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Conserved domains on  [gi|1835597353|ref|XP_033801972|]
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putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 [Geotrypetes seraphini]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OTU_ALG13 cd22795
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 308-436 7.37e-87

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: 276.69  E-value: 7.37e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  308 MDEYLGSLGLYRKLTAKDASCLFRAVSEQLFHCQIHHMKIRKICVAYMRDNQQNFESYVEGPFEKYLERLEDPKESAGQL 387
Cdd:cd22795      1 MDEYLGSLGLYRKLTAKDASCLFRAVSEQLFLCQIHHLEIRKACVSYMRANQCNFESYVEGSFEKYLERLEDPKESAGQL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1835597353  388 EINALSLIYNRDIILYRYPGKPPTYVTDHGFEEKIMLCCSTNGHYDSVF 436
Cdd:cd22795     81 EISALSLIYNRDFILYRYPGKPPTYATDNGFEDKILLCCSSNGHYDSVY 129
Tudor_TDRD13 cd20447
Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called ...
 578-657 2.16e-51

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: 175.04  E-value: 2.16e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  578 FAGRQYCLGDKCQVRLETGGKYYNSHIQEVGHDSNSVTVFIEELAEKHIVPLVNLKPVTQVTPVPAWNVSPIRKGGGYQK 657
Cdd:cd20447      1 FAGRQYYLGDKCQVRLEPGGKYYNAHIQEVGQDSNSVTVFIEELAEKHTVPLANLKPVTQVTPVPAWNMMPNRKGGNYQK 80
PssE super family cl49515
PssE/Cps14G family polysaccharide biosynthesis glycosyltransferase;
5-146 8.09e-31

PssE/Cps14G family polysaccharide biosynthesis glycosyltransferase;


The actual alignment was detected with superfamily member NF041548:

Pssm-ID: 469433 [Multi-domain]  Cd Length: 146  Bit Score: 118.78  E-value: 8.09e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353    5 VFVTVGTTSFDELVARVSEEASVQIlrslgYNKLILQIGRGSVEPKPCSSaaftmevFRYKESLRDDIKWADLVISHAGA 84
Cdd:NF041548     1 IFVTVGTTRFDSLIKAIDELIEGLI-----DYEVTFQIGDGKYIPKNGEY-------FDFLEEIDEYYKKADLIITHAGA 68

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835597353   85 GSCLETLGEGKPLIVVINEKLMGNHQLELAKQLHSDGHLLYCT-CSTLMETLQSMDPSALKPF 146
Cdd:NF041548    69 GTIYSLLELGKKVIVVPNLERVDDHQLDLAEYVEENGYALVCYdLDELEDAIKEAENFKPNPY 131
DUF5585 super family cl39316
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 807-1014 5.47e-06

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


The actual alignment was detected with superfamily member pfam17823:

Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 50.34  E-value: 5.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  807 NGEEPRGLEETITFYEIEEGDETAFPAINSQGSSSPIVPTT--AGFWVTRRGPTSITSgkqTMTSSEEEVDEPSDGG--- 881
Cdd:pfam17823   31 NKMWNGAGKQNASGDAVPRADNKSSEQ*NFCAATAAPAPVTltKGTSAAHLNSTEVTA---EHTPHGTDLSEPATREgaa 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  882 DFHGDYIYTASDSGFETPVLYGTTESTANLSLQDDGPPSGPSPEGSVSYSYSQQVSAAV-----ISTSTCASTAPTPLIT 956
Cdd:pfam17823  108 DGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASaphaaSPAPRTAASSTTAASS 187

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835597353  957 SNSATLAPVTSAVPAQ---TAVHPIIMSPAAVGRPGLPSVPFPFYSPPPTPATETVDPGNV 1014
Cdd:pfam17823  188 TTAASSAPTTAASSAPatlTPARGISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTV 248
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 905-1199 5.10e-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.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.84  E-value: 5.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  905 TESTANLSLQDDGPPSGPSPEGSVSysysqQVSAAVISTSTCASTAPTPLITSNSATLAPVTSAVPAQT----AVHPIIM 980
Cdd:pfam03154  158 SDSSAQQQILQTQPPVLQAQSGAAS-----PPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTqstaAPHTLIQ 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  981 SPAAVGRPGLPS-----VPFPFYSPPP-TPATETVDPGNVPPPPPPPPPYSCDPSGSDLPRDTKVLQYYFNLGlQCyhqs 1054
Cdd:pfam03154  233 QTPTLHPQRLPSphpplQPMTQPPPPSqVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSS-QS---- 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353 1055 ywhsmvymQHVPQPTPVEPYPVFSDPVPIIDQTVPQMYNdgriDGRHVPLEPANGAFPNVEassvPHGTVYYPVMADPYS 1134
Cdd:pfam03154  308 --------QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQ----PPREQPLPPAPLSMPHIK----PPPTTPIPQLPNPQS 371

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835597353 1135 Q-------PPLP-GYESCVPIVPTYHYVSSWHPANPSYGSSPRIHNTVNSGQLHQvsyvAAASPPTHFVSQSI 1199
Cdd:pfam03154  372 HkhpphlsGPSPfQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPP----PPAQPPVLTQSQSL 440
 
Name Accession Description Interval E-value
OTU_ALG13 cd22795
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 308-436 7.37e-87

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: 276.69  E-value: 7.37e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  308 MDEYLGSLGLYRKLTAKDASCLFRAVSEQLFHCQIHHMKIRKICVAYMRDNQQNFESYVEGPFEKYLERLEDPKESAGQL 387
Cdd:cd22795      1 MDEYLGSLGLYRKLTAKDASCLFRAVSEQLFLCQIHHLEIRKACVSYMRANQCNFESYVEGSFEKYLERLEDPKESAGQL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1835597353  388 EINALSLIYNRDIILYRYPGKPPTYVTDHGFEEKIMLCCSTNGHYDSVF 436
Cdd:cd22795     81 EISALSLIYNRDFILYRYPGKPPTYATDNGFEDKILLCCSSNGHYDSVY 129
Tudor_TDRD13 cd20447
Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called ...
 578-657 2.16e-51

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: 175.04  E-value: 2.16e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  578 FAGRQYCLGDKCQVRLETGGKYYNSHIQEVGHDSNSVTVFIEELAEKHIVPLVNLKPVTQVTPVPAWNVSPIRKGGGYQK 657
Cdd:cd20447      1 FAGRQYYLGDKCQVRLEPGGKYYNAHIQEVGQDSNSVTVFIEELAEKHTVPLANLKPVTQVTPVPAWNMMPNRKGGNYQK 80
PssE NF041548
PssE/Cps14G family polysaccharide biosynthesis glycosyltransferase;
5-146 8.09e-31

PssE/Cps14G family polysaccharide biosynthesis glycosyltransferase;


Pssm-ID: 469433 [Multi-domain]  Cd Length: 146  Bit Score: 118.78  E-value: 8.09e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353    5 VFVTVGTTSFDELVARVSEEASVQIlrslgYNKLILQIGRGSVEPKPCSSaaftmevFRYKESLRDDIKWADLVISHAGA 84
Cdd:NF041548     1 IFVTVGTTRFDSLIKAIDELIEGLI-----DYEVTFQIGDGKYIPKNGEY-------FDFLEEIDEYYKKADLIITHAGA 68

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835597353   85 GSCLETLGEGKPLIVVINEKLMGNHQLELAKQLHSDGHLLYCT-CSTLMETLQSMDPSALKPF 146
Cdd:NF041548    69 GTIYSLLELGKKVIVVPNLERVDDHQLDLAEYVEENGYALVCYdLDELEDAIKEAENFKPNPY 131
Glyco_tran_28_C pfam04101
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ...
 5-147 5.32e-29

Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). Structural analysis suggests the C-terminal domain contains the UDP-GlcNAc binding site.


Pssm-ID: 427711 [Multi-domain]  Cd Length: 166  Bit Score: 113.96  E-value: 5.32e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353    5 VFVTVGTTSFDELVARVSEEASVQILRslGYNKLILQIGRGSVEPKPCSSAAFT--MEVFRYKESLRDDIKWADLVISHA 82
Cdd:pfam04101    2 ILVTGGSQGARALNELVLSVLPLLELK--GELQVLHQTGKGDLEEVKIDYAELGinYEVFPFIDNMAEYIKAADLVISRA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353   83 GAGSCLETLGEGKPLIVVINEK----LMGNHQLELAKQLHSDGHLLYC-TCSTLMETLQSMDPSALKPFP 147
Cdd:pfam04101   80 GAGTIAELLALGKPAILVPNPSaargHQDNNAKELVKAGAALVILQKElTPEKLIEALLKLLLNPLRLAE 149
COG5017 COG5017
UDP-N-acetylglucosamine transferase subunit ALG13 [Carbohydrate transport and metabolism];
5-163 1.32e-15

UDP-N-acetylglucosamine transferase subunit ALG13 [Carbohydrate transport and metabolism];


Pssm-ID: 444041 [Multi-domain]  Cd Length: 164  Bit Score: 75.73  E-value: 1.32e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353    5 VFVTVGTT--SFDELVARVSEEASvQILRSLgynKLILQIGRGSVEPKPCSSAAFtMEvfryKESLRDDIKWADLVISHA 82
Cdd:COG5017      2 IFVTVGTHqlPFDRLVRWVDELAA-EGIIDE---EVFVQTGHTTYVPRNAEAVPF-LP----PDEFQKLIAQARLVISHA 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353   83 GAGSCLETLGEGKPLIVV---------INeklmgNHQLELAKQLHSDGHLLYCTCSTLMETL--QSMDPSALKPFPIGRP 151
Cdd:COG5017     73 GMGSILTALKLGKPFILVprlarygehVD-----DHQLETARALEKLGGIIVVEDPADLEAAldEALALKSPEPFSVPSP 147

                          170
                   ....*....|....
gi 1835597353  152 --EIFAAFLDKAVG 163
Cdd:COG5017    148 arGALVDFLRAFIT 161
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 325-432 1.63e-15

OTU-like cysteine protease; This family is comprised of a group of predicted cysteine proteases, homologous to the Ovarian Tumour (OTU) gene in Drosophila. Members include proteins from eukaryotes, viruses and pathogenic bacterium. The conserved cysteine and histidine, and possibly the aspartate, represent the catalytic residues in this putative group of proteases.


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 74.02  E-value: 1.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  325 DASCLFRAVSEQLF-----HCQIHHMKIRKICVAYMRDNQQNFESYVEGPFEKYLERLEDPKESAGQLEINALSLIYNRD 399
Cdd:pfam02338    3 DGNCLYRSISHQLWgvhdvLRKMLVQELRETLAEYMREHKEEFEPFLEDDETGDIIEIEQTGAWGGEIEIFALAHILRRP 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1835597353  400 IILYRYPGKPPT-------YVTDHGFEEKIMLC-----CSTNGHY 432
Cdd:pfam02338   83 IIVYKSEGGEELgglkeygIYLPLGWDPSLCLVyprhlYYLGGHY 127
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 807-1014 5.47e-06

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: 50.34  E-value: 5.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  807 NGEEPRGLEETITFYEIEEGDETAFPAINSQGSSSPIVPTT--AGFWVTRRGPTSITSgkqTMTSSEEEVDEPSDGG--- 881
Cdd:pfam17823   31 NKMWNGAGKQNASGDAVPRADNKSSEQ*NFCAATAAPAPVTltKGTSAAHLNSTEVTA---EHTPHGTDLSEPATREgaa 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  882 DFHGDYIYTASDSGFETPVLYGTTESTANLSLQDDGPPSGPSPEGSVSYSYSQQVSAAV-----ISTSTCASTAPTPLIT 956
Cdd:pfam17823  108 DGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASaphaaSPAPRTAASSTTAASS 187

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835597353  957 SNSATLAPVTSAVPAQ---TAVHPIIMSPAAVGRPGLPSVPFPFYSPPPTPATETVDPGNV 1014
Cdd:pfam17823  188 TTAASSAPTTAASSAPatlTPARGISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTV 248
GT28_MurG cd03785
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ...
 10-121 3.14e-05

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340818 [Multi-domain]  Cd Length: 350  Bit Score: 47.60  E-value: 3.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353   10 GTTSFDELVARVSEEasvqiLRSLGYNkLILQIGRGSVEP--KPCSSAAFTMEVFRYKESLRDDIKWADLVISHAGAGSC 87
Cdd:cd03785    192 GARAINRAVPKALPK-----LLERGIQ-VIHQTGKGDYDEvkKLYEDLGINVKVFPFIDDMAAAYAAADLVISRAGASTI 265

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1835597353   88 LETLGEGKPLIVVINEKLMGNHQLELAKQLHSDG 121
Cdd:cd03785    266 AELTAAGKPAILIPYPYAADDHQEANARALEKAG 299
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 905-1199 5.10e-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: 47.84  E-value: 5.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  905 TESTANLSLQDDGPPSGPSPEGSVSysysqQVSAAVISTSTCASTAPTPLITSNSATLAPVTSAVPAQT----AVHPIIM 980
Cdd:pfam03154  158 SDSSAQQQILQTQPPVLQAQSGAAS-----PPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTqstaAPHTLIQ 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  981 SPAAVGRPGLPS-----VPFPFYSPPP-TPATETVDPGNVPPPPPPPPPYSCDPSGSDLPRDTKVLQYYFNLGlQCyhqs 1054
Cdd:pfam03154  233 QTPTLHPQRLPSphpplQPMTQPPPPSqVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSS-QS---- 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353 1055 ywhsmvymQHVPQPTPVEPYPVFSDPVPIIDQTVPQMYNdgriDGRHVPLEPANGAFPNVEassvPHGTVYYPVMADPYS 1134
Cdd:pfam03154  308 --------QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQ----PPREQPLPPAPLSMPHIK----PPPTTPIPQLPNPQS 371

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835597353 1135 Q-------PPLP-GYESCVPIVPTYHYVSSWHPANPSYGSSPRIHNTVNSGQLHQvsyvAAASPPTHFVSQSI 1199
Cdd:pfam03154  372 HkhpphlsGPSPfQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPP----PPAQPPVLTQSQSL 440
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
 888-1001 3.66e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 44.70  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  888 IYTASDSGFETPvlyGTTESTANLSLQDDGPPSGPSPEGSVSYSYSQQVSAAVISTSTCASTAPTPLITSN-------SA 960
Cdd:PRK08691   407 VQTASAAAMPSE---GKTAGPVSNQENNDVPPWEDAPDEAQTAAGTAQTSAKSIQTASEAETPPENQVSKNkaadnetDA 483

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1835597353  961 TLAPVTSAVPAQTAVHPIIMSPAAVGRPGlPSVPFPFYSPP 1001
Cdd:PRK08691   484 PLSEVPSENPIQATPNDEAVETETFAHEA-PAEPFYGYGFP 523
PHA03247 PHA03247
large tegument protein UL36; Provisional
 917-1157 3.68e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 3.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  917 GPPSGPSPEGSVSYSYSQQVSAAVISTSTCASTAPTPlitsnsATLAPVTSAVPAQTAVHPIIMSPAavgrPGLPSVPFP 996
Cdd:PHA03247  2765 GPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSP------WDPADPPAAVLAPAAALPPAASPA----GPLPPPTSA 2834

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  997 FYSPPPTPatetvdPGNVPPPPPP---------------PPPYSCDPSGSDLPRDTKVLQyyfnLGLQCYHQSYWHSMVY 1061
Cdd:PHA03247  2835 QPTAPPPP------PGPPPPSLPLggsvapggdvrrrppSRSPAAKPAAPARPPVRRLAR----PAVSRSTESFALPPDQ 2904

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353 1062 MQHVPQPTPVEPyPVFSDPVPIIDQTVPQMYNDGRIDGrhvPLEP---------ANGAFPNVEASSVPHGTVYYPVMADP 1132
Cdd:PHA03247  2905 PERPPQPQAPPP-PQPQPQPPPPPQPQPPPPPPPRPQP---PLAPttdpagagePSGAVPQPWLGALVPGRVAVPRFRVP 2980

                          250       260
                   ....*....|....*....|....*...
gi 1835597353 1133 YSQPPLPGYESCVPiVPTYHY---VSSW 1157
Cdd:PHA03247  2981 QPAPSREAPASSTP-PLTGHSlsrVSSW 3007
 
Name Accession Description Interval E-value
OTU_ALG13 cd22795
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 308-436 7.37e-87

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: 276.69  E-value: 7.37e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  308 MDEYLGSLGLYRKLTAKDASCLFRAVSEQLFHCQIHHMKIRKICVAYMRDNQQNFESYVEGPFEKYLERLEDPKESAGQL 387
Cdd:cd22795      1 MDEYLGSLGLYRKLTAKDASCLFRAVSEQLFLCQIHHLEIRKACVSYMRANQCNFESYVEGSFEKYLERLEDPKESAGQL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1835597353  388 EINALSLIYNRDIILYRYPGKPPTYVTDHGFEEKIMLCCSTNGHYDSVF 436
Cdd:cd22795     81 EISALSLIYNRDFILYRYPGKPPTYATDNGFEDKILLCCSSNGHYDSVY 129
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
 308-436 1.67e-68

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: 225.71  E-value: 1.67e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  308 MDEYLGSLGLYRKLTAKDASCLFRAVSEQLFHCQIHHMKIRKICVAYMRDNQQNFESYVEGPFEKYLERLEDPKESAGQL 387
Cdd:cd22794      1 MDEYLRSLGLYRKQIAKDGSCLFRAVAEQVFHTQSRHLEVRKACVDYLRRNREKFEAFIEGPFEQYLKNLENPKEWAGQV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1835597353  388 EINALSLIYNRDIILYRYPGKPPTYVTDHGFEEKIMLCCSTNGHYDSVF 436
Cdd:cd22794     81 EISALSLMYKRDFIIYQEPGKPPSNVTENGFPDKILLCFSNGNHYDSVY 129
OTU_ALG13-like cd22753
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 308-436 1.47e-61

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: 205.85  E-value: 1.47e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  308 MDEYLGSLGLYRKLTAKDASCLFRAVSEQLFHCQIHHMKIRKICVAYMRDNQQNFESYVEGPFEKYLERLEDPKESAGQL 387
Cdd:cd22753      1 IDEYLDSLGLYRKHIPRDGSCLFRAVSEQLFFTQSYHQQVRQACVEYLEKNREEFEKFSEISFDDYLERLSDPKEWGGLL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1835597353  388 EINALSLIYNRDIILYRYPGKPPTYVTDHGFEEKIMLCCSTNGHYDSVF 436
Cdd:cd22753     81 ELEALSLLYKVDFIVYSIPDQPPSNITNNGYPKKIMLCYSGGNHYDSVY 129
Tudor_TDRD13 cd20447
Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called ...
 578-657 2.16e-51

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: 175.04  E-value: 2.16e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  578 FAGRQYCLGDKCQVRLETGGKYYNSHIQEVGHDSNSVTVFIEELAEKHIVPLVNLKPVTQVTPVPAWNVSPIRKGGGYQK 657
Cdd:cd20447      1 FAGRQYYLGDKCQVRLEPGGKYYNAHIQEVGQDSNSVTVFIEELAEKHTVPLANLKPVTQVTPVPAWNMMPNRKGGNYQK 80
PssE NF041548
PssE/Cps14G family polysaccharide biosynthesis glycosyltransferase;
5-146 8.09e-31

PssE/Cps14G family polysaccharide biosynthesis glycosyltransferase;


Pssm-ID: 469433 [Multi-domain]  Cd Length: 146  Bit Score: 118.78  E-value: 8.09e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353    5 VFVTVGTTSFDELVARVSEEASVQIlrslgYNKLILQIGRGSVEPKPCSSaaftmevFRYKESLRDDIKWADLVISHAGA 84
Cdd:NF041548     1 IFVTVGTTRFDSLIKAIDELIEGLI-----DYEVTFQIGDGKYIPKNGEY-------FDFLEEIDEYYKKADLIITHAGA 68

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835597353   85 GSCLETLGEGKPLIVVINEKLMGNHQLELAKQLHSDGHLLYCT-CSTLMETLQSMDPSALKPF 146
Cdd:NF041548    69 GTIYSLLELGKKVIVVPNLERVDDHQLDLAEYVEENGYALVCYdLDELEDAIKEAENFKPNPY 131
Glyco_tran_28_C pfam04101
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ...
 5-147 5.32e-29

Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). Structural analysis suggests the C-terminal domain contains the UDP-GlcNAc binding site.


Pssm-ID: 427711 [Multi-domain]  Cd Length: 166  Bit Score: 113.96  E-value: 5.32e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353    5 VFVTVGTTSFDELVARVSEEASVQILRslGYNKLILQIGRGSVEPKPCSSAAFT--MEVFRYKESLRDDIKWADLVISHA 82
Cdd:pfam04101    2 ILVTGGSQGARALNELVLSVLPLLELK--GELQVLHQTGKGDLEEVKIDYAELGinYEVFPFIDNMAEYIKAADLVISRA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353   83 GAGSCLETLGEGKPLIVVINEK----LMGNHQLELAKQLHSDGHLLYC-TCSTLMETLQSMDPSALKPFP 147
Cdd:pfam04101   80 GAGTIAELLALGKPAILVPNPSaargHQDNNAKELVKAGAALVILQKElTPEKLIEALLKLLLNPLRLAE 149
OTU_plant_OTU7-like cd22771
OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar ...
 316-435 4.67e-28

OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar proteins; Arabidopsis thaliana deubiquitinating enzyme OTU7, also called OTU domain-containing protein 7, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that shows a preference for 'Lys-63' over 'Lys-48' over 'Met-1'-linked ubiquitin (UB) tetramers as substrates. DUBs 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. OTU7 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438608 [Multi-domain]  Cd Length: 124  Bit Score: 109.95  E-value: 4.67e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  316 GLYRKLTAKDASCLFRAVSEQLFHCQIHHMKIRKICVAYMRDNQQNFESYVEG--PFEKYLERLEDPKESAGQLEINALS 393
Cdd:cd22771      1 GLRIRDVEGDGNCLFRALADQLYGDEERHAELRKKVVDYMEAHEEDFEPFFEDdeTFEDYVSRMREDGTWGGNLELQAAS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1835597353  394 LIYNRDIILYRYpGKPPTYVTDHGFEEK--IMLCCSTNGHYDSV 435
Cdd:cd22771     81 LVYRVNIVVHQL-GQPRWEIENFPDKGArtIHLSYHDGEHYNSV 123
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
 322-435 3.34e-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.


Pssm-ID: 438581 [Multi-domain]  Cd Length: 128  Bit Score: 99.05  E-value: 3.34e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  322 TAKDASCLFRAVSEQLFHCQIHHMKIRKICVAYMRDNQQNFES------YVEGPFEKYLERLEDPKESAGQLEINALSLI 395
Cdd:cd22744      5 VPGDGNCLFRALAHALYGDQESHRELRQEVVDYLRENPDLYEPaeladeDDGEDFDEYLQRMRKPGTWGGELELQALANA 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1835597353  396 YNRDIILYRY-PGKPPTYVTDHGFEEK---IMLCCSTNGHYDSV 435
Cdd:cd22744     85 LNVPIVVYSEdGGFLPVSVFGPGPGPSgrpIHLLYTGGNHYDAL 128
Tudor_OTUD4 cd20448
Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called ...
 574-637 2.57e-23

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: 94.18  E-value: 2.57e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835597353  574 EYMVFAGRQYCLGDKCQVRLETGGKYYNSHIQEVGHDSNSVTVFIEELAEKHIVPLVNLKPVTQ 637
Cdd:cd20448      1 DFSIAAGMQYSVGDKCKVRLDHNGKFYNAHIQEVSPENGPVVVFVEELGKKHTVPLKNLKPPPQ 64
OTU_OTUD5-like cd22752
OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU ...
 316-437 6.33e-22

OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU domain-containing protein 5 (OTUD5), also called deubiquitinating enzyme A (DUBA), is a phosphorylation-dependent deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that can hydrolyze 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, and may function as negative regulator of the innate immune system. It limits type I interferon production in macrophages and suppresses interleukin-17A production in T cells. OTUD5 also functions in an apoptotic signaling cascade by mediating the sequential activation of PDCD5 (programmed cell death 5) and p53 in response to genotoxic stress. In Drosophila, OTUD5/DUBA is essential for spermatogenesis. This subfamily also includes Arabidopsis thaliana OTU domain-containing protein 6, also called deubiquitinating enzyme OTU6 or otubain-like deubiquitinase 1 (OTLD1), which binds chromatin and has enzymatic histone deubiquitinase activity specific for the H2B histone. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It also includes plant OTU6.


Pssm-ID: 438589 [Multi-domain]  Cd Length: 124  Bit Score: 92.23  E-value: 6.33e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  316 GLYRKLTAKDASCLFRAVSEQLFHCQIHHMKIRKICVAYMRDNQQNFESYVEGPFEKYLERLEDPKESAGQLEINALSLI 395
Cdd:cd22752      1 GFIIKEMEEDGNCLFRAVADQVYGDQEMHDVVRKHCMDYMEKNRDYFSQFVTEDFEEYINRKRQDGVWGNHIEIQAMSEL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1835597353  396 YNRDIILYRYPGKP-PTYVTDHGFE-EKIMLCCSTNGHYDSVFN 437
Cdd:cd22752     81 YNRPIEVYAYSTEPiNTFHEASSSDnEPIRLSYHGNSHYNSIVD 124
Tudor_TDRD13-like cd20380
Tudor domain found in Tudor domain-containing protein 13 (TDRD13) and similar proteins; The ...
 582-635 1.29e-20

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: 86.10  E-value: 1.29e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1835597353  582 QYCLGDKCQVRLETGGKYYNSHIQEVGHDSNSVTVFIEELAEKHIVPLVNLKPV 635
Cdd:cd20380      1 QFKPGDKCQVELDSPGKVYEAHIQEISPDKGPVTVFVEELGEKKTVPYENLKPL 54
OTU_OTUD3-like cd22756
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This ...
 325-435 1.68e-20

OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This subfamily includes bilaterial OTU domain-containing protein 3 (OTUD3), Arabidopsis thaliana deubiquitinating enzyme OTU7, also called OTU domain-containing protein 7, and similar proteins. OTUD3 is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. It is an acetylation-dependent deubiquitinase that restricts innate antiviral immune signaling. It directly hydrolyzes lysine 63 (Lys63)-linked polyubiquitination of MAVS (mitochondrial antiviral-signaling protein) and shuts off innate antiviral immune response. OTUD3 can elicit tumor-suppressing or tumor-promoting activities in a cell- and tissue-dependent manner. It is a DUB for PTEN (phosphatase and tension homologue deleted on chromosome 10); the OTUD3-PTEN signaling axis plays a critical role in suppression of breast tumorigenesis. OTUD3 is also a DUB for glucose-regulated protein GRP78, stabilizing it and promoting lung tumorigenesis. OTU7 is a DUB that shows a preference for 'Lys-63' over 'Lys-48' over 'Met-1'-linked ubiquitin (UB) tetramers as substrates. 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: 438593 [Multi-domain]  Cd Length: 131  Bit Score: 88.39  E-value: 1.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  325 DASCLFRAVSEQLFHCQIHHMKIRKICVAYMRDNQQNFESY--------VEGPFEKYLERLEDPKESAGQLEINALSLIY 396
Cdd:cd22756      8 DGNCLFRALSDQLYGDPDRHLEIRAEVVEYMRANPDDFKPFseaatfaeDDEAFEDYLARMAKDGTYGDNLEIVAFARAY 87

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1835597353  397 NRDIILYR---------------YPGKPPTYVTDHGFEekimlccstngHYDSV 435
Cdd:cd22756     88 NVDVKVYQpdpvyvisapedgspGPARRVLHIAYHNWE-----------HYSSV 130
OTU_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
 325-435 5.93e-18

OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; This subfamily is composed of mammalian OTU domain-containing protein 6A (OTUD6A, also called DUBA-2, vertebrate OTU domain-containing protein 6B (OTUD6B, also called DUBA-5), fungal OTU domain-containing protein 2 (OTU2), and similar proteins. OTUD6A, OTUD6B, and Schizosaccharomyces pombe OTU2 are deubiquitinating enzymes/ubiquitinyl hydrolases (EC 3.4.19.12). OTUD6A hydrolyzes 'Lys-27'-, 'Lys-29'-, and 'Lys-33'-linked polyubiquitin chains, and may also be able to hydrolyze 'Lys-11'-linked ubiquitin chains. It deubiquitylates and stabilizes dynamin-related protein 1 (Drp1), a cytosolic protein responsible for mitochondrial fission and is essential in the initiation and development of several human diseases including cancer, thereby facilitating tumorigenesis. OTUD6B is a functional deubiquitinase in in vitro enzyme assays. It may play a role in the ubiquitin-dependent regulation of protein synthesis downstream of mTORC1, and may modify the ubiquitination of the protein synthesis initiation complex to repress translation. Biallelic variants in OTUD6B cause an intellectual disability syndrome that is associated with seizures and dysmorphic features. 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: 438585 [Multi-domain]  Cd Length: 144  Bit Score: 81.84  E-value: 5.93e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  325 DASCLFRAVSEQLFH-----CQIHHMKIRKICVAYMRDNQQNFESYV---------EGPFEKYLERLEDPKESAGQLEIN 390
Cdd:cd22748     14 DGHCLYRAIADQLKLrggseEPYSYKELRKLAADYMRAHRDDFLPFLtnddgdlmtEEEFEEYCDKIENTAEWGGQLELR 93

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1835597353  391 ALSLIYNRDIILYRyPGKPPTYVTDHGFE-EKIMLC-----CSTNGHYDSV 435
Cdd:cd22748     94 ALSKALKRPIHVYQ-AGSPPLVIGEEFDSgEPLRLSyhrhaYGLGEHYNSV 143
OTU_plant_OTU6-like cd22796
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; ...
 316-435 9.93e-18

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; Deubiquitinating enzyme OTU6, also called OTU domain-containing protein 6 or otubain-like deubiquitinase 1 (OTLD1), is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes 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. OTU6 binds chromatin and has enzymatic histone deubiquitinase activity specific for the H2B histone. OTU6 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438617 [Multi-domain]  Cd Length: 128  Bit Score: 80.55  E-value: 9.93e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  316 GLYRKLTAKDASCLFRAVSEQLFHCQIHHMKIRKICVAYMRDNQQNFESYVEGPFEKYLERLEDPKESAGQLEINALSLI 395
Cdd:cd22796      4 GLEIRRMDGDGNCLFRAVADQVYGDQEMHDEVREMCMDYMEKERDHFSQFVTEDFTQYVKRKRRDRVFGNNLEIQAMSEI 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1835597353  396 YNRDIILYRYPGKPPTYVTDHGFEEK---IMLCCSTNGHYDSV 435
Cdd:cd22796     84 YNRPIEVYSYSNGEPINIFHGSYEGDdppIRLSYHDGNHYNSI 126
OTU_plant_OTU9-like cd22751
OTU (ovarian tumor) domain of plant deubiquitinating enzyme OTU9 and similar proteins; This ...
 309-436 9.18e-16

OTU (ovarian tumor) domain of plant deubiquitinating enzyme OTU9 and similar proteins; This subfamily contains Arabidopsis thaliana deubiquitinating enzymes OTU8, OTU9, OTU10, OTU11, and OTU12, and similar proteins from plants and other eukaryotes. OTU8-OTU12 are 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. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438588 [Multi-domain]  Cd Length: 134  Bit Score: 75.27  E-value: 9.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  309 DEYLGSLGLYRKLTAKDASCLFRAVSEQLFHCQIHHMKIRKICVAYMRDNQQ-NFESYVEGPFEKYLERLEDPKESAGQL 387
Cdd:cd22751      2 LRRLDLYGLVERKVEGDGNCQFRALSDQLFGTQDHHAEVRELVVKQLRAHPElYYEFYVPEEYDEYLKKMSKDGEWGDEL 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1835597353  388 EINALSLIYNRDI-ILYRYPGKPPTYVTDHGFEEK---IMLCCSTNGHYDSVF 436
Cdd:cd22751     82 TLQAAADAFGVKIhVITSFEDNWFLEIEPRGLVRSkrvLFLSYWAEVHYNSIY 134
COG5017 COG5017
UDP-N-acetylglucosamine transferase subunit ALG13 [Carbohydrate transport and metabolism];
5-163 1.32e-15

UDP-N-acetylglucosamine transferase subunit ALG13 [Carbohydrate transport and metabolism];


Pssm-ID: 444041 [Multi-domain]  Cd Length: 164  Bit Score: 75.73  E-value: 1.32e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353    5 VFVTVGTT--SFDELVARVSEEASvQILRSLgynKLILQIGRGSVEPKPCSSAAFtMEvfryKESLRDDIKWADLVISHA 82
Cdd:COG5017      2 IFVTVGTHqlPFDRLVRWVDELAA-EGIIDE---EVFVQTGHTTYVPRNAEAVPF-LP----PDEFQKLIAQARLVISHA 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353   83 GAGSCLETLGEGKPLIVV---------INeklmgNHQLELAKQLHSDGHLLYCTCSTLMETL--QSMDPSALKPFPIGRP 151
Cdd:COG5017     73 GMGSILTALKLGKPFILVprlarygehVD-----DHQLETARALEKLGGIIVVEDPADLEAAldEALALKSPEPFSVPSP 147

                          170
                   ....*....|....
gi 1835597353  152 --EIFAAFLDKAVG 163
Cdd:COG5017    148 arGALVDFLRAFIT 161
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 325-432 1.63e-15

OTU-like cysteine protease; This family is comprised of a group of predicted cysteine proteases, homologous to the Ovarian Tumour (OTU) gene in Drosophila. Members include proteins from eukaryotes, viruses and pathogenic bacterium. The conserved cysteine and histidine, and possibly the aspartate, represent the catalytic residues in this putative group of proteases.


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 74.02  E-value: 1.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  325 DASCLFRAVSEQLF-----HCQIHHMKIRKICVAYMRDNQQNFESYVEGPFEKYLERLEDPKESAGQLEINALSLIYNRD 399
Cdd:pfam02338    3 DGNCLYRSISHQLWgvhdvLRKMLVQELRETLAEYMREHKEEFEPFLEDDETGDIIEIEQTGAWGGEIEIFALAHILRRP 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1835597353  400 IILYRYPGKPPT-------YVTDHGFEEKIMLC-----CSTNGHY 432
Cdd:pfam02338   83 IIVYKSEGGEELgglkeygIYLPLGWDPSLCLVyprhlYYLGGHY 127
OTU_232R-like cd22758
OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase ...
 312-435 6.00e-14

OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase 232R and similar proteins; This subfamily contains putative ubiquitin thioesterases 232R from Invertebrate iridescent virus and L96 from Tipula iridescent virus (TIV), Dictyostelium discoideum OTU domain-containing protein DDB_G0284757, and similar proteins. L96 may be involved in TIV genomic DNA packaging in a manner related to the Gag polyproteins of the mammalian viruses. Proteins in this subfamily contain an OTU domain. 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. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438595 [Multi-domain]  Cd Length: 135  Bit Score: 69.99  E-value: 6.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  312 LGSLGLYRKLTAKDASCLFRAVSEQLFHCQI--HHMKIRKICVAYMRDNQQNFESYV------EGPFEKYLERLEDPKES 383
Cdd:cd22758      1 AKENGFEIRDVPGDGNCFFHAVSDQLYGNGIehSHKELRQQAVNYLRENPELYDGFFlsefdeEESWEEYLNRMSKDGTW 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1835597353  384 AGQLEINALSLIYNRDI-ILYRYPGKPPTYVTDHGFEEK--IMLCCSTNGHYDSV 435
Cdd:cd22758     81 GDHIILQAAANLFNVRIvIISSDGSDETTIIEPGNSKNGrtIYLGHIGENHYVSL 135
OTU_OTUD1 cd22747
OTU (ovarian tumor) domain of OTU domain-containing protein 1 and similar proteins; OTU ...
 303-437 1.13e-13

OTU (ovarian tumor) domain of OTU domain-containing protein 1 and similar proteins; OTU domain-containing protein 1 (OTUD1), also called DUBA-7 in humans, is a deubiquitinating enzyme/ubiquitinyl hydrolase (EC 3.4.19.12) that specifically hydrolyzes 'Lys-63'-linked polyubiquitin to monoubiquitin; this specificity is facilitated by the C-terminal Ub-interacting motif (UIM) of OTUD1. It interacts and promotes the deubiquitination of myeloid cell leukemia 1 (MCL1), a pro-survival Bcl-2 family protein that plays important roles in cell survival, proliferation, differentiation and tumorigenesis. OTUD1 also deubiquitinates IFN regulatory factor 3 (IRF3) and attenuates its function; IRF3 is critical for the transcription of type I IFNs in defensing virus and promoting inflammatory responses. Loss-of-function mutations of OTUD1 associated with multiple autoimmune diseases including systemic lupus erythematosus (SLE), rheumatoid arthritis (RA), ulcerative colitis (UC) and Hashimoto's thyroiditis (HT). OTUD1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438584 [Multi-domain]  Cd Length: 149  Bit Score: 69.45  E-value: 1.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  303 LTEVTM-DEYLGSLGLYRKLTAKDASCLFRAVSEQLFHCQIHHMKIRKICVAYMRDNQQNFESYVEGPFEKYLERLEDPK 381
Cdd:cd22747      6 LAEVEKqDKYLRERNKYRFHIIPDGNCLYRAVSKAVYGDQALHRELREQTVHYIADHLDEFNPIIEGDVGEFLIKAAQDG 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835597353  382 ESAGQLEINALSLIYNRDIILYR--YPGKPPTYVTDHGFEEK------IMLCCSTNGHYDSVFN 437
Cdd:cd22747     86 AWAGYPELLAMGQMLNVNIRLTTggSLESPTVSTMVHYLGPEdsgkpsIWLSWLSNGHYDAVFD 149
OTU_OTUD3 cd22770
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU ...
 312-435 6.79e-13

OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU domain-containing protein 3 (OTUD3) is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. It is an acetylation-dependent deubiquitinase that restricts innate antiviral immune signaling. It directly hydrolyzes lysine 63 (Lys63)-linked polyubiquitination of MAVS (mitochondrial antiviral-signaling protein) and shuts off innate antiviral immune response. OTUD3 can elicit tumor-suppressing or tumor-promoting activities in a cell- and tissue-dependent manner. It is a DUB for PTEN (phosphatase and tension homologue deleted on chromosome 10); the OTUD3-PTEN signaling axis plays a critical role in suppression of breast tumorigenesis. OTUD3 is also a DUB for glucose-regulated protein GRP78, stabilizing it and promoting lung tumorigenesis. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438607 [Multi-domain]  Cd Length: 145  Bit Score: 67.31  E-value: 6.79e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  312 LGSLGL-YRKLTAkDASCLFRAVSEQLFHCQIHHMKIRKICVAYMRDNQQNFESYVEG--PFEKYLERLEDPKESAGQLE 388
Cdd:cd22770      9 LQALGLkLRDIPG-DGNCLFRALGDQLEGHSRNHLKHRQETVQYMIEHREDFEPFVEDdvPFDKHVANLSKPGTYAGNDA 87

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1835597353  389 INALSLIYNRDIILYRyPGKPPTYV---TDHGFEEkimLCCS-TNG-HYDSV 435
Cdd:cd22770     88 IVAFARLHQVNVVIHQ-LNAPLWQIrgtEKSSSRE---LHISyHNGdHYSSV 135
OTU_plant_OTU5-like cd22797
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU5 from plants and similar proteins; ...
 312-435 1.32e-12

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU5 from plants and similar proteins; Deubiquitinating enzyme OTU5, also called OTU domain-containing protein 6, is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes 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. OTU5 is an inactive cysteine protease. It regulates gene expression by contributing to chromatin organization and DNA methylation patterns (e.g. H3K4me3 and H3K27me3). It is required for phosphate (Pi) homeostasis. OTU5 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438618 [Multi-domain]  Cd Length: 149  Bit Score: 66.60  E-value: 1.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  312 LGSLGLYRKLTAKDASCLFRAVSEQL-----FHCQIHHMKIRKICVAYMRDNQQNFESYVEGP---------FEKYLERL 377
Cdd:cd22797      5 LAPLGLAIKEIKADGHCLYRAVEDQLqlrggGAPAPDYQQLRELAADYMRAHPDDFLPFLEDEdeggdgdeaFEAYCREV 84

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835597353  378 EDPKESAGQLEINALSLIYNRDIILyrYPGKPPTYVTDHGF---EEKIMLCCSTNG-----HYDSV 435
Cdd:cd22797     85 ESTAAWGGQLELGALAHALRRHIKV--YSAGMPDVEMGEEYagtGPPLRLCYHRHAfglgeHYNSV 148
OTU_fungi_OTU2-like cd22762
OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; ...
 325-421 1.06e-11

OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; This subfamily includes Schizosaccharomyces pombe and Saccharomyces cerevisiae OTU domain-containing protein 2 (OTU2) and similar proteins. S. pombe OTU2 is a ubiquitin thioesterase/hydrolase (EC 3.4.19.12) that can remove conjugated ubiquitin from protein substrates and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Fungal OTU2 bbelongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438599 [Multi-domain]  Cd Length: 142  Bit Score: 63.79  E-value: 1.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  325 DASCLFRAVSEQLfhcQIHHM-------KIRKICVAYMRDNQQNFESYV------EGPFEKYLERLEDPKESAGQLEINA 391
Cdd:cd22762     15 DGHCLFAAIADQL---QLRGSeinldykELRKLAAEYIRKHPDDFEPFLfeetdeLEDIDEYCKKIENTAEWGGELELLA 91

                           90       100       110
                   ....*....|....*....|....*....|
gi 1835597353  392 LSLIYNRDIILYRYPGKPPTYVTDHGFEEK 421
Cdd:cd22762     92 LAKAFGVPIHVVQAEGRVIKINEEGDSDKP 121
OTU_P87_VP80-like cd22757
OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The ...
 325-433 1.32e-11

OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The VP80 protein is a capsid-associated structural protein that was first identified as P87 in Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus (OpMNPV); its homologs are found only in NPV genomes. The Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) VP80 protein is essential for the formation of both budded virus (BV) and occlusion-derived virus (ODV). It has also been shown to interact with the virus-triggered, nuclear F-actin cytoskeleton. P87/VP80 contains an N-terminal OTU domain. 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. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438594 [Multi-domain]  Cd Length: 128  Bit Score: 62.99  E-value: 1.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  325 DASCLFRAVSEQLFHCQIHHMKIRKICVAYMRDNQQNFESYV---EGPFEKYLERLED----PKESAGQLEINALSLIYN 397
Cdd:cd22757      9 DGACLFRALSYLLYGTQSRHLEVRKEVVDYVVNNWDEFSIYThdsEGNNYKSAEEYRAdmskPGTYGTLCELVAAAELYP 88

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1835597353  398 RDIILYRyPGKPPTYVTDHGFEEKIMLCCS--TNGHYD 433
Cdd:cd22757     89 FHFEVYR-NGKLYASFGDPSNPVKRLKFSGdlSNGHFD 125
OTU_OTUD6 cd22761
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; ...
 310-400 1.47e-11

OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; This subfamily is composed of mammalian OTU domain-containing protein 6A (OTUD6A, also called DUBA-2) and vertebrate OTU domain-containing protein 6B (OTUD6B, also called DUBA-5), which are deubiquitinating enzymes/ubiquitinyl hydrolases (EC 3.4.19.12). OTUD6A hydrolyzes 'Lys-27'-, 'Lys-29'-, and 'Lys-33'-linked polyubiquitin chains, and may also be able to hydrolyze 'Lys-11'-linked ubiquitin chains. It deubiquitylates and stabilizes dynamin-related protein 1 (Drp1), a cytosolic protein responsible for mitochondrial fission and is essential in the initiation and development of several human diseases including cancer, thereby facilitating tumorigenesis. OTUD6B is a functional deubiquitinase in in vitro enzyme assays. It may play a role in the ubiquitin-dependent regulation of protein synthesis downstream of mTORC1, and may modify the ubiquitination of the protein synthesis initiation complex to repress translation. Biallelic variants in OTUD6B cause an intellectual disability syndrome that is associated with seizures and dysmorphic features. 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: 438598 [Multi-domain]  Cd Length: 146  Bit Score: 63.29  E-value: 1.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  310 EYLGSLGLYRKLTAKDASCLFRAVSEQLfhcQIHHMKI-----RKICVAYMRDNQQNF----------ESYVEGPFEKYL 374
Cdd:cd22761      3 KILKERGLKIHEIPSDGDCLYNAIAHQL---SLRGIETsveelRKQTADYMRENKDDFlpfltnpdtgDPLTEEEFEKYC 79

                           90       100
                   ....*....|....*....|....*.
gi 1835597353  375 ERLEDPKESAGQLEINALSLIYNRDI 400
Cdd:cd22761     80 DDVENTGAWGGQLELRALSHVLKRPI 105
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
 325-403 2.25e-09

OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and OTU domains, and similar proteins; This subfamily is composed of mostly uncharacterized proteins containing an OTU domain, similar to Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and OTU domains. OTU domain-containing proteins 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. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438592 [Multi-domain]  Cd Length: 132  Bit Score: 56.89  E-value: 2.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  325 DASCLFRAVSEQLFHCQIHHMKIRKICVAYMRDNQQNFESYV---EGPFEKYLERLEDPKES--AGQLEINALSLIYNRD 399
Cdd:cd22755      9 DGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKNPDEFRNLLrsdYESVEEYLEKSRMRYDGtwATDVEIFAAATLLGVD 88


                   ....
gi 1835597353  400 IILY 403
Cdd:cd22755     89 IYVY 92
OTU_plant_OTU3_4-like cd22746
OTU (ovarian tumor) domain of deubiquitinating enzymes OTU3 and OTU4 from plants, and similar ...
 325-433 8.77e-08

OTU (ovarian tumor) domain of deubiquitinating enzymes OTU3 and OTU4 from plants, and similar proteins; Deubiquitinating enzyme OTU3 (also called OTU domain-containing protein 3) and deubiquitinating enzyme OTU4 (also called OTU domain-containing protein 4) are deubiquitinases (DUBs) or 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. OTU3 and OTU4 may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438583 [Multi-domain]  Cd Length: 141  Bit Score: 52.27  E-value: 8.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  325 DASCLFRAVSEQLFHC------------QIHHmKIRKICVAYMRDNQQNFES---YVEGPFEKYLERLEDPKESAGQLEI 389
Cdd:cd22746     10 DGRCLFRAVARGLALAtggrplserrerADAD-ALRKAVVEEIRKRRDELFEgslVIEGDFDAYCQRMSHPDTWGGEPEL 88

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1835597353  390 NALSLIYNRDIILYRYPGKPP------TYVTDHGFEEKIMLCCSTNGHYD 433
Cdd:cd22746     89 LMLADVLQRPIAVYLPTPGKGglrkiqEYGEEYLGGEPIRLLYNGGNHYD 138
OTU_plant_OTU1_2-like cd22793
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU1 and OTU2 from plants and similar ...
 319-433 2.01e-06

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU1 and OTU2 from plants and similar proteins; Deubiquitinating enzyme OTU2, also called OTU domain-containing protein 2, is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes 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. OTU2 exhibited equivalent binding affinities for K48- and K63-linked ubiquitin chains and no cleavage activity toward linear UB chains. It may also be involved in endoplasmic-reticulum-associated protein degradation (ERAD). OTU2 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438614  Cd Length: 163  Bit Score: 48.86  E-value: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  319 RKLTAKDASCLFRAVSEQLFHCQIHHMKIRKICVAYMRDNQQNF-ESYVEGPFEKYLERLEDPKESAGQLEINALSLIYN 397
Cdd:cd22793      5 RRVIDSDNSCLFNAVGYVMEGSRKKAPELRQVIADAVLSDPFEYnEAFLGKSNKEYCEWILNPNSWGGAIELSILSDHYG 84

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1835597353  398 RDIILYRY-PGKPPTYVTDHGFEEKIMLCcsTNG-HYD 433
Cdd:cd22793     85 REIAAFDIqTKRCDVYGEGKGYTERVMLI--YDGlHYD 120
YjiC COG1819
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
5-100 3.33e-06

UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];


Pssm-ID: 441424 [Multi-domain]  Cd Length: 268  Bit Score: 50.24  E-value: 3.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353    5 VFVTVGTTSFD--ELVARVseeasVQILRSLGYNkLILQIGRGSVEPKPCSSAafTMEVFRYkESLRDDIKWADLVISHA 82
Cdd:COG1819    123 VYVTLGTSANDraDLLRAV-----LEALADLGVR-VVVTTGGLDPAELGPLPD--NVRVVDY-VPQDALLPRADAVVHHG 193

                           90
                   ....*....|....*...
gi 1835597353   83 GAGSCLETLGEGKPLIVV 100
Cdd:COG1819    194 GAGTTAEALRAGVPQVVV 211
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 807-1014 5.47e-06

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: 50.34  E-value: 5.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  807 NGEEPRGLEETITFYEIEEGDETAFPAINSQGSSSPIVPTT--AGFWVTRRGPTSITSgkqTMTSSEEEVDEPSDGG--- 881
Cdd:pfam17823   31 NKMWNGAGKQNASGDAVPRADNKSSEQ*NFCAATAAPAPVTltKGTSAAHLNSTEVTA---EHTPHGTDLSEPATREgaa 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  882 DFHGDYIYTASDSGFETPVLYGTTESTANLSLQDDGPPSGPSPEGSVSYSYSQQVSAAV-----ISTSTCASTAPTPLIT 956
Cdd:pfam17823  108 DGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASaphaaSPAPRTAASSTTAASS 187

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835597353  957 SNSATLAPVTSAVPAQ---TAVHPIIMSPAAVGRPGLPSVPFPFYSPPPTPATETVDPGNV 1014
Cdd:pfam17823  188 TTAASSAPTTAASSAPatlTPARGISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTV 248
GT28_MurG cd03785
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ...
 10-121 3.14e-05

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340818 [Multi-domain]  Cd Length: 350  Bit Score: 47.60  E-value: 3.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353   10 GTTSFDELVARVSEEasvqiLRSLGYNkLILQIGRGSVEP--KPCSSAAFTMEVFRYKESLRDDIKWADLVISHAGAGSC 87
Cdd:cd03785    192 GARAINRAVPKALPK-----LLERGIQ-VIHQTGKGDYDEvkKLYEDLGINVKVFPFIDDMAAAYAAADLVISRAGASTI 265

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1835597353   88 LETLGEGKPLIVVINEKLMGNHQLELAKQLHSDG 121
Cdd:cd03785    266 AELTAAGKPAILIPYPYAADDHQEANARALEKAG 299
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 905-1199 5.10e-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: 47.84  E-value: 5.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  905 TESTANLSLQDDGPPSGPSPEGSVSysysqQVSAAVISTSTCASTAPTPLITSNSATLAPVTSAVPAQT----AVHPIIM 980
Cdd:pfam03154  158 SDSSAQQQILQTQPPVLQAQSGAAS-----PPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTqstaAPHTLIQ 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  981 SPAAVGRPGLPS-----VPFPFYSPPP-TPATETVDPGNVPPPPPPPPPYSCDPSGSDLPRDTKVLQYYFNLGlQCyhqs 1054
Cdd:pfam03154  233 QTPTLHPQRLPSphpplQPMTQPPPPSqVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSS-QS---- 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353 1055 ywhsmvymQHVPQPTPVEPYPVFSDPVPIIDQTVPQMYNdgriDGRHVPLEPANGAFPNVEassvPHGTVYYPVMADPYS 1134
Cdd:pfam03154  308 --------QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQ----PPREQPLPPAPLSMPHIK----PPPTTPIPQLPNPQS 371

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835597353 1135 Q-------PPLP-GYESCVPIVPTYHYVSSWHPANPSYGSSPRIHNTVNSGQLHQvsyvAAASPPTHFVSQSI 1199
Cdd:pfam03154  372 HkhpphlsGPSPfQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPP----PPAQPPVLTQSQSL 440
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 829-1009 8.98e-05

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: 46.83  E-value: 8.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  829 TAFPAINSQGSSSPivPTTAGFWVTRRGPTSITSgkqtmtsseeevdePSDGGDfhgdyiyTASDSGFETPVLYGTTEST 908
Cdd:pfam05109  429 TTSPTLNTTGFAAP--NTTTGLPSSTHVPTNLTA--------------PASTGP-------TVSTADVTSPTPAGTTSGA 485

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  909 ANLSlqddgPPSGPSPEGSVSYSYSQQVSAAVISTSTCASTAPTPLITS-----NSATL------APVTSAVPAQTAVHP 977
Cdd:pfam05109  486 SPVT-----PSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTptpnaTSPTLgktsptSAVTTPTPNATSPTP 560

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1835597353  978 IIMSP---AAVGRPGLPSVPFPFYSPPPTPATETV 1009
Cdd:pfam05109  561 AVTTPtpnATIPTLGKTSPTSAVTTPTPNATSPTV 595
Tudor_SMN_SPF30-like cd21182
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ...
 586-635 1.32e-04

Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing factor 30 (SPF30), and similar proteins; This group contains SMN, SPF30, Tudor domain-containing protein 3 (TDRD3), DNA excision repair protein ERCC-6-like 2 (ERCC6L2), and similar proteins. SMN, also called component of gems 1, or Gemin-1, is part of a multimeric SMN complex that includes spliceosomal Sm core proteins and plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. SPF30, also called 30 kDa splicing factor SMNrp, SMN-related protein, or survival motor neuron domain-containing protein 1 (SMNDC1), is an essential pre-mRNA splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. Members of this group contain a single 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: 410549  Cd Length: 50  Bit Score: 40.70  E-value: 1.32e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1835597353  586 GDKCQVRLETGGKYYNSHIQEVGHDSNSVTVFIEELAEKHIVPLVNLKPV 635
Cdd:cd21182      1 GDKCLAPYSDDGKYYEATIEEITEESDTATVVFDGYGNSEEVPLSDLKPL 50
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
 888-1001 3.66e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 44.70  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  888 IYTASDSGFETPvlyGTTESTANLSLQDDGPPSGPSPEGSVSYSYSQQVSAAVISTSTCASTAPTPLITSN-------SA 960
Cdd:PRK08691   407 VQTASAAAMPSE---GKTAGPVSNQENNDVPPWEDAPDEAQTAAGTAQTSAKSIQTASEAETPPENQVSKNkaadnetDA 483

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1835597353  961 TLAPVTSAVPAQTAVHPIIMSPAAVGRPGlPSVPFPFYSPP 1001
Cdd:PRK08691   484 PLSEVPSENPIQATPNDEAVETETFAHEA-PAEPFYGYGFP 523
PHA03247 PHA03247
large tegument protein UL36; Provisional
 917-1157 3.68e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 3.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  917 GPPSGPSPEGSVSYSYSQQVSAAVISTSTCASTAPTPlitsnsATLAPVTSAVPAQTAVHPIIMSPAavgrPGLPSVPFP 996
Cdd:PHA03247  2765 GPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSP------WDPADPPAAVLAPAAALPPAASPA----GPLPPPTSA 2834

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  997 FYSPPPTPatetvdPGNVPPPPPP---------------PPPYSCDPSGSDLPRDTKVLQyyfnLGLQCYHQSYWHSMVY 1061
Cdd:PHA03247  2835 QPTAPPPP------PGPPPPSLPLggsvapggdvrrrppSRSPAAKPAAPARPPVRRLAR----PAVSRSTESFALPPDQ 2904

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353 1062 MQHVPQPTPVEPyPVFSDPVPIIDQTVPQMYNDGRIDGrhvPLEP---------ANGAFPNVEASSVPHGTVYYPVMADP 1132
Cdd:PHA03247  2905 PERPPQPQAPPP-PQPQPQPPPPPQPQPPPPPPPRPQP---PLAPttdpagagePSGAVPQPWLGALVPGRVAVPRFRVP 2980

                          250       260
                   ....*....|....*....|....*...
gi 1835597353 1133 YSQPPLPGYESCVPiVPTYHY---VSSW 1157
Cdd:PHA03247  2981 QPAPSREAPASSTP-PLTGHSlsrVSSW 3007
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
 325-404 1.04e-03

OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase L is also called protein L, large structural protein, replicase, transcriptase, or ubiquitin thioesterase. It displays RNA-directed RNA polymerase (EC 2.7.7.48), deubiquitinase (DUB)/ubiquitin thiolesterase (EC 3.4.19.12), and deISGylating activities. It is a viral homolog of ovarian tumor protease (vOTU) that has been implicated in the downregulation of type I interferon immune response by removing post-translational modifying proteins ubiquitin (Ub) and the Ub-like interferon-simulated gene 15 (ISG15) from host cellular proteins. The attachment of Ub and ISG15 to cellular proteins mediates important innate antiviral responses, and their removal inhibits these antiviral pathways. 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: 438580  Cd Length: 148  Bit Score: 40.66  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  325 DASCLFRAVSEQLFHCQIHHMKIRKICVAYMRdnqQNFESYVEGPF-----EKYLERLEDPKESAGQLEINALSLIYNRD 399
Cdd:cd21880     30 DGNCFFRSIAELLFDTEDEWRLVKNTIESYAR---ANWDECPEARLyylslEEYLRDAMKDGYWGGSLEAEILSKALGIT 106


                   ....*
gi 1835597353  400 IILYR 404
Cdd:cd21880    107 IIIWV 111
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 585-634 1.28e-03

Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar proteins; dTUD is required during oogenesis for the formation of primordial germ cells and for normal abdominal segmentation. It contains 11 Tudor domains. The family also includes mitochondrial A-kinase anchor protein 1 (AKAP1) and Tudor domain-containing proteins (TDRDs). AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), or dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), or protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. TDRDs have diverse biological functions and may contain one or more copies of the 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: 410450  Cd Length: 50  Bit Score: 37.88  E-value: 1.28e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1835597353  585 LGDKCQVRLETGGKYYNSHIQEVgHDSNSVTVFIEELAEKHIVPLVNLKP 634
Cdd:cd20379      1 VGDLCAAKYEEDGKWYRARVLEV-LSNDKVEVFFVDYGNTETVPLSDLRP 49
MurG COG0707
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ...
 60-117 2.27e-03

UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440471 [Multi-domain]  Cd Length: 363  Bit Score: 41.65  E-value: 2.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835597353   60 EVFRYKESLRDDIKWADLVISHAGAGSCLETLGEGKPLIVVINEKLMGNHQLELAKQL 117
Cdd:COG0707    244 EVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARAL 301
Tudor_SPF30 cd20399
Tudor domain found in survival of motor neuron-related-splicing factor 30 (SPF30) and similar ...
 585-636 2.29e-03

Tudor domain found in survival of motor neuron-related-splicing factor 30 (SPF30) and similar proteins; SPF30, also called 30 kDa splicing factor SMNrp, SMN-related protein, or survival motor neuron domain-containing protein 1 (SMNDC1), is an essential pre-mRNA splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. Overexpression of SPF30 causes apoptosis. 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: 410470 [Multi-domain]  Cd Length: 55  Bit Score: 37.29  E-value: 2.29e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1835597353  585 LGDKCQVRLETGGKYYNSHIQEVGHDSnSVTVFIEELAEKHIVPLVNLKPVT 636
Cdd:cd20399      3 VGDKCMAVWSEDGQYYEATIEEISEDG-TCTVTFDGYGNTEVTPLSQLKPRE 53
OTU_OTU1 cd22745
OTU (ovarian tumor) domain of ubiquitin thioesterase OTU1 and similar proteins; Ubiquitin ...
 325-473 4.44e-03

OTU (ovarian tumor) domain of ubiquitin thioesterase OTU1 and similar proteins; Ubiquitin thioesterase (EC 3.4.19.12) OTU1 is also called OTU domain-containing protein 1 in yeast, while human OTU1 is also called HIV-1-induced protease 7 (HIN7), DUBA-8, or OTU domain-containing protein 2 (OTUD2). OTU1 is a deubiquitinase (DUB) that catalyzes 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. OTU1 has been implicated in the ER-associated degradation (ERAD) pathway. In yeast, it counteracts the activity of Ufd2 by deubiquitinating Ufd2 substrates; Ufd2 is a E4 ubiquitin ligase that interacts with Cdc48, an AAA ATPase that plays a central role in the ERAD pathway by chaperoning proteins to the proteasome for destruction. OTU1 also functions as a substrate-processing factor of valosin-containing protein (VCP, the mammalian counterpart of yeast Cdc48) that is required for the retrotranslocation of the ERAD pathway. OTU1 has been shown to preferentially hydrolyze polyubiquitin chains with Lys48 linkages. It contains ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a C2H2-type zinc finger, and an OTU (ovarian tumor) domain. This model represents the OTU domain that interacts with ubiquitin and possesses catalytic activity. OTU1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. This family also contains plant OTU1 and OTU2.


Pssm-ID: 438582  Cd Length: 161  Bit Score: 39.00  E-value: 4.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  325 DASCLFRAVSEQLFHCQI-HHMKIRKICVAYMRDNQQNFESYVEG-PFEKYLERLEDPKESAGQLEINALSLIYNRDII- 401
Cdd:cd22745     11 DNSCLFTSISYLLEGGLLdSAPELREIVADAILSDPDTYNEAILGkPPDEYCAWILKPDSWGGAIELSILSKHFGVEICv 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353  402 -------LYRYpGKpptyvtDHGFEEKIMLCCStnG-HYDS-VFNKQFQTDAAICQAvlyetlykgVFAVDEEE-LRSAV 471
Cdd:cd22745     91 vdvqtgrVDRF-GE------DKGYSKRIFLLYS--GiHYDAlALNPSLDAPEDFDVT---------VFSVSDDEvLEAAL 152


                   ..
gi 1835597353  472 EL 473
Cdd:cd22745    153 EL 154
GT1_Gtf-like cd03784
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ...
 5-100 7.18e-03

UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.


Pssm-ID: 340817 [Multi-domain]  Cd Length: 404  Bit Score: 40.23  E-value: 7.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835597353    5 VFVTVGTTsFDELVARVSEEAsVQILRSLGYNKLIlqigrgSVEPKPCSSAAFTMEVFRYkeslrddIKWA--------- 75
Cdd:cd03784    242 VYVSFGSM-VRDLPEELLELI-AEALASLGQRFLW------VVGPDPLGGLERLPDNVLV-------VKWVpqdellahp 306

                           90       100
                   ....*....|....*....|....*..
gi 1835597353   76 --DLVISHAGAGSCLETLGEGKPLIVV 100
Cdd:cd03784    307 avGAFVTHGGWNSTLEALYAGVPMVVV 333
 
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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