSPENGPVVVfvEELGKKHTVplKNLKPPPQ 64
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
 1-43 6.03e-24

OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU domain-containing protein 4 (OTUD4), also called HIV-1-induced protein HIN-1, is a deubiquitinase that specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein upon phosphorylation, triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators. OTUD4 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438615 [Multi-domain]  Cd Length: 130  Bit Score: 98.21  E-value: 6.03e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622941541    1 MYRKDFIIYREPNVSPSQVTENNFPEKVLLCFSNGNHYDIVYP 43
Cdd:cd22794     88 MYKRDFIIYQEPGKPPSNVTENGFPDKILLCFSNGNHYDSVYP 130
OTU_ALG13-like cd22753
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 1-43 1.75e-16

OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 and similar proteins; Bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 is alco called asparagine-linked glycosylation 13 homolog, glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13 homolog. It displays both glycosyltransferase (EC 2.4.1.141) and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. With ALG14, it forms a UDP-N-acetylglucosamine transferase that catalyzes the second step of eukaryotic N-linked glycosylation in the endoplasmic reticulum. ALG13 variants cause a form of early infantile epileptic encephalopathy known as EIEE36 refractory seizures, neurodevelopmental impairment, and poor prognosis; given the essential role of ALG13 in glycosylation, it is also considered a congenital disorder of glycosylation (CDG). This subfamily also contains OTU domain-containing protein 4 (OTUD4), also called HIV-1-induced protein HIN-1, a DUB that specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein upon phosphorylation, triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438590 [Multi-domain]  Cd Length: 130  Bit Score: 76.81  E-value: 1.75e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622941541    1 MYRKDFIIYREPNVSPSQVTENNFPEKVLLCFSNGNHYDIVYP 43
Cdd:cd22753     88 LYKVDFIVYSIPDQPPSNITNNGYPKKIMLCYSGGNHYDSVYS 130
Tudor_TDRD13-like cd20380
Tudor domain found in Tudor domain-containing protein 13 (TDRD13) and similar proteins; The ...
 171-218 7.21e-15

Tudor domain found in Tudor domain-containing protein 13 (TDRD13) and similar proteins; The TDRD13 family includes TDRD13 and OTU domain-containing protein 4 (OTUD4). TDRD13, also called asparagine-linked glycosylation 13 (ALG13), glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13, is a putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase (EC 2.4.1.141/EC 3.4.19.12). It is a potential member of the Alg7p/Alg13p/Alg14p complex catalyzing the first two initial reactions in the N-glycosylation process. OTUD4, also called HIV-1-induced protein HIN-1, is a phospho-activated K63 deubiquitinase that hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein. It may negatively regulate inflammatory and pathogen recognition signaling in innate immune response. Members of this family contain one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410451  Cd Length: 54  Bit Score: 69.53  E-value: 7.21e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622941541  171 QYEVGDKCQVRLDHNGKFLNADVQGVHSENGPVLV--EELGKKHT--SKNLK 218
Cdd:cd20380      1 QFKPGDKCQVELDSPGKVYEAHIQEISPDKGPVTVfvEELGEKKTvpYENLK 52
OTU_ALG13 cd22795
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 1-43 2.01e-13

OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13; Bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 is also called asparagine-linked glycosylation 13 homolog, glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13 homolog. It displays both glycosyltransferase (EC 2.4.1.141) and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. With ALG14, it forms a UDP-N-acetylglucosamine transferase that catalyzes the second step of eukaryotic N-linked glycosylation in the endoplasmic reticulum. ALG13 variants cause a form of early infantile epileptic encephalopathy known as EIEE36 refractory seizures, neurodevelopmental impairment, and poor prognosis; given the essential role of ALG13 in glycosylation, it is also considered a congenital disorder of glycosylation (CDG). ALG13 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438616 [Multi-domain]  Cd Length: 130  Bit Score: 67.91  E-value: 2.01e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622941541    1 MYRKDFIIYREPNVSPSQVTENNFPEKVLLCFSNGNHYDIVYP 43
Cdd:cd22795     88 IYNRDFILYRYPGKPPTYATDNGFEDKILLCCSSNGHYDSVYT 130
Tudor_TDRD13 cd20447
Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called ...
 168-232 4.57e-12

Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called asparagine-linked glycosylation 13 (ALG13), glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13, is a putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase (EC 2.4.1.141/EC 3.4.19.12). It is a potential member of the Alg7p/Alg13p/Alg14p complex catalyzing the first two initial reactions in the N-glycosylation process. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410518  Cd Length: 80  Bit Score: 62.56  E-value: 4.57e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622941541  168 AGLQYEVGDKCQVRLDHNGKFLNADVQ--GVHSENGPVLVEELGKKHTSK--NLK----APPPESWNTVSGKK 232
Cdd:cd20447      2 AGRQYYLGDKCQVRLEPGGKYYNAHIQevGQDSNSVTVFIEELAEKHTVPlaNLKpvtqVTPVPAWNMMPNRK 74
PHA03247 PHA03247
large tegument protein UL36; Provisional
 431-774 4.93e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 4.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  431 TVSSPSKSKKLECPSPAEQKPAEHVSLSNPAPLLVSPEVHLTPavPSLPATVPAWPS--EPTTFGPTGVPAPIPILSVTq 508
Cdd:PHA03247  2643 PPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRR--RAARPTVGSLTSlaDPPPPPPTPEPAPHALVSAT- 2719

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  509 TLTTGPDSAVSQAHLTPSpVPVSIQAVNQPLMPL-------PQTLSLYQDPLYPGFPCNEKGDRAIVPPY-SLCQTGEDL 580
Cdd:PHA03247  2720 PLPPGPAAARQASPALPA-APAPPAVPAGPATPGgparparPPTTAGPPAPAPPAAPAAGPPRRLTRPAVaSLSESRESL 2798

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  581 PKDKNILRFFFNLGVKAYSCPMWAPHSYLYPLHQAYLAACRMYPKVPVP--------VYPHNPWFQEAPAAQNESDCAcT 652
Cdd:PHA03247  2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPpslplggsVAPGGDVRRRPPSRSPAAKPA-A 2877

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  653 DAHFPMQteasvngQMPQPEIGPPTFSSPLviPPSQVSESHGQLSYQADLESETPGQLLHADYEESLSGKnmfPQPSFGP 732
Cdd:PHA03247  2878 PARPPVR-------RLARPAVSRSTESFAL--PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR---PQPPLAP 2945

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1622941541  733 NPFLGPVPIAPPFFPHVWYGYPFQGFIENPVMRQNIVLPSDE 774
Cdd:PHA03247  2946 TTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSRE 2987
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 416-531 4.74e-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: 4.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  416 PEPSTLENITDDKYATVSSPSKSKKLECPSPAEQKPAehvsLSNPAPLLVSPEVHLTPavPSLPATVPAwpsePTTFGPT 495
Cdd:pfam05109  490 PSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPA----VTTPTPNATSPTLGKTS--PTSAVTTPT----PNATSPT 559

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1622941541  496 -GVPAPIPILSVTQTLTTGPDSAVSqahlTPSPVPVS 531
Cdd:pfam05109  560 pAVTTPTPNATIPTLGKTSPTSAVT----TPTPNATS 592
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 393-747 6.11e-04

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: 43.99  E-value: 6.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  393 RRMDTEERKDKDSIHGHSQLDKKPEPSTLENITDDkyatvSSPSKSKKLECPSPAEQkpAEHVSLSNPAPLLVSPEVHLT 472
Cdd:pfam03154  124 RSVNDEGSSDPKDIDQDNRSTSPSIPSPQDNESDS-----DSSAQQQILQTQPPVLQ--AQSGAASPPSPPPPGTTQAAT 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  473 PAVPSLPATVPAWPSEPTTFGPTGVPAPIPILSVTQTLTT-------GPDSAVSQAHLTPSPVPVSIQAVNQPLM----- 540
Cdd:pfam03154  197 AGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTlhpqrlpSPHPPLQPMTQPPPPSQVSPQPLPQPSLhgqmp 276

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  541 PLPQTL----SLYQDPLYP-GFPCNEKGDRAIVPPYSLCQ------------------TGEDLPKDKNILRFFFNL-GVK 596
Cdd:pfam03154  277 PMPHSLqtgpSHMQHPVPPqPFPLTPQSSQSQVPPGPSPAapgqsqqrihtppsqsqlQSQQPPREQPLPPAPLSMpHIK 356

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  597 AYSC----PMWAPHSYLYPLHQAYLAACRMYPKVPVPvyphnpwfqeaPAAQNESDCAC---TDAHFPMQTEASVNGQMP 669
Cdd:pfam03154  357 PPPTtpipQLPNPQSHKHPPHLSGPSPFQMNSNLPPP-----------PALKPLSSLSThhpPSAHPPPLQLMPQSQQLP 425

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622941541  670 QPEIGPPTFSSPLVIPPSqvSESHGQLSYQADLESETPgqllhadyeeslsgknmFPQPSFGPNpflGPVPIAPPFFP 747
Cdd:pfam03154  426 PPPAQPPVLTQSQSLPPP--AASHPPTSGLHQVPSQSP-----------------FPQHPFVPG---GPPPITPPSGP 481
PHA03247 PHA03247
large tegument protein UL36; Provisional
 418-521 7.92e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 7.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622941541  418 PSTLENITD-DKYATVSSPSKSKKLECPSPAEQKPAEHVSLSNPAPLLVSPEVHLTPAVPSLPATVPAWPSEPTTF---- 492
Cdd:PHA03247   362 PSSLEDLSAgRHHPKRASLPTRKRRSARHAATPFARGPGGDDQTRPAAPVPASVPTPAPTPVPASAPPPPATPLPSaepg 441

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622941541  493 ---GPTGVPAPIPILSVTQTLTTGPDSAVSQA 521
Cdd:PHA03247   442 sddGPAPPPERQPPAPATEPAPDDPDDATRKA 473
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH