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Conserved domains on  [gi|291226516|ref|XP_002733238|]
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PREDICTED: uncharacterized protein LOC100378309, partial [Saccoglossus kowalevskii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
 331-459 4.67e-58

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: 196.71  E-value: 4.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  331 CKTKTIKEDGNCFFRALSYALSGTENNHRKIRLAIVKHLKDNPTAFRSCLRSDYDSVENYLLASRMKYLTTWATEVEILA 410
Cdd:cd22755     1 CKTIKIVGDGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKNPDEFRNLLRSDYESVEEYLEKSRMRYDGTWATDVEIFA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 291226516  411 AADLLRTDIYTFTRD--KWLKYSNHQIHNNALNSGKAIYLKHCLNIHYEFV 459
Cdd:cd22755    81 AATLLGVDIYVYSKGgyKWLLYSPRFKLGKRNGSREAIYLKNTNGNHFEPV 131
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 1689-2107 1.80e-47

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


:

Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 179.40  E-value: 1.80e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1689 HMFLSGGAGTGKSHLIKAIyyeaSRILAHTVPRpddisVLLTAPTGVAA------FNIDALTIHSTFAiavdaklpYQPL 1762
Cdd:COG0507   142 VSVLTGGAGTGKTTTLRAL----LAALEALGLR-----VALAAPTGKAAkrlsesTGIEARTIHRLLG--------LRPD 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1763 GEEKINTIRSKLANLQILIIDEISMVDKRLLVYVhgrLRQIkqtgdysPFGNVSVIAVGDFYQLAPVKGKALFVenqgiD 1842
Cdd:COG0507   205 SGRFRHNRDNPLTPADLLVVDEASMVDTRLMAAL---LEAL-------PRAGARLILVGDPDQLPSVGAGAVLR-----D 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1843 LWND-YFSIAELTHIVRQ-QDSKFAETLNNIRtRQKSDEMLT---SDVNMLRCRETGEECDGIY---------------I 1902
Cdd:COG0507   270 LIESgTVPVVELTEVYRQaDDSRIIELAHAIR-EGDAPEALNaryADVVFVEAEDAEEAAEAIVelyadrpaggediqvL 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1903 FATNKEVDKCNVEklhslcsdpicIRAQdFSRNHKSKKLERKDtlyvkvyntnlaKTVTLAVGARVMLIKNiDVSDGLVN 1982
Cdd:COG0507   349 APTNAGVDALNQA-----------IREA-LNPAGELERELAED------------GELELYVGDRVMFTRN-DYDLGVFN 403

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1983 GVFGTVSYISLNPGeifpsKIFVVFDNKKVgIKLrsqseSFSSLPEnstqinpqedrvnngggirrqfpLKLAWACTVHK 2062
Cdd:COG0507   404 GDIGTVLSIDEDEG-----RLTVRFDGREI-VTY-----DPSELDQ-----------------------LELAYAITVHK 449

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 291226516 2063 VQGLTVEKATVSLGK----IFSPGQAYVALSRVKTLNGLVI-KEFKESAL 2107
Cdd:COG0507   450 SQGSTFDRVILVLPSehspLLSRELLYTALTRARELLTLVGdRDALARAV 499
Helitron_like_N pfam14214
Helitron helicase-like domain at N-terminus; This family is found in Helitrons, recently ...
 921-1115 1.37e-35

Helitron helicase-like domain at N-terminus; This family is found in Helitrons, recently recognized eukaryotic transposons that are predicted to amplify by a rolling-circle mechanism. In many instances a protein-coding gene is disrupted by their insertion.


:

Pssm-ID: 464105  Cd Length: 199  Bit Score: 135.10  E-value: 1.37e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516   921 RLMNADGRFARNTDFIFYAQYLSEVQQVVSNVSIALRKGSTKSCSKTITASTLIDtqSLKDILKNDEGYK-------FMK 993
Cdd:pfam14214    4 RLQHHDGRFARHPRFLFVAFNLFQQARAESRRLSFIRVNQKELRAESYTGERLRD--ALEEETDDPEVLAllgsiviLPS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516   994 PIRGTPPFWQSAQKDLFAMLRQLGIPTWFCSFSSADMrWPEmiesILNERGDYCKTEELDWSEK-CAILRNNPVTAARMF 1072
Cdd:pfam14214   82 SVPGSPRYMLQLRQDAMAIVRRLGKPDLFITFTPNDL-WPE----IKRELARYREWKLPGAQTRlRRLASDRPDIVARVF 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 291226516  1073 EHRFHCFLKRVILSPAEPIGKIEDYFYRVEFQQRGSPHTHCLF 1115
Cdd:pfam14214  157 HRKLELFLKDLLRFKEGVFGNVSAYVYTVEFQKRGLPHAHGLL 199
DUF6570 pfam20209
Domain of unknown function (DUF6570); This entry represents a presumed domain of unknown ...
 677-815 5.40e-19

Domain of unknown function (DUF6570); This entry represents a presumed domain of unknown function that is found in a wide range of proteins that includes eukaryotic transposon protein.


:

Pssm-ID: 466360  Cd Length: 134  Bit Score: 85.08  E-value: 5.40e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516   677 KGRMPAEASVNNLHLQRIPQKLNCLNSLEQHLIGLHIPFMKMLAL--PKGGQNGVHGPVVCVPSSIDKtTSILPRSgPDD 754
Cdd:pfam20209    1 RGKLPKFSLANGLWIGEVPEELQDLTFVEELLIARVRPRVYVVKLrpKSGGQRGLRGNVIAFPQDVGK-LSVLPRP-PED 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291226516   755 --QMIQVKLKR-KLTYKGHYQYQF-VNDSHIKNALRYLKMNNKWYNNVEyntdwtnplsrIDEEN 815
Cdd:pfam20209   79 ldDVIAVLFIGpKKPTKEWLKKPFrVRRAKVRAALRWLKANNPLYRDIE-----------IDEEN 132
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 2140-2299 6.34e-07

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


:

Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 51.84  E-value: 6.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  2140 MLHNIEGLYSHIEDLKFDKRFL-------KADIICLTETWLPNANPPSVLQLDNFRFHHqprslCYDTSDKltaelkeQA 2212
Cdd:pfam03372    1 LTWNVNGGNADAAGDDRKLDALaalirayDPDVVALQETDDDDASRLLLALLAYGGFLS-----YGGPGGG-------GG 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  2213 HGGVGVYYSF-------HRCIEFLDLSIS--NLEYLAFHVNDANMKVAVVYRPRSYKADVFRRNLLTLATEMDKIPGGTI 2283
Cdd:pfam03372   69 GGGVAILSRYplssvilVDLGEFGDPALRgaIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVI 148

                          170
                   ....*....|....*..
gi 291226516  2284 IMGDFNE-NLFVSSSVR 2299
Cdd:pfam03372  149 LAGDFNAdYILVSGGLT 165
Herpes_teg_N super family cl04795
Herpesvirus tegument protein, N-terminal conserved region;
68-213 3.13e-06

Herpesvirus tegument protein, N-terminal conserved region;


The actual alignment was detected with superfamily member pfam04843:

Pssm-ID: 461453 [Multi-domain]  Cd Length: 183  Bit Score: 49.81  E-value: 3.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516    68 SFHQGDPQFLNNSGRQCVANA---LVSVIFSNIKDICSWDKydLDTILRSGNELYGYLQNSTTI-NHELLLVTELPQIL- 142
Cdd:pfam04843    1 SRNQFDCKFGPRAGSQCLSNCvsfLHSSYLNGINPVLSREA--LDAVLEEGARLDTLLRTSGRLpPRQYAQLHEIPGIIi 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516   143 ------------DIF-DTQFTLSigEPLFGIIGKVAVETDFFMSFDNALNVSLREYNACFVIFGGAAFAVIKKDSIYWVF 209
Cdd:pfam04843   79 tgawgcliyrssEIYgLLGHELS--RNFNGTPQTGDIDTQMPAGIFFRYAKAKRRPSYTLIICNSLAMAIVIKDKTYYLF 156


                   ....
gi 291226516   210 DSHS 213
Cdd:pfam04843  157 DPHC 160
 
Name Accession Description Interval E-value
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
 331-459 4.67e-58

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: 196.71  E-value: 4.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  331 CKTKTIKEDGNCFFRALSYALSGTENNHRKIRLAIVKHLKDNPTAFRSCLRSDYDSVENYLLASRMKYLTTWATEVEILA 410
Cdd:cd22755     1 CKTIKIVGDGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKNPDEFRNLLRSDYESVEEYLEKSRMRYDGTWATDVEIFA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 291226516  411 AADLLRTDIYTFTRD--KWLKYSNHQIHNNALNSGKAIYLKHCLNIHYEFV 459
Cdd:cd22755    81 AATLLGVDIYVYSKGgyKWLLYSPRFKLGKRNGSREAIYLKNTNGNHFEPV 131
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 1689-2107 1.80e-47

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 179.40  E-value: 1.80e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1689 HMFLSGGAGTGKSHLIKAIyyeaSRILAHTVPRpddisVLLTAPTGVAA------FNIDALTIHSTFAiavdaklpYQPL 1762
Cdd:COG0507   142 VSVLTGGAGTGKTTTLRAL----LAALEALGLR-----VALAAPTGKAAkrlsesTGIEARTIHRLLG--------LRPD 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1763 GEEKINTIRSKLANLQILIIDEISMVDKRLLVYVhgrLRQIkqtgdysPFGNVSVIAVGDFYQLAPVKGKALFVenqgiD 1842
Cdd:COG0507   205 SGRFRHNRDNPLTPADLLVVDEASMVDTRLMAAL---LEAL-------PRAGARLILVGDPDQLPSVGAGAVLR-----D 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1843 LWND-YFSIAELTHIVRQ-QDSKFAETLNNIRtRQKSDEMLT---SDVNMLRCRETGEECDGIY---------------I 1902
Cdd:COG0507   270 LIESgTVPVVELTEVYRQaDDSRIIELAHAIR-EGDAPEALNaryADVVFVEAEDAEEAAEAIVelyadrpaggediqvL 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1903 FATNKEVDKCNVEklhslcsdpicIRAQdFSRNHKSKKLERKDtlyvkvyntnlaKTVTLAVGARVMLIKNiDVSDGLVN 1982
Cdd:COG0507   349 APTNAGVDALNQA-----------IREA-LNPAGELERELAED------------GELELYVGDRVMFTRN-DYDLGVFN 403

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1983 GVFGTVSYISLNPGeifpsKIFVVFDNKKVgIKLrsqseSFSSLPEnstqinpqedrvnngggirrqfpLKLAWACTVHK 2062
Cdd:COG0507   404 GDIGTVLSIDEDEG-----RLTVRFDGREI-VTY-----DPSELDQ-----------------------LELAYAITVHK 449

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 291226516 2063 VQGLTVEKATVSLGK----IFSPGQAYVALSRVKTLNGLVI-KEFKESAL 2107
Cdd:COG0507   450 SQGSTFDRVILVLPSehspLLSRELLYTALTRARELLTLVGdRDALARAV 499
DEXSc_Pif1_like cd18037
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ...
 1690-1858 2.58e-36

DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like helicases involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. The members of Pif1 helicase subfamily studied so far all appear to contribute to telomere maintenance. Pif1 is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350795 [Multi-domain]  Cd Length: 183  Bit Score: 136.61  E-value: 2.58e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1690 MFLSGGAGTGKSHLIKAIyyeasrilaHTVPRPDDISVLLTAPTGVAAFNIDALTIHSTFAIAVDAKLPYQPLGEEKI-N 1768
Cdd:cd18037    15 VFFTGSAGTGKSYLLRRI---------IRALPSRPKRVAVTASTGIAACNIGGTTLHSFAGIGLGSEPAEDLLERVKRsP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1769 TIRSKLANLQILIIDEISMVDKRLLVYVHGRLRQIKqtGDYSPFGNVSVIAVGDFYQLAPVKGKALFVENQGIDLWNDYF 1848
Cdd:cd18037    86 YLVQRWRKCDVLIIDEISMLDADLFDKLDRVAREVR--GSDKPFGGIQLILCGDFLQLPPVTKNSERQAFFFRGDQQFCF 163

                         170       180
                  ....*....|....*....|
gi 291226516 1849 S----------IAELTHIVR 1858
Cdd:cd18037   164 EakswerciflTVELTKVFR 183
Helitron_like_N pfam14214
Helitron helicase-like domain at N-terminus; This family is found in Helitrons, recently ...
 921-1115 1.37e-35

Helitron helicase-like domain at N-terminus; This family is found in Helitrons, recently recognized eukaryotic transposons that are predicted to amplify by a rolling-circle mechanism. In many instances a protein-coding gene is disrupted by their insertion.


Pssm-ID: 464105  Cd Length: 199  Bit Score: 135.10  E-value: 1.37e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516   921 RLMNADGRFARNTDFIFYAQYLSEVQQVVSNVSIALRKGSTKSCSKTITASTLIDtqSLKDILKNDEGYK-------FMK 993
Cdd:pfam14214    4 RLQHHDGRFARHPRFLFVAFNLFQQARAESRRLSFIRVNQKELRAESYTGERLRD--ALEEETDDPEVLAllgsiviLPS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516   994 PIRGTPPFWQSAQKDLFAMLRQLGIPTWFCSFSSADMrWPEmiesILNERGDYCKTEELDWSEK-CAILRNNPVTAARMF 1072
Cdd:pfam14214   82 SVPGSPRYMLQLRQDAMAIVRRLGKPDLFITFTPNDL-WPE----IKRELARYREWKLPGAQTRlRRLASDRPDIVARVF 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 291226516  1073 EHRFHCFLKRVILSPAEPIGKIEDYFYRVEFQQRGSPHTHCLF 1115
Cdd:pfam14214  157 HRKLELFLKDLLRFKEGVFGNVSAYVYTVEFQKRGLPHAHGLL 199
PIF1 pfam05970
PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits ...
 1661-1988 1.91e-27

PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits telomerase activity and is cell cycle regulated. This family includes a large number of largely uncharacterized plant proteins. This family includes a P-loop motif that is involved in nucleotide binding.


Pssm-ID: 428699 [Multi-domain]  Cd Length: 361  Bit Score: 116.33  E-value: 1.91e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  1661 LNDRQCDIFYTVRKWCLSKCNGIhvepfhMFLSGGAGTGKSHLIKAIYyeasrilahTVPRPDDISVLLTAPTGVAAFNI 1740
Cdd:pfam05970    1 LNDEQKKVFDAIIESVINNKGGV------FFVYGYGGTGKTFLWKAII---------TSLRSEGKIVLAVASSGVAALLL 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  1741 D-ALTIHSTFAIAVDaklpyqpLGEEKINTIR--SKLANL----QILIIDEISMVDKRLLVYVHGRLRQIKQTGDYSPFG 1813
Cdd:pfam05970   66 PgGRTAHSRFGIPLD-------IDELSTCKIKrgSKLAELlektSLIVWDEAPMTHRHCFEALDRTLRDILSETDDKPFG 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  1814 NVSVIAVGDFYQLAPV--KGKALFVENQGID---LWNdYFSIAELTHIVRQQDS-----------KFAETLNNIR----- 1872
Cdd:pfam05970  139 GKTVVLGGDFRQILPVipKGSRPEIVNASITnsyLWK-HVKVLELTKNMRLLADsldqteakelqDFSDWLLAIGdgkin 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  1873 --TRQKSDEMLTSDVNMLRCRETGEE-------------CDGIY-----IFA-TNKEVDKCN---VEKLHS-----LCSD 1923
Cdd:pfam05970  218 deNEREQLIDIPIDILLNTGGDPIEAivsevypdilqnsTDPNYleeraILCpTNEDVDEINnyrLSQLPGeekeyLSSD 297

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291226516  1924 PICiraqDFSRNHKSKKLerkdtlyvkvYNTNLAKTVT----------LAVGARVMLIKNIDVSDGLVNGVFGTV 1988
Cdd:pfam05970  298 SIS----KSDNDSEIDAL----------YPTEFLNSLNanglpnhvlkLKVGAPVMLLRNLDQSRGLCNGTRLIV 358
DUF6570 pfam20209
Domain of unknown function (DUF6570); This entry represents a presumed domain of unknown ...
 677-815 5.40e-19

Domain of unknown function (DUF6570); This entry represents a presumed domain of unknown function that is found in a wide range of proteins that includes eukaryotic transposon protein.


Pssm-ID: 466360  Cd Length: 134  Bit Score: 85.08  E-value: 5.40e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516   677 KGRMPAEASVNNLHLQRIPQKLNCLNSLEQHLIGLHIPFMKMLAL--PKGGQNGVHGPVVCVPSSIDKtTSILPRSgPDD 754
Cdd:pfam20209    1 RGKLPKFSLANGLWIGEVPEELQDLTFVEELLIARVRPRVYVVKLrpKSGGQRGLRGNVIAFPQDVGK-LSVLPRP-PED 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291226516   755 --QMIQVKLKR-KLTYKGHYQYQF-VNDSHIKNALRYLKMNNKWYNNVEyntdwtnplsrIDEEN 815
Cdd:pfam20209   79 ldDVIAVLFIGpKKPTKEWLKKPFrVRRAKVRAALRWLKANNPLYRDIE-----------IDEEN 132
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 2140-2299 6.34e-07

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 51.84  E-value: 6.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  2140 MLHNIEGLYSHIEDLKFDKRFL-------KADIICLTETWLPNANPPSVLQLDNFRFHHqprslCYDTSDKltaelkeQA 2212
Cdd:pfam03372    1 LTWNVNGGNADAAGDDRKLDALaalirayDPDVVALQETDDDDASRLLLALLAYGGFLS-----YGGPGGG-------GG 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  2213 HGGVGVYYSF-------HRCIEFLDLSIS--NLEYLAFHVNDANMKVAVVYRPRSYKADVFRRNLLTLATEMDKIPGGTI 2283
Cdd:pfam03372   69 GGGVAILSRYplssvilVDLGEFGDPALRgaIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVI 148

                          170
                   ....*....|....*..
gi 291226516  2284 IMGDFNE-NLFVSSSVR 2299
Cdd:pfam03372  149 LAGDFNAdYILVSGGLT 165
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
 1691-1829 1.12e-06

exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha subunit, RecD. RecD is part of a RecBCD complex. A related family in the Gram-positive bacteria separates in a phylogenetic tree, has an additional N-terminal extension of about 200 residues, and is not supported as a member of a RecBCD complex by neighboring genes. The related family is consequently described by a different model. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273631 [Multi-domain]  Cd Length: 582  Bit Score: 54.00  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  1691 FLSGGAGTGKSHLIKAIYyeasRILAHTVPRPDDISVLLTAPTGVAA----------FNIDALTIHSTFAIAVDAKLPYQ 1760
Cdd:TIGR01447  163 LITGGPGTGKTTTVARLL----LALVKQSPKQGKLRIALAAPTGKAAarlaeslrkaVKNLAAAEALIAALPSEAVTIHR 238

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291226516  1761 PLGEEKINT----IRSKLANLQILIIDEISMVDKRLLvyvHGRLRQIKqtgdyspfGNVSVIAVGDFYQLAPV 1829
Cdd:TIGR01447  239 LLGIKPDTKrfrhHERNPLPLDVLVVDEASMVDLPLM---AKLLKALP--------PNTKLILLGDKNQLPSV 300
Herpes_teg_N pfam04843
Herpesvirus tegument protein, N-terminal conserved region;
68-213 3.13e-06

Herpesvirus tegument protein, N-terminal conserved region;


Pssm-ID: 461453 [Multi-domain]  Cd Length: 183  Bit Score: 49.81  E-value: 3.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516    68 SFHQGDPQFLNNSGRQCVANA---LVSVIFSNIKDICSWDKydLDTILRSGNELYGYLQNSTTI-NHELLLVTELPQIL- 142
Cdd:pfam04843    1 SRNQFDCKFGPRAGSQCLSNCvsfLHSSYLNGINPVLSREA--LDAVLEEGARLDTLLRTSGRLpPRQYAQLHEIPGIIi 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516   143 ------------DIF-DTQFTLSigEPLFGIIGKVAVETDFFMSFDNALNVSLREYNACFVIFGGAAFAVIKKDSIYWVF 209
Cdd:pfam04843   79 tgawgcliyrssEIYgLLGHELS--RNFNGTPQTGDIDTQMPAGIFFRYAKAKRRPSYTLIICNSLAMAIVIKDKTYYLF 156


                   ....
gi 291226516   210 DSHS 213
Cdd:pfam04843  157 DPHC 160
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 1689-1820 8.49e-05

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 45.06  E-value: 8.49e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516   1689 HMFLSGGAGTGKSHLIKAIYYEAsrilahtvpRPDDISVLLTAPTGVAAFNIDALTIHSTFAIavdaklPYQPLGEEKIN 1768
Cdd:smart00382    4 VILIVGPPGSGKTTLARALAREL---------GPPGGGVIYIDGEDILEEVLDQLLLIIVGGK------KASGSGELRLR 68

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 291226516   1769 TIRSKLANLQ--ILIIDEISMVDKRLLVYVHGRLRQIKQTGDYSPFGNVSVIAV 1820
Cdd:smart00382   69 LALALARKLKpdVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILT 122
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 339-455 2.87e-04

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: 42.82  E-value: 2.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516   339 DGNCFFRALSYAL-----SGTENNHRKIRLAIVKHLKDNPTAFRSCLRSDYDsvENYLLASRMKYlttWATEVEILAAAD 413
Cdd:pfam02338    3 DGNCLYRSISHQLwgvhdVLRKMLVQELRETLAEYMREHKEEFEPFLEDDET--GDIIEIEQTGA---WGGEIEIFALAH 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 291226516   414 LLRTDIYTFTRDKWLKYSNHQIHNNALNSGKAIYLKHCLNIH 455
Cdd:pfam02338   78 ILRRPIIVYKSEGGEELGGLKEYGIYLPLGWDPSLCLVYPRH 119
 
Name Accession Description Interval E-value
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
 331-459 4.67e-58

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: 196.71  E-value: 4.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  331 CKTKTIKEDGNCFFRALSYALSGTENNHRKIRLAIVKHLKDNPTAFRSCLRSDYDSVENYLLASRMKYLTTWATEVEILA 410
Cdd:cd22755     1 CKTIKIVGDGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKNPDEFRNLLRSDYESVEEYLEKSRMRYDGTWATDVEIFA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 291226516  411 AADLLRTDIYTFTRD--KWLKYSNHQIHNNALNSGKAIYLKHCLNIHYEFV 459
Cdd:cd22755    81 AATLLGVDIYVYSKGgyKWLLYSPRFKLGKRNGSREAIYLKNTNGNHFEPV 131
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 1689-2107 1.80e-47

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 179.40  E-value: 1.80e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1689 HMFLSGGAGTGKSHLIKAIyyeaSRILAHTVPRpddisVLLTAPTGVAA------FNIDALTIHSTFAiavdaklpYQPL 1762
Cdd:COG0507   142 VSVLTGGAGTGKTTTLRAL----LAALEALGLR-----VALAAPTGKAAkrlsesTGIEARTIHRLLG--------LRPD 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1763 GEEKINTIRSKLANLQILIIDEISMVDKRLLVYVhgrLRQIkqtgdysPFGNVSVIAVGDFYQLAPVKGKALFVenqgiD 1842
Cdd:COG0507   205 SGRFRHNRDNPLTPADLLVVDEASMVDTRLMAAL---LEAL-------PRAGARLILVGDPDQLPSVGAGAVLR-----D 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1843 LWND-YFSIAELTHIVRQ-QDSKFAETLNNIRtRQKSDEMLT---SDVNMLRCRETGEECDGIY---------------I 1902
Cdd:COG0507   270 LIESgTVPVVELTEVYRQaDDSRIIELAHAIR-EGDAPEALNaryADVVFVEAEDAEEAAEAIVelyadrpaggediqvL 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1903 FATNKEVDKCNVEklhslcsdpicIRAQdFSRNHKSKKLERKDtlyvkvyntnlaKTVTLAVGARVMLIKNiDVSDGLVN 1982
Cdd:COG0507   349 APTNAGVDALNQA-----------IREA-LNPAGELERELAED------------GELELYVGDRVMFTRN-DYDLGVFN 403

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1983 GVFGTVSYISLNPGeifpsKIFVVFDNKKVgIKLrsqseSFSSLPEnstqinpqedrvnngggirrqfpLKLAWACTVHK 2062
Cdd:COG0507   404 GDIGTVLSIDEDEG-----RLTVRFDGREI-VTY-----DPSELDQ-----------------------LELAYAITVHK 449

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 291226516 2063 VQGLTVEKATVSLGK----IFSPGQAYVALSRVKTLNGLVI-KEFKESAL 2107
Cdd:COG0507   450 SQGSTFDRVILVLPSehspLLSRELLYTALTRARELLTLVGdRDALARAV 499
DEXSc_Pif1_like cd18037
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ...
 1690-1858 2.58e-36

DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like helicases involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. The members of Pif1 helicase subfamily studied so far all appear to contribute to telomere maintenance. Pif1 is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350795 [Multi-domain]  Cd Length: 183  Bit Score: 136.61  E-value: 2.58e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1690 MFLSGGAGTGKSHLIKAIyyeasrilaHTVPRPDDISVLLTAPTGVAAFNIDALTIHSTFAIAVDAKLPYQPLGEEKI-N 1768
Cdd:cd18037    15 VFFTGSAGTGKSYLLRRI---------IRALPSRPKRVAVTASTGIAACNIGGTTLHSFAGIGLGSEPAEDLLERVKRsP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1769 TIRSKLANLQILIIDEISMVDKRLLVYVHGRLRQIKqtGDYSPFGNVSVIAVGDFYQLAPVKGKALFVENQGIDLWNDYF 1848
Cdd:cd18037    86 YLVQRWRKCDVLIIDEISMLDADLFDKLDRVAREVR--GSDKPFGGIQLILCGDFLQLPPVTKNSERQAFFFRGDQQFCF 163

                         170       180
                  ....*....|....*....|
gi 291226516 1849 S----------IAELTHIVR 1858
Cdd:cd18037   164 EakswerciflTVELTKVFR 183
Helitron_like_N pfam14214
Helitron helicase-like domain at N-terminus; This family is found in Helitrons, recently ...
 921-1115 1.37e-35

Helitron helicase-like domain at N-terminus; This family is found in Helitrons, recently recognized eukaryotic transposons that are predicted to amplify by a rolling-circle mechanism. In many instances a protein-coding gene is disrupted by their insertion.


Pssm-ID: 464105  Cd Length: 199  Bit Score: 135.10  E-value: 1.37e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516   921 RLMNADGRFARNTDFIFYAQYLSEVQQVVSNVSIALRKGSTKSCSKTITASTLIDtqSLKDILKNDEGYK-------FMK 993
Cdd:pfam14214    4 RLQHHDGRFARHPRFLFVAFNLFQQARAESRRLSFIRVNQKELRAESYTGERLRD--ALEEETDDPEVLAllgsiviLPS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516   994 PIRGTPPFWQSAQKDLFAMLRQLGIPTWFCSFSSADMrWPEmiesILNERGDYCKTEELDWSEK-CAILRNNPVTAARMF 1072
Cdd:pfam14214   82 SVPGSPRYMLQLRQDAMAIVRRLGKPDLFITFTPNDL-WPE----IKRELARYREWKLPGAQTRlRRLASDRPDIVARVF 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 291226516  1073 EHRFHCFLKRVILSPAEPIGKIEDYFYRVEFQQRGSPHTHCLF 1115
Cdd:pfam14214  157 HRKLELFLKDLLRFKEGVFGNVSAYVYTVEFQKRGLPHAHGLL 199
PIF1 pfam05970
PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits ...
 1661-1988 1.91e-27

PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits telomerase activity and is cell cycle regulated. This family includes a large number of largely uncharacterized plant proteins. This family includes a P-loop motif that is involved in nucleotide binding.


Pssm-ID: 428699 [Multi-domain]  Cd Length: 361  Bit Score: 116.33  E-value: 1.91e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  1661 LNDRQCDIFYTVRKWCLSKCNGIhvepfhMFLSGGAGTGKSHLIKAIYyeasrilahTVPRPDDISVLLTAPTGVAAFNI 1740
Cdd:pfam05970    1 LNDEQKKVFDAIIESVINNKGGV------FFVYGYGGTGKTFLWKAII---------TSLRSEGKIVLAVASSGVAALLL 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  1741 D-ALTIHSTFAIAVDaklpyqpLGEEKINTIR--SKLANL----QILIIDEISMVDKRLLVYVHGRLRQIKQTGDYSPFG 1813
Cdd:pfam05970   66 PgGRTAHSRFGIPLD-------IDELSTCKIKrgSKLAELlektSLIVWDEAPMTHRHCFEALDRTLRDILSETDDKPFG 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  1814 NVSVIAVGDFYQLAPV--KGKALFVENQGID---LWNdYFSIAELTHIVRQQDS-----------KFAETLNNIR----- 1872
Cdd:pfam05970  139 GKTVVLGGDFRQILPVipKGSRPEIVNASITnsyLWK-HVKVLELTKNMRLLADsldqteakelqDFSDWLLAIGdgkin 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  1873 --TRQKSDEMLTSDVNMLRCRETGEE-------------CDGIY-----IFA-TNKEVDKCN---VEKLHS-----LCSD 1923
Cdd:pfam05970  218 deNEREQLIDIPIDILLNTGGDPIEAivsevypdilqnsTDPNYleeraILCpTNEDVDEINnyrLSQLPGeekeyLSSD 297

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291226516  1924 PICiraqDFSRNHKSKKLerkdtlyvkvYNTNLAKTVT----------LAVGARVMLIKNIDVSDGLVNGVFGTV 1988
Cdd:pfam05970  298 SIS----KSDNDSEIDAL----------YPTEFLNSLNanglpnhvlkLKVGAPVMLLRNLDQSRGLCNGTRLIV 358
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
 332-459 3.54e-27

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: 108.29  E-value: 3.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  332 KTKTIKEDGNCFFRALSYALSGTENNHRKIRLAIVKHLKDNPTAFRSCL---RSDYDSVENYLlaSRMKYLTTWATEVEI 408
Cdd:cd22744     1 RVVDVPGDGNCLFRALAHALYGDQESHRELRQEVVDYLRENPDLYEPAEladEDDGEDFDEYL--QRMRKPGTWGGELEL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 291226516  409 LAAADLLRTDIYTFTRDKWlKYSNHQIHNNALNSGKAIYLKHCLNIHYEFV 459
Cdd:cd22744    79 QALANALNVPIVVYSEDGG-FLPVSVFGPGPGPSGRPIHLLYTGGNHYDAL 128
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 1690-1857 3.86e-20

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 89.15  E-value: 3.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1690 MFLSGGAGTGKSHLIKAI--YYEASRilahtvprpddISVLLTAPTGVAA------FNIDALTIHSTFAIAVDAKLPYQP 1761
Cdd:cd17933    15 SVLTGGAGTGKTTTLKALlaALEAEG-----------KRVVLAAPTGKAAkrlsesTGIEASTIHRLLGINPGGGGFYYN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1762 lgeekintiRSKLANLQILIIDEISMVDKRLLvyvHGRLRQIKqtgdyspfGNVSVIAVGDFYQLAPV-KGKALfvenqG 1840
Cdd:cd17933    84 ---------EENPLDADLLIVDEASMVDTRLM---AALLSAIP--------AGARLILVGDPDQLPSVgAGNVL-----R 138

                         170
                  ....*....|....*..
gi 291226516 1841 IDLWNDYFSIAELTHIV 1857
Cdd:cd17933   139 DLIASKGVPTVELTEVF 155
OTU_232R-like cd22758
OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase ...
 339-456 1.08e-19

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: 87.32  E-value: 1.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  339 DGNCFFRALSYALSGT--ENNHRKIRLAIVKHLKDNPT---AFRSCLRSDYDSVENYLlaSRMKYLTTWATEVEILAAAD 413
Cdd:cd22758    14 DGNCFFHAVSDQLYGNgiEHSHKELRQQAVNYLRENPElydGFFLSEFDEEESWEEYL--NRMSKDGTWGDHIILQAAAN 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 291226516  414 LLRTDIYTFTRDKWlkYSNHQIHNNALNSGKAIYLKHCLNIHY 456
Cdd:cd22758    92 LFNVRIVIISSDGS--DETTIIEPGNSKNGRTIYLGHIGENHY 132
DUF6570 pfam20209
Domain of unknown function (DUF6570); This entry represents a presumed domain of unknown ...
 677-815 5.40e-19

Domain of unknown function (DUF6570); This entry represents a presumed domain of unknown function that is found in a wide range of proteins that includes eukaryotic transposon protein.


Pssm-ID: 466360  Cd Length: 134  Bit Score: 85.08  E-value: 5.40e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516   677 KGRMPAEASVNNLHLQRIPQKLNCLNSLEQHLIGLHIPFMKMLAL--PKGGQNGVHGPVVCVPSSIDKtTSILPRSgPDD 754
Cdd:pfam20209    1 RGKLPKFSLANGLWIGEVPEELQDLTFVEELLIARVRPRVYVVKLrpKSGGQRGLRGNVIAFPQDVGK-LSVLPRP-PED 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291226516   755 --QMIQVKLKR-KLTYKGHYQYQF-VNDSHIKNALRYLKMNNKWYNNVEyntdwtnplsrIDEEN 815
Cdd:pfam20209   79 ldDVIAVLFIGpKKPTKEWLKKPFrVRRAKVRAALRWLKANNPLYRDIE-----------IDEEN 132
OTU_plant_OTU7-like cd22771
OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar ...
 331-456 5.95e-18

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: 81.83  E-value: 5.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  331 CKTKTIKEDGNCFFRALSYALSGTENNHRKIRLAIVKHLKDNPTAFRSCLrSDYDSVENYLlaSRMKYLTTWATEVEILA 410
Cdd:cd22771     2 LRIRDVEGDGNCLFRALADQLYGDEERHAELRKKVVDYMEAHEEDFEPFF-EDDETFEDYV--SRMREDGTWGGNLELQA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 291226516  411 AADLLRTDI--YTFTRDKWlkysnhQIHNNALNSGKAIYLKHCLNIHY 456
Cdd:cd22771    79 ASLVYRVNIvvHQLGQPRW------EIENFPDKGARTIHLSYHDGEHY 120
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 1690-1873 6.78e-18

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.


Pssm-ID: 433343 [Multi-domain]  Cd Length: 191  Bit Score: 83.77  E-value: 6.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  1690 MFLSGGAGTGKSHLIKAIyyeasRILAHTVPRPddisVLLTAPTGVAA------FNIDALTIHstfaiavdaKLPYQplg 1763
Cdd:pfam13604   21 AVLVGPAGTGKTTALKAL-----REAWEAAGYR----VIGLAPTGRAAkvlgeeLGIPADTIA---------KLLHR--- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  1764 eekiNTIRSKLANLQILIIDEISMVDKRLLVYVhgrLRQIKQTGDyspfgnvSVIAVGDFYQLAPVKGKALFVenqgiDL 1843
Cdd:pfam13604   80 ----LGGRAGLDPGTLLIVDEAGMVGTRQMARL---LKLAEDAGA-------RVILVGDPRQLPSVEAGGAFR-----DL 140

                          170       180       190
                   ....*....|....*....|....*....|
gi 291226516  1844 WNDYFSIAELTHIVRQQDSKFAETLNNIRT 1873
Cdd:pfam13604  141 LAAGIGTAELTEIVRQRDPWQRAASLALRD 170
OTU_P87_VP80-like cd22757
OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The ...
 336-422 7.14e-17

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: 78.78  E-value: 7.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  336 IKEDGNCFFRALSYALSGTENNHRKIRLAIVKHLKDN-----PTAFRSCLRSdYDSVENYllASRMKYLTTWATEVEILA 410
Cdd:cd22757     6 IPGDGACLFRALSYLLYGTQSRHLEVRKEVVDYVVNNwdefsIYTHDSEGNN-YKSAEEY--RADMSKPGTYGTLCELVA 82

                          90
                  ....*....|..
gi 291226516  411 AADLLRTDIYTF 422
Cdd:cd22757    83 AAELYPFHFEVY 94
OTU_OTUD3-like cd22756
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This ...
 332-425 1.97e-16

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: 77.60  E-value: 1.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  332 KTKTIKEDGNCFFRALSYALSGTENNHRKIRLAIVKHLKDNPTAFRSCLRSDYD-----SVENYLlaSRMKYLTTWATEV 406
Cdd:cd22756     1 YAKDITGDGNCLFRALSDQLYGDPDRHLEIRAEVVEYMRANPDDFKPFSEAATFaeddeAFEDYL--ARMAKDGTYGDNL 78

                          90
                  ....*....|....*....
gi 291226516  407 EILAAADLLRTDIYTFTRD 425
Cdd:cd22756    79 EIVAFARAYNVDVKVYQPD 97
OTU_plant_OTU9-like cd22751
OTU (ovarian tumor) domain of plant deubiquitinating enzyme OTU9 and similar proteins; This ...
 336-456 3.77e-15

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: 74.11  E-value: 3.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  336 IKEDGNCFFRALSYALSGTENNHRKIRLAIVKHLKDNPTA-FRSCLRSDYDsveNYLlaSRMKYLTTWATEVEILAAADL 414
Cdd:cd22751    15 VEGDGNCQFRALSDQLFGTQDHHAEVRELVVKQLRAHPELyYEFYVPEEYD---EYL--KKMSKDGEWGDELTLQAAADA 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 291226516  415 LRTDIY--TFTRDKW-LKYsnhqIHNNALNSGKAIYLKHCLNIHY 456
Cdd:cd22751    90 FGVKIHviTSFEDNWfLEI----EPRGLVRSKRVLFLSYWAEVHY 130
AAA_19 pfam13245
AAA domain;
1689-1829 2.18e-12

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 66.47  E-value: 2.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  1689 HMFLSGGAGTGKSHLIKAIYyeASRILAHTVPRPddisVLLTAPTGVAAFNI------DALTIHStfAIAVDAKLPYQPL 1762
Cdd:pfam13245   13 VVLLTGGPGTGKTTTIRHIV--ALLVALGGVSFP----ILLAAPTGRAAKRLsertglPASTIHR--LLGFDDLEAGGFL 84

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291226516  1763 GEEkintirSKLANLQILIIDEISMVD----KRLlvyvhgrLRQIKQtgdyspfgNVSVIAVGDFYQLAPV 1829
Cdd:pfam13245   85 RDE------EEPLDGDLLIVDEFSMVDlplaYRL-------LKALPD--------GAQLLLVGDPDQLPSV 134
SF1_C_RecD cd18809
C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11. ...
 2053-2099 9.90e-12

C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD family helicases are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350196 [Multi-domain]  Cd Length: 80  Bit Score: 62.58  E-value: 9.90e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 291226516 2053 KLAWACTVHKVQGLTVEKATVSLGKI---FSPGQAYVALSRVKTLNGLVI 2099
Cdd:cd18809    31 LQAYAMTIHKSQGSEFDRVIVVLPTShpmLSRGLLYTALTRARKLLTLVG 80
OTU_ALG13-like cd22753
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 334-459 5.62e-10

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: 59.09  E-value: 5.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  334 KTIKEDGNCFFRALSYALSGTENNHRKIRLAIVKHLKDNPTAFRscLRSDYdSVENYLlaSRMKYLTTWATEVEILAAAD 413
Cdd:cd22753    13 KHIPRDGSCLFRAVSEQLFFTQSYHQQVRQACVEYLEKNREEFE--KFSEI-SFDDYL--ERLSDPKEWGGLLELEALSL 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 291226516  414 LLRTDIYTFtrdkwlkYSNHQIHNNALNSG--KAIYLKHCLNIHYEFV 459
Cdd:cd22753    88 LYKVDFIVY-------SIPDQPPSNITNNGypKKIMLCYSGGNHYDSV 128
OTU_OTUD1 cd22747
OTU (ovarian tumor) domain of OTU domain-containing protein 1 and similar proteins; OTU ...
 336-423 2.76e-08

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: 55.20  E-value: 2.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  336 IKEDGNCFFRALSYALSGTENNHRKIRLAIVKHLKDNPTAFRSCLRSDydsVENYLLASRMKylTTWATEVEILAAADLL 415
Cdd:cd22747    26 IIPDGNCLYRAVSKAVYGDQALHRELREQTVHYIADHLDEFNPIIEGD---VGEFLIKAAQD--GAWAGYPELLAMGQML 100


                  ....*...
gi 291226516  416 RTDIYTFT 423
Cdd:cd22747   101 NVNIRLTT 108
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
 334-420 1.10e-07

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: 52.76  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  334 KTIKEDGNCFFRALSYALSGTENNHRKIRLAIVKHLKDNPTAFRSCLRSDYDsveNYLlaSRMKYLTTWATEVEILAAAD 413
Cdd:cd22794    13 KQIAKDGSCLFRAVAEQVFHTQSRHLEVRKACVDYLRRNREKFEAFIEGPFE---QYL--KNLENPKEWAGQVEISALSL 87


                  ....*....
gi 291226516  414 LLRTD--IY 420
Cdd:cd22794    88 MYKRDfiIY 96
OTU_VRTN cd22791
OTU (ovarian tumor) domain of vertnin and similar proteins; Vertnin (VRTN) is an OTU ...
 329-421 1.17e-07

OTU (ovarian tumor) domain of vertnin and similar proteins; Vertnin (VRTN) is an OTU domain-containing protein that is required for the development of thoracic vertebrae in mammals. 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. Vertnin and some subfamily members do not possess the conserved catalytic residues and may not have DUB activity. VRTN gene is associated with variations in vertebral number.


Pssm-ID: 438612  Cd Length: 137  Bit Score: 52.99  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  329 EPCKTKTikeDGNCFFRALSYALSGTENNHRKIRLAIVKHLkdnptafrsCLRSDY--DSVENYLLASRMKYltTWATEV 406
Cdd:cd22791     2 EPLRVTG---DGNCLFRAASLLLFGDESLHLELRLRTVLEL---------VLNSEFyeAIYEAEIKATCKPG--SYSGIW 67

                          90
                  ....*....|....*
gi 291226516  407 EILAAADLLRTDIYT 421
Cdd:cd22791    68 HIYALSSVLQRPIFS 82
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
 2047-2099 6.28e-07

C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Similar to SF2 helicases, they do not form toroidal, predominantly hexameric structures like SF3-6. SF1 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350173 [Multi-domain]  Cd Length: 89  Bit Score: 49.36  E-value: 6.28e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 291226516 2047 RRQFPLKLAWACTVHKVQGLTVEKATVSL--GKIFSPGQAYVALSRVKTlnGLVI 2099
Cdd:cd18786    35 LDEFDLQLVGAITIDSSQGLTFDVVTLYLptANSLTPRRLYVALTRARK--RLVI 87
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 2140-2299 6.34e-07

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 51.84  E-value: 6.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  2140 MLHNIEGLYSHIEDLKFDKRFL-------KADIICLTETWLPNANPPSVLQLDNFRFHHqprslCYDTSDKltaelkeQA 2212
Cdd:pfam03372    1 LTWNVNGGNADAAGDDRKLDALaalirayDPDVVALQETDDDDASRLLLALLAYGGFLS-----YGGPGGG-------GG 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  2213 HGGVGVYYSF-------HRCIEFLDLSIS--NLEYLAFHVNDANMKVAVVYRPRSYKADVFRRNLLTLATEMDKIPGGTI 2283
Cdd:pfam03372   69 GGGVAILSRYplssvilVDLGEFGDPALRgaIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVI 148

                          170
                   ....*....|....*..
gi 291226516  2284 IMGDFNE-NLFVSSSVR 2299
Cdd:pfam03372  149 LAGDFNAdYILVSGGLT 165
OTU_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
 321-420 8.80e-07

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: 50.64  E-value: 8.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  321 SRLNMEMgepcktKTIKEDGNCFFRALSYAL-----SGTENNHRKIRLAIVKHLKDNPTAFRSCLRSD------YDSVEN 389
Cdd:cd22748     2 KPLGLRI------KEIPPDGHCLYRAIADQLklrggSEEPYSYKELRKLAADYMRAHRDDFLPFLTNDdgdlmtEEEFEE 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 291226516  390 YllASRMKYLTTWATEVEILAAADLLRTDIY 420
Cdd:cd22748    76 Y--CDKIENTAEWGGQLELRALSKALKRPIH 104
OTU_OTUD5-like cd22752
OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU ...
 334-456 9.43e-07

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: 49.85  E-value: 9.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  334 KTIKEDGNCFFRALSYALSGTENNHRKIRLAIVKHLKDNPTAFrsclrSDY--DSVENYLlaSRMKYLTTWATEVEILAA 411
Cdd:cd22752     5 KEMEEDGNCLFRAVADQVYGDQEMHDVVRKHCMDYMEKNRDYF-----SQFvtEDFEEYI--NRKRQDGVWGNHIEIQAM 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 291226516  412 ADLLRTDIYTFtrdkwlKYSNHQI---HNNALNSGKAIYLKHCLNIHY 456
Cdd:cd22752    78 SELYNRPIEVY------AYSTEPIntfHEASSSDNEPIRLSYHGNSHY 119
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
 1691-1829 1.12e-06

exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha subunit, RecD. RecD is part of a RecBCD complex. A related family in the Gram-positive bacteria separates in a phylogenetic tree, has an additional N-terminal extension of about 200 residues, and is not supported as a member of a RecBCD complex by neighboring genes. The related family is consequently described by a different model. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273631 [Multi-domain]  Cd Length: 582  Bit Score: 54.00  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  1691 FLSGGAGTGKSHLIKAIYyeasRILAHTVPRPDDISVLLTAPTGVAA----------FNIDALTIHSTFAIAVDAKLPYQ 1760
Cdd:TIGR01447  163 LITGGPGTGKTTTVARLL----LALVKQSPKQGKLRIALAAPTGKAAarlaeslrkaVKNLAAAEALIAALPSEAVTIHR 238

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291226516  1761 PLGEEKINT----IRSKLANLQILIIDEISMVDKRLLvyvHGRLRQIKqtgdyspfGNVSVIAVGDFYQLAPV 1829
Cdd:TIGR01447  239 LLGIKPDTKrfrhHERNPLPLDVLVVDEASMVDLPLM---AKLLKALP--------PNTKLILLGDKNQLPSV 300
OTU_RDRP-like cd22792
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ...
 339-457 1.17e-06

OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; RNA replication polyprotein (RDRP) is a viral homolog of ovarian tumor protease (vOTU), which displays RNA helicase (EC 3.6.4.13), RNA-directed RNA polymerase (EC 2.7.7.48), viral methyltransferase, Fe(2+) 2-oxoglutarate dioxygenase and protease activities. The central part of this protein possibly functions as an ATP-binding helicase. It is an RNA-directed RNA polymerase involved in viral RNA replication. It also acts as a thiol protease that cleaves the polyprotein. 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: 438613 [Multi-domain]  Cd Length: 108  Bit Score: 49.14  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  339 DGNCFFRALSYALSGTennhrkirlaiVKHLKdnptafRSCLRSDYDSVENYLLASRMKYLTTWATEVEILAAADLLRTD 418
Cdd:cd22792     8 DGNCFWHSLGHFLGLS-----------ALELK------KLLRDSLFDDPELDEELDEQLEPGVYAEDEAIAAAAKLFGVN 70

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 291226516  419 IYTFTRDKwlkysnHQIHNNALNSGKAIYLKHCLNIHYE 457
Cdd:cd22792    71 ICVHDPDE------GVLYTFTPNESSKSIHLLLENEHFE 103
Herpes_teg_N pfam04843
Herpesvirus tegument protein, N-terminal conserved region;
68-213 3.13e-06

Herpesvirus tegument protein, N-terminal conserved region;


Pssm-ID: 461453 [Multi-domain]  Cd Length: 183  Bit Score: 49.81  E-value: 3.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516    68 SFHQGDPQFLNNSGRQCVANA---LVSVIFSNIKDICSWDKydLDTILRSGNELYGYLQNSTTI-NHELLLVTELPQIL- 142
Cdd:pfam04843    1 SRNQFDCKFGPRAGSQCLSNCvsfLHSSYLNGINPVLSREA--LDAVLEEGARLDTLLRTSGRLpPRQYAQLHEIPGIIi 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516   143 ------------DIF-DTQFTLSigEPLFGIIGKVAVETDFFMSFDNALNVSLREYNACFVIFGGAAFAVIKKDSIYWVF 209
Cdd:pfam04843   79 tgawgcliyrssEIYgLLGHELS--RNFNGTPQTGDIDTQMPAGIFFRYAKAKRRPSYTLIICNSLAMAIVIKDKTYYLF 156


                   ....
gi 291226516   210 DSHS 213
Cdd:pfam04843  157 DPHC 160
OTU_ALG13 cd22795
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 334-418 2.91e-05

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: 45.96  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  334 KTIKEDGNCFFRALSYALSGTENNHRKIRLAIVKHLKDNPTAFRSCLRSdydSVENYLlaSRMKYLTTWATEVEILAAAD 413
Cdd:cd22795    13 KLTAKDASCLFRAVSEQLFLCQIHHLEIRKACVSYMRANQCNFESYVEG---SFEKYL--ERLEDPKESAGQLEISALSL 87


                  ....*
gi 291226516  414 LLRTD 418
Cdd:cd22795    88 IYNRD 92
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
 339-412 3.86e-05

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: 45.67  E-value: 3.86e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291226516  339 DGNCFFRALSYALSGTENNHRKIRLAIVKHLKDNptaFRSC--LRSDYDSVENYLlaSRMKYLTTWA--TEVEILAAA 412
Cdd:cd21880    30 DGNCFFRSIAELLFDTEDEWRLVKNTIESYARAN---WDECpeARLYYLSLEEYL--RDAMKDGYWGgsLEAEILSKA 102
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 1689-1820 8.49e-05

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 45.06  E-value: 8.49e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516   1689 HMFLSGGAGTGKSHLIKAIYYEAsrilahtvpRPDDISVLLTAPTGVAAFNIDALTIHSTFAIavdaklPYQPLGEEKIN 1768
Cdd:smart00382    4 VILIVGPPGSGKTTLARALAREL---------GPPGGGVIYIDGEDILEEVLDQLLLIIVGGK------KASGSGELRLR 68

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 291226516   1769 TIRSKLANLQ--ILIIDEISMVDKRLLVYVHGRLRQIKQTGDYSPFGNVSVIAV 1820
Cdd:smart00382   69 LALALARKLKpdVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILT 122
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 1687-1820 1.14e-04

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 44.44  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1687 PFHMFLSGGAGTGKSHLIKAIYYEASRilahtvprpddisvlltaptgvAAFNIDALTIHSTFAIAVDAKLPYqpLGEEK 1766
Cdd:cd00009    19 PKNLLLYGPPGTGKTTLARAIANELFR----------------------PGAPFLYLNASDLLEGLVVAELFG--HFLVR 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 291226516 1767 INTIRSKLANLQILIIDEISMVDKRLlvyvHGRLRQIKQTGDYSP--FGNVSVIAV 1820
Cdd:cd00009    75 LLFELAEKAKPGVLFIDEIDSLSRGA----QNALLRVLETLNDLRidRENVRVIGA 126
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 339-455 2.87e-04

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: 42.82  E-value: 2.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516   339 DGNCFFRALSYAL-----SGTENNHRKIRLAIVKHLKDNPTAFRSCLRSDYDsvENYLLASRMKYlttWATEVEILAAAD 413
Cdd:pfam02338    3 DGNCLYRSISHQLwgvhdVLRKMLVQELRETLAEYMREHKEEFEPFLEDDET--GDIIEIEQTGA---WGGEIEIFALAH 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 291226516   414 LLRTDIYTFTRDKWLKYSNHQIHNNALNSGKAIYLKHCLNIH 455
Cdd:pfam02338   78 ILRRPIIVYKSEGGEELGGLKEYGIYLPLGWDPSLCLVYPRH 119
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
1691-1785 1.51e-03

Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 43.26  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516 1691 FLSGGAGTGKSHLIKAIyyeASRILAHtvpRPDDISVLLTAPTGVAAFnIDALTihstfaiavdaklpyqplgEEKINTI 1770
Cdd:COG0593    38 FLYGGVGLGKTHLLHAI---GNEALEN---NPGARVVYLTAEEFTNDF-INAIR-------------------NNTIEEF 91

                          90
                  ....*....|....*
gi 291226516 1771 RSKLANLQILIIDEI 1785
Cdd:COG0593    92 KEKYRSVDVLLIDDI 106
OTU_OTUD3 cd22770
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU ...
 332-372 1.67e-03

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: 41.12  E-value: 1.67e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 291226516  332 KTKTIKEDGNCFFRALSYALSGTENNHRKIRLAIVKHLKDN 372
Cdd:cd22770    15 KLRDIPGDGNCLFRALGDQLEGHSRNHLKHRQETVQYMIEH 55
OTU_fungi_OTU2-like cd22762
OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; ...
 336-419 1.82e-03

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: 40.67  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291226516  336 IKEDGNCFFRA----LSYALSGTENNHRKIRLAIVKHLKDNPTAFRSCLRSDYD---SVENYLlaSRMKYLTTWATEVEI 408
Cdd:cd22762    12 IKPDGHCLFAAiadqLQLRGSEINLDYKELRKLAAEYIRKHPDDFEPFLFEETDeleDIDEYC--KKIENTAEWGGELEL 89

                          90
                  ....*....|.
gi 291226516  409 LAAADLLRTDI 419
Cdd:cd22762    90 LALAKAFGVPI 100
 
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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