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Conserved domains on  [gi|1708930973|ref|XP_029976981|]
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uncharacterized protein LOC115409845 isoform X1 [Salarias fasciatus]

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 ...
 1016-1140 1.29e-59

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: 201.72  E-value: 1.29e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1016 CTTIDIQGDGNCFFRSLSYVFSGLESHHRTVRLAVVKHVEQNPDVYRNVVREQFTSVQQYVNDSRMKYVGTWATEVEIQA 1095
Cdd:cd22755      1 CKTIKIVGDGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKNPDEFRNLLRSDYESVEEYLEKSRMRYDGTWATDVEIFA 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1708930973 1096 AANLFNVDIYTYSEQ--KWLKYGSSGA----AARNKAIYIKHCNECHYEPI 1140
Cdd:cd22755     81 AATLLGVDIYVYSKGgyKWLLYSPRFKlgkrNGSREAIYLKNTNGNHFEPV 131
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 2450-2853 7.70e-46

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: 175.16  E-value: 7.70e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2450 HVFLSGGAGTGKSHLIKALyyeaTRLLARLshnpdAVHVLLTAPTGVAAYN------INATTIHNTFAiptnvslpYQPL 2523
Cdd:COG0507    142 VSVLTGGAGTGKTTTLRAL----LAALEAL-----GLRVALAAPTGKAAKRlsestgIEARTIHRLLG--------LRPD 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2524 KEEKVNTLRAALRDLKILIIDEISMVDHKLLAYIHgrvrqikqsgDFAPFGNVSVIAVGDFYQLPPV-KGKPLYtdqagi 2602
Cdd:COG0507    205 SGRFRHNRDNPLTPADLLVVDEASMVDTRLMAALL----------EALPRAGARLILVGDPDQLPSVgAGAVLR------ 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2603 DLWGS-TFKHVELTEIVRQKNQD-FAVTLNRIRKHKKGDKLNAQD-----------EKLLKQCQTGVGDDTEDLH----I 2665
Cdd:COG0507    269 DLIESgTVPVVELTEVYRQADDSrIIELAHAIREGDAPEALNARYadvvfveaedaEEAAEAIVELYADRPAGGEdiqvL 348

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2666 FATNSDVDAHNfKMLhkvcsdvvqikaqdfeknpQTGRFAQKTTSHAFNKHTHlsalLSIAPNARVMLIKNiDTCDGLVN 2745
Cdd:COG0507    349 APTNAGVDALN-QAI-------------------REALNPAGELERELAEDGE----LELYVGDRVMFTRN-DYDLGVFN 403

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2746 GVLGTVSLIKCDEKTkvpklIYVKFDDDRIgsklrakfpctvpglqnatpVGLDEDKVPYrggirrqfpLRLAWACTIHK 2825
Cdd:COG0507    404 GDIGTVLSIDEDEGR-----LTVRFDGREI--------------------VTYDPSELDQ---------LELAYAITVHK 449

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1708930973 2826 VQGLTLEKAVV----SFKKIFSAGQAYVALSR 2853
Cdd:COG0507    450 SQGSTFDRVILvlpsEHSPLLSRELLYTALTR 481
Helitron_like_N super family cl16715
Helitron helicase-like domain at N-terminus; This family is found in Helitrons, recently ...
 1706-1900 1.02e-31

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.


The actual alignment was detected with superfamily member pfam14214:

Pssm-ID: 464105  Cd Length: 199  Bit Score: 124.31  E-value: 1.02e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1706 RILNADGRFGSNVEYIFYAQYLSEINQVVSNVSIALRkgHHGGE--SSQITSSML-----ASTDFVNNVLRCDMGYKFLK 1778
Cdd:pfam14214    4 RLQHHDGRFARHPRFLFVAFNLFQQARAESRRLSFIR--VNQKElrAESYTGERLrdaleEETDDPEVLALLGSIVILPS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1779 PIRGTPVFWQRVQKDLFAMVKQLGIPTWFCSFSSADLrWTELMQTFMEVQNVQGNVDEMDWsqkCNLLNNNPVTAARMFD 1858
Cdd:pfam14214   82 SVPGSPRYMLQLRQDAMAIVRRLGKPDLFITFTPNDL-WPEIKRELARYREWKLPGAQTRL---RRLASDRPDIVARVFH 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1708930973 1859 HRFRSFLHDVIMSPAQPIGKIIDYFYRVEFQQRGSPHTHCLF 1900
Cdd:pfam14214  158 RKLELFLKDLLRFKEGVFGNVSAYVYTVEFQKRGLPHAHGLL 199
DUF6570 pfam20209
Domain of unknown function (DUF6570); This entry represents a presumed domain of unknown ...
 1470-1595 1.85e-25

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: 103.95  E-value: 1.85e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1470 GKVPDQSVINNLQLDPIPQELNTLNPLEQHLIAPHIPFMKLVAL--PKGGQNGVHGPVTCVPSNTNAVNVLPR-LENQDL 1546
Cdd:pfam20209    2 GKLPKFSLANGLWIGEVPEELQDLTFVEELLIARVRPRVYVVKLrpKSGGQRGLRGNVIAFPQDVGKLSVLPRpPEDLDD 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1708930973 1547 MIRVKLKR-KLSYKGHYEYQY-VNTSKVHSALENLKQNNKWYKDVEINTDW 1595
Cdd:pfam20209   82 VIAVLFIGpKKPTKEWLKKPFrVRRAKVRAALRWLKANNPLYRDIEIDEEN 132
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 72-234 4.59e-10

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


:

Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 61.58  E-value: 4.59e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973   72 ILVVGDShlraLVDGFVQMPEGC----LSFGFMST---------PGASAAQLRTEVEHAVLPQIPEAVCLLAPGNDLTAS 138
Cdd:COG2755     11 IVALGDS----ITAGYGASRERGwpalLARRLAAAdvrvvnagiSGATTADLLARLDRDLLALKPDLVVIELGTNDLLRG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  139 Q--TIEEAAKEFRRLLYSICKRWPN--VCVLD-FPRRLTMTM-DHQKLLSQEYHRVAARMGIRYLDTDSHFPTCHR--EL 210
Cdd:COG2755     87 LgvSPEEFRANLEALIDRLRAAGPGarVVLVTpPPRLRPNYLnERIEAYNAAIRELAAEYGVPLVDLYAALRDAGDlpDL 166

                          170       180
                   ....*....|....*....|....
gi 1708930973  211 WCSDGVHLSDsDGMPILSQLLWTA 234
Cdd:COG2755    167 LTADGLHPNA-AGYRLIAEAVLPA 189
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 2904-3059 5.35e-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: 52.61  E-value: 5.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2904 NIQGLQAHIADLKHDRRML-------DADLLCLTETWLQHNTAQGNIDMAGWTFHCKARSQSYSNQgafsalqkqqhGGV 2976
Cdd:pfam03372    4 NVNGGNADAAGDDRKLDALaalirayDPDVVALQETDDDDASRLLLALLAYGGFLSYGGPGGGGGG-----------GGV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2977 GFYHKNHIISNIIN---------LPCSELEAIIFNIQPMNHNYIVLYRPPSYQISLFKQNLSAVVSHFNALSGGKIIMGD 3047
Cdd:pfam03372   73 AILSRYPLSSVILVdlgefgdpaLRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGD 152

                          170
                   ....*....|...
gi 1708930973 3048 FN-DNAVVSKSME 3059
Cdd:pfam03372  153 FNaDYILVSGGLT 165
Herpes_teg_N super family cl04795
Herpesvirus tegument protein, N-terminal conserved region;
702-877 7.83e-03

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: 40.18  E-value: 7.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  702 SFNQGNPRFGENKGKQCATNSITAVMTNVLKSAWTWTTTD-LDNVLVNGNDLYTyvkDKHKVSVLEGKGYILVKELPtEY 780
Cdd:pfam04843    1 SRNQFDCKFGPRAGSQCLSNCVSFLHSSYLNGINPVLSREaLDAVLEEGARLDT---LLRTSGRLPPRQYAQLHEIP-GI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  781 ELLDKKFCLEYMES----LSGHIDVEEYHPAVQDYVMPLDVAFQRAMLNADA------CLLNIKKNICAVLKQRDQFAVF 850
Cdd:pfam04843   77 IITGAWGCLIYRSSeiygLLGHELSRNFNGTPQTGDIDTQMPAGIFFRYAKAkrrpsyTLIICNSLAMAIVIKDKTYYLF 156

                          170       180
                   ....*....|....*....|....*..
gi 1708930973  851 DPHArgadgglQHDGTSIVACYDTLDA 877
Cdd:pfam04843  157 DPHC-------TPEGNSTAAVIVTVDA 176
 
Name Accession Description Interval E-value
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
 1016-1140 1.29e-59

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: 201.72  E-value: 1.29e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1016 CTTIDIQGDGNCFFRSLSYVFSGLESHHRTVRLAVVKHVEQNPDVYRNVVREQFTSVQQYVNDSRMKYVGTWATEVEIQA 1095
Cdd:cd22755      1 CKTIKIVGDGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKNPDEFRNLLRSDYESVEEYLEKSRMRYDGTWATDVEIFA 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1708930973 1096 AANLFNVDIYTYSEQ--KWLKYGSSGA----AARNKAIYIKHCNECHYEPI 1140
Cdd:cd22755     81 AATLLGVDIYVYSKGgyKWLLYSPRFKlgkrNGSREAIYLKNTNGNHFEPV 131
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 2450-2853 7.70e-46

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: 175.16  E-value: 7.70e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2450 HVFLSGGAGTGKSHLIKALyyeaTRLLARLshnpdAVHVLLTAPTGVAAYN------INATTIHNTFAiptnvslpYQPL 2523
Cdd:COG0507    142 VSVLTGGAGTGKTTTLRAL----LAALEAL-----GLRVALAAPTGKAAKRlsestgIEARTIHRLLG--------LRPD 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2524 KEEKVNTLRAALRDLKILIIDEISMVDHKLLAYIHgrvrqikqsgDFAPFGNVSVIAVGDFYQLPPV-KGKPLYtdqagi 2602
Cdd:COG0507    205 SGRFRHNRDNPLTPADLLVVDEASMVDTRLMAALL----------EALPRAGARLILVGDPDQLPSVgAGAVLR------ 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2603 DLWGS-TFKHVELTEIVRQKNQD-FAVTLNRIRKHKKGDKLNAQD-----------EKLLKQCQTGVGDDTEDLH----I 2665
Cdd:COG0507    269 DLIESgTVPVVELTEVYRQADDSrIIELAHAIREGDAPEALNARYadvvfveaedaEEAAEAIVELYADRPAGGEdiqvL 348

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2666 FATNSDVDAHNfKMLhkvcsdvvqikaqdfeknpQTGRFAQKTTSHAFNKHTHlsalLSIAPNARVMLIKNiDTCDGLVN 2745
Cdd:COG0507    349 APTNAGVDALN-QAI-------------------REALNPAGELERELAEDGE----LELYVGDRVMFTRN-DYDLGVFN 403

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2746 GVLGTVSLIKCDEKTkvpklIYVKFDDDRIgsklrakfpctvpglqnatpVGLDEDKVPYrggirrqfpLRLAWACTIHK 2825
Cdd:COG0507    404 GDIGTVLSIDEDEGR-----LTVRFDGREI--------------------VTYDPSELDQ---------LELAYAITVHK 449

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1708930973 2826 VQGLTLEKAVV----SFKKIFSAGQAYVALSR 2853
Cdd:COG0507    450 SQGSTFDRVILvlpsEHSPLLSRELLYTALTR 481
DEXSc_Pif1_like cd18037
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ...
 2434-2619 3.39e-40

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: 148.17  E-value: 3.39e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2434 QKWCLDTV-NGHNpapfhVFLSGGAGTGKSHLIKalyyeatRLLARLSHNPDAVHVllTAPTGVAAYNINATTIHNTFAI 2512
Cdd:cd18037      2 QRRVLDLVlDGKN-----VFFTGSAGTGKSYLLR-------RIIRALPSRPKRVAV--TASTGIAACNIGGTTLHSFAGI 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2513 PTNVSLPYQPLKEEK-VNTLRAALRDLKILIIDEISMVDHKLLAYIHGRVRQIKQSGDfaPFGNVSVIAVGDFYQLPPVK 2591
Cdd:cd18037     68 GLGSEPAEDLLERVKrSPYLVQRWRKCDVLIIDEISMLDADLFDKLDRVAREVRGSDK--PFGGIQLILCGDFLQLPPVT 145

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1708930973 2592 GKPL---YTDQAGI------DLW-GSTFKHVELTEIVR 2619
Cdd:cd18037    146 KNSErqaFFFRGDQqfcfeaKSWeRCIFLTVELTKVFR 183
Helitron_like_N pfam14214
Helitron helicase-like domain at N-terminus; This family is found in Helitrons, recently ...
 1706-1900 1.02e-31

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: 124.31  E-value: 1.02e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1706 RILNADGRFGSNVEYIFYAQYLSEINQVVSNVSIALRkgHHGGE--SSQITSSML-----ASTDFVNNVLRCDMGYKFLK 1778
Cdd:pfam14214    4 RLQHHDGRFARHPRFLFVAFNLFQQARAESRRLSFIR--VNQKElrAESYTGERLrdaleEETDDPEVLALLGSIVILPS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1779 PIRGTPVFWQRVQKDLFAMVKQLGIPTWFCSFSSADLrWTELMQTFMEVQNVQGNVDEMDWsqkCNLLNNNPVTAARMFD 1858
Cdd:pfam14214   82 SVPGSPRYMLQLRQDAMAIVRRLGKPDLFITFTPNDL-WPEIKRELARYREWKLPGAQTRL---RRLASDRPDIVARVFH 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1708930973 1859 HRFRSFLHDVIMSPAQPIGKIIDYFYRVEFQQRGSPHTHCLF 1900
Cdd:pfam14214  158 RKLELFLKDLLRFKEGVFGNVSAYVYTVEFQKRGLPHAHGLL 199
DUF6570 pfam20209
Domain of unknown function (DUF6570); This entry represents a presumed domain of unknown ...
 1470-1595 1.85e-25

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: 103.95  E-value: 1.85e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1470 GKVPDQSVINNLQLDPIPQELNTLNPLEQHLIAPHIPFMKLVAL--PKGGQNGVHGPVTCVPSNTNAVNVLPR-LENQDL 1546
Cdd:pfam20209    2 GKLPKFSLANGLWIGEVPEELQDLTFVEELLIARVRPRVYVVKLrpKSGGQRGLRGNVIAFPQDVGKLSVLPRpPEDLDD 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1708930973 1547 MIRVKLKR-KLSYKGHYEYQY-VNTSKVHSALENLKQNNKWYKDVEINTDW 1595
Cdd:pfam20209   82 VIAVLFIGpKKPTKEWLKKPFrVRRAKVRAALRWLKANNPLYRDIEIDEEN 132
PIF1 pfam05970
PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits ...
 2422-2751 6.34e-24

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: 106.31  E-value: 6.34e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2422 LNELQSQVFYTIqkwcLDTVNGHNPAPFhvFLSGGAGTGKSHLIKALyyeatrlLARLshNPDAVHVLLTAPTGVAAYNI 2501
Cdd:pfam05970    1 LNDEQKKVFDAI----IESVINNKGGVF--FVYGYGGTGKTFLWKAI-------ITSL--RSEGKIVLAVASSGVAALLL 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2502 -NATTIHNTFAIPTNVSlPYQPLKEEKVNTLRAALRDLKILIIDEISMVDHKLLAYIHGRVRQIKQSGDFAPFGNVSVIA 2580
Cdd:pfam05970   66 pGGRTAHSRFGIPLDID-ELSTCKIKRGSKLAELLEKTSLIVWDEAPMTHRHCFEALDRTLRDILSETDDKPFGGKTVVL 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2581 VGDFYQLPPV--KGKPLYTDQAGID---LWGStFKHVELTEIVRQKN-----------QDFAVTLNRIRKHKKGDKLNAQ 2644
Cdd:pfam05970  145 GGDFRQILPVipKGSRPEIVNASITnsyLWKH-VKVLELTKNMRLLAdsldqteakelQDFSDWLLAIGDGKINDENERE 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2645 ------DEKLLKQCQTG--------VGD------DTEDLHIFA----TNSDVDAHNFKMLHKVCSDVVQIKAQDfeknpq 2700
Cdd:pfam05970  224 qlidipIDILLNTGGDPieaivsevYPDilqnstDPNYLEERAilcpTNEDVDEINNYRLSQLPGEEKEYLSSD------ 297

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1708930973 2701 tgRFAQKTTSHAFNKHTHLSALLSIA----PN--------ARVMLIKNIDTCDGLVNGVLGTV 2751
Cdd:pfam05970  298 --SISKSDNDSEIDALYPTEFLNSLNanglPNhvlklkvgAPVMLLRNLDQSRGLCNGTRLIV 358
recD_rel TIGR01448
helicase, putative, RecD/TraA family; This model describes a family similar to RecD, the ...
 2433-2828 2.88e-12

helicase, putative, RecD/TraA family; This model describes a family similar to RecD, the exodeoxyribonuclease V alpha chain of TIGR01447. Members of this family, however, are not found in a context of RecB and RecC and are longer by about 200 amino acids at the amino end. Chlamydia muridarum has both a member of this family and a RecD. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273632 [Multi-domain]  Cd Length: 720  Bit Score: 72.89  E-value: 2.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2433 IQKWCLDTVNGHNPapfhVFLSGGAGTGKSHLIKA---LYYEATRLLArlshnpdavhVLLTAPTGVAAYNIN------A 2503
Cdd:TIGR01448  327 EQKQALDTAIQHKV----VILTGGPGTGKTTITRAiieLAEELGGLLP----------VGLAAPTGRAAKRLGevtgltA 392

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2504 TTIHNTfaiptnvsLPYQPlKEEKVNTLRAALrDLKILIIDEISMVD----HKLLAYI--HGRVrqikqsgdfapfgnvs 2577
Cdd:TIGR01448  393 STIHRL--------LGYGP-DTFRHNHLEDPI-DCDLLIVDESSMMDtwlaLSLLAALpdHARL---------------- 446

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2578 vIAVGDFYQLPPV-KGKPLytdqagIDLWGStfKHVE---LTEIVRQKNQD----FAVTLNRIRKHKKGDKLNAQDEKLL 2649
Cdd:TIGR01448  447 -LLVGDTDQLPSVgPGQVL------KDLILS--QAIPvtrLTKVYRQAAGSpiitLAHGILHGEAPAWGDFKFLNLTRSE 517

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2650 KQCQTG-VGDDTEDLHIFATNSDVDAHNFKMLHKVCSDVVQIKA-----QDFEKNPQTGRFAQKTTSHAFNkhthlsall 2723
Cdd:TIGR01448  518 PEGAARhIPLMVEKIVGMARVGGIPGADIQVLAPMYKGPLGIDAlnqhlQALLNPYQKGQGGIEIAEGEYR--------- 588

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2724 siaPNARVMLIKNiDTCDGLVNGVLGTVSLIKCDEKTKVPKLIyVKFDDDRIgsklrakfpcTVPGLQnatpvgldedkv 2803
Cdd:TIGR01448  589 ---KGDRVMQTKN-DYNNEIFNGDLGMIVKIEGAKQGKKDQVV-VDFDGNEV----------ELTRAE------------ 641

                          410       420
                   ....*....|....*....|....*
gi 1708930973 2804 pyrggirrQFPLRLAWACTIHKVQG 2828
Cdd:TIGR01448  642 --------LFNLTLAYATSIHKSQG 658
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 72-234 4.59e-10

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 61.58  E-value: 4.59e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973   72 ILVVGDShlraLVDGFVQMPEGC----LSFGFMST---------PGASAAQLRTEVEHAVLPQIPEAVCLLAPGNDLTAS 138
Cdd:COG2755     11 IVALGDS----ITAGYGASRERGwpalLARRLAAAdvrvvnagiSGATTADLLARLDRDLLALKPDLVVIELGTNDLLRG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  139 Q--TIEEAAKEFRRLLYSICKRWPN--VCVLD-FPRRLTMTM-DHQKLLSQEYHRVAARMGIRYLDTDSHFPTCHR--EL 210
Cdd:COG2755     87 LgvSPEEFRANLEALIDRLRAAGPGarVVLVTpPPRLRPNYLnERIEAYNAAIRELAAEYGVPLVDLYAALRDAGDlpDL 166

                          170       180
                   ....*....|....*....|....
gi 1708930973  211 WCSDGVHLSDsDGMPILSQLLWTA 234
Cdd:COG2755    167 LTADGLHPNA-AGYRLIAEAVLPA 189
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 72-234 4.28e-09

SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.


Pssm-ID: 238141 [Multi-domain]  Cd Length: 187  Bit Score: 58.58  E-value: 4.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973   72 ILVVGDSHLR-----ALVDGFVQMPEGCLSFGFM-------STPGASAAQL--RTEVEHAVLPQIPEAVCLLAPGNDLTA 137
Cdd:cd00229      1 ILVIGDSITAgygasSGSTFYSLLLYLLLLAGGPgvevinlGVSGATTADAlrRLGLRLALLKDKPDLVIIELGTNDLGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  138 SQ--TIEEAAKEFRRLLYSICKRWPNVCVL-----DFPRRLTMTMDHQKLLSQEYHRVAARM----GIRYLDTDSHFPTC 206
Cdd:cd00229     81 GGdtSIDEFKANLEELLDALRERAPGAKVIlitppPPPPREGLLGRALPRYNEAIKAVAAENpapsGVDLVDLAALLGDE 160

                          170       180
                   ....*....|....*....|....*...
gi 1708930973  207 HRELWCSDGVHLSDsDGMPILSQLLWTA 234
Cdd:cd00229    161 DKSLYSPDGIHPNP-AGHKLIAEALASA 187
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 103-220 3.56e-07

GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are similar to pfam00657.


Pssm-ID: 463889  Cd Length: 176  Bit Score: 52.93  E-value: 3.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  103 PGASAAQLRTEVEHAVLPQIPEAVCLLAPGNDLTASQTIEEAAKEFRRLLYSICKRWPNVCVLD---------FPRRLTM 173
Cdd:pfam13472   42 SGATTRLDLLERLDDVLRLKPDLVVILLGTNDLGRGVSAARAAANLEALIDALRAAGPDARVLLigplpvgppPPLDERR 121

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1708930973  174 TMDHQKLLSQEYHRVAARMGIRYLDTDSHF---PTCHRELWCSDGVHLSD 220
Cdd:pfam13472  122 LNARIAEYNAAIREVAAERGVPYVDLWDALrddGGWLPDLLADDGLHPNA 171
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 2904-3059 5.35e-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: 52.61  E-value: 5.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2904 NIQGLQAHIADLKHDRRML-------DADLLCLTETWLQHNTAQGNIDMAGWTFHCKARSQSYSNQgafsalqkqqhGGV 2976
Cdd:pfam03372    4 NVNGGNADAAGDDRKLDALaalirayDPDVVALQETDDDDASRLLLALLAYGGFLSYGGPGGGGGG-----------GGV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2977 GFYHKNHIISNIIN---------LPCSELEAIIFNIQPMNHNYIVLYRPPSYQISLFKQNLSAVVSHFNALSGGKIIMGD 3047
Cdd:pfam03372   73 AILSRYPLSSVILVdlgefgdpaLRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGD 152

                          170
                   ....*....|...
gi 1708930973 3048 FN-DNAVVSKSME 3059
Cdd:pfam03372  153 FNaDYILVSGGLT 165
COG5539 COG5539
Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, ...
 1008-1131 2.24e-05

Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227826 [Multi-domain]  Cd Length: 306  Bit Score: 49.10  E-value: 2.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1008 LDIEQPQPCTTI---DIQGDGNCFFRSLSyvfSGLESHHRTVRLAVVKHVEQNPDVYRNVVREQFTS------------V 1072
Cdd:COG5539    160 LEIDVIAYATWIvkpDSQGDGCIEIAIIS---DQLPVRIHVVDVDKDSEDRYNSHPYVQRISILFTGihfdeetlamvlW 236

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1073 QQYVNDsrMKYVGTWATEVEIQAAANLFNVDIYTY-SEQKWLKYGSSGAAARNKAIYIKH 1131
Cdd:COG5539    237 DTYVNE--VLFDASDGITIEIQQLASLLKNPHYYTnTASPSIKCNICGTGFVGEKDYYAH 294
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 2450-2581 2.95e-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: 46.60  E-value: 2.95e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  2450 HVFLSGGAGTGKSHLIKAlyyeatrlLARLShNPDAVHVLLTAPTGVAAYNINATTIHNTFAIPTNVSlpyqplKEEKVN 2529
Cdd:smart00382    4 VILIVGPPGSGKTTLARA--------LAREL-GPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS------GELRLR 68

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1708930973  2530 TLRAALR--DLKILIIDEISMVDHKLLAYIHGRVRQIKQSGDFAPFGNVSVIAV 2581
Cdd:smart00382   69 LALALARklKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILT 122
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 1022-1161 8.18e-05

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: 44.75  E-value: 8.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1022 QGDGNCFFRSLS----YVFSGLESH-HRTVRLAVVkhveqnpdvyrNVVREQFTSVQQYVNDSRMKYV------GTWATE 1090
Cdd:pfam02338    1 PGDGNCLYRSIShqlwGVHDVLRKMlVQELRETLA-----------EYMREHKEEFEPFLEDDETGDIieieqtGAWGGE 69

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708930973 1091 VEIQAAANLFNVDIYTYseqkwlkYGSSGAAARNKAIYiKHCNECHYEPIECVKdisgkcfSLRTLGETNH 1161
Cdd:pfam02338   70 IEIFALAHILRRPIIVY-------KSEGGEELGGLKEY-GIYLPLGWDPSLCLV-------YPRHLYYLGG 125
PHA03311 PHA03311
helicase-primase subunit BBLF4; Provisional
 2820-2862 1.05e-04

helicase-primase subunit BBLF4; Provisional


Pssm-ID: 223040  Cd Length: 782  Bit Score: 47.98  E-value: 1.05e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1708930973 2820 ACTIHKVQGLTLEKAVVSF---KKIfSAGQAYVALSRVTSIENLII 2862
Cdd:PHA03311   706 AMTIAKSQGLSLDKVAICFgnhKNL-KLSHVYVAMSRVTSSNFLVM 750
L1-EN cd09076
Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; ...
 2900-3056 2.20e-03

Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; This family contains the endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains, including the endonuclease of Xenopus laevis Tx1. These retrotranspons belong to the subtype 2, L1-clade. LINES can be classified into two subtypes. Subtype 2 has two ORFs: the second (ORF2) encodes a modular protein consisting of an N-terminal apurine/apyrimidine endonuclease domain (EN), a central reverse transcriptase, and a zinc-finger-like domain at the C-terminus. LINE-1/L1 elements (full length and truncated) comprise about 17% of the human genome. This endonuclease nicks the genomic DNA at the consensus target sequence 5'TTTT-AA3' producing a ribose 3'-hydroxyl end as a primer for reverse transcription of associated template RNA. This subgroup also includes the endonuclease of Xenopus laevis Tx1, another member of the L1-clade. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197310 [Multi-domain]  Cd Length: 236  Bit Score: 42.34  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2900 VCLLNIQGL--QAHIADLKHDRRMLDADLLCLTETWLQHNTAQGNIDMAGWTFhckarsqsysnqgaFSALQKQQHGGVG 2977
Cdd:cd09076      1 IGTLNVRGLrsPGKRAQLLEELKRKKLDILGLQETHWTGEGELKKKREGGTIL--------------YSGSDSGKSRGVA 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2978 FYHKNHIISNIINLPCSELEAII---FNIQPMNHNYIVLYRPPSYQ---ISLFKQNLSAVVSHFNAlSGGKIIMGDFndN 3051
Cdd:cd09076     67 ILLSKTAANKLLEYTKVVSGRIImvrFKIKGKRLTIINVYAPTARDeeeKEEFYDQLQDVLDKVPR-HDTLIIGGDF--N 143


                   ....*
gi 1708930973 3052 AVVSK 3056
Cdd:cd09076    144 AVLGP 148
Herpes_teg_N pfam04843
Herpesvirus tegument protein, N-terminal conserved region;
702-877 7.83e-03

Herpesvirus tegument protein, N-terminal conserved region;


Pssm-ID: 461453 [Multi-domain]  Cd Length: 183  Bit Score: 40.18  E-value: 7.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  702 SFNQGNPRFGENKGKQCATNSITAVMTNVLKSAWTWTTTD-LDNVLVNGNDLYTyvkDKHKVSVLEGKGYILVKELPtEY 780
Cdd:pfam04843    1 SRNQFDCKFGPRAGSQCLSNCVSFLHSSYLNGINPVLSREaLDAVLEEGARLDT---LLRTSGRLPPRQYAQLHEIP-GI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  781 ELLDKKFCLEYMES----LSGHIDVEEYHPAVQDYVMPLDVAFQRAMLNADA------CLLNIKKNICAVLKQRDQFAVF 850
Cdd:pfam04843   77 IITGAWGCLIYRSSeiygLLGHELSRNFNGTPQTGDIDTQMPAGIFFRYAKAkrrpsyTLIICNSLAMAIVIKDKTYYLF 156

                          170       180
                   ....*....|....*....|....*..
gi 1708930973  851 DPHArgadgglQHDGTSIVACYDTLDA 877
Cdd:pfam04843  157 DPHC-------TPEGNSTAAVIVTVDA 176
 
Name Accession Description Interval E-value
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
 1016-1140 1.29e-59

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: 201.72  E-value: 1.29e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1016 CTTIDIQGDGNCFFRSLSYVFSGLESHHRTVRLAVVKHVEQNPDVYRNVVREQFTSVQQYVNDSRMKYVGTWATEVEIQA 1095
Cdd:cd22755      1 CKTIKIVGDGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKNPDEFRNLLRSDYESVEEYLEKSRMRYDGTWATDVEIFA 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1708930973 1096 AANLFNVDIYTYSEQ--KWLKYGSSGA----AARNKAIYIKHCNECHYEPI 1140
Cdd:cd22755     81 AATLLGVDIYVYSKGgyKWLLYSPRFKlgkrNGSREAIYLKNTNGNHFEPV 131
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 2450-2853 7.70e-46

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: 175.16  E-value: 7.70e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2450 HVFLSGGAGTGKSHLIKALyyeaTRLLARLshnpdAVHVLLTAPTGVAAYN------INATTIHNTFAiptnvslpYQPL 2523
Cdd:COG0507    142 VSVLTGGAGTGKTTTLRAL----LAALEAL-----GLRVALAAPTGKAAKRlsestgIEARTIHRLLG--------LRPD 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2524 KEEKVNTLRAALRDLKILIIDEISMVDHKLLAYIHgrvrqikqsgDFAPFGNVSVIAVGDFYQLPPV-KGKPLYtdqagi 2602
Cdd:COG0507    205 SGRFRHNRDNPLTPADLLVVDEASMVDTRLMAALL----------EALPRAGARLILVGDPDQLPSVgAGAVLR------ 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2603 DLWGS-TFKHVELTEIVRQKNQD-FAVTLNRIRKHKKGDKLNAQD-----------EKLLKQCQTGVGDDTEDLH----I 2665
Cdd:COG0507    269 DLIESgTVPVVELTEVYRQADDSrIIELAHAIREGDAPEALNARYadvvfveaedaEEAAEAIVELYADRPAGGEdiqvL 348

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2666 FATNSDVDAHNfKMLhkvcsdvvqikaqdfeknpQTGRFAQKTTSHAFNKHTHlsalLSIAPNARVMLIKNiDTCDGLVN 2745
Cdd:COG0507    349 APTNAGVDALN-QAI-------------------REALNPAGELERELAEDGE----LELYVGDRVMFTRN-DYDLGVFN 403

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2746 GVLGTVSLIKCDEKTkvpklIYVKFDDDRIgsklrakfpctvpglqnatpVGLDEDKVPYrggirrqfpLRLAWACTIHK 2825
Cdd:COG0507    404 GDIGTVLSIDEDEGR-----LTVRFDGREI--------------------VTYDPSELDQ---------LELAYAITVHK 449

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1708930973 2826 VQGLTLEKAVV----SFKKIFSAGQAYVALSR 2853
Cdd:COG0507    450 SQGSTFDRVILvlpsEHSPLLSRELLYTALTR 481
DEXSc_Pif1_like cd18037
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ...
 2434-2619 3.39e-40

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: 148.17  E-value: 3.39e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2434 QKWCLDTV-NGHNpapfhVFLSGGAGTGKSHLIKalyyeatRLLARLSHNPDAVHVllTAPTGVAAYNINATTIHNTFAI 2512
Cdd:cd18037      2 QRRVLDLVlDGKN-----VFFTGSAGTGKSYLLR-------RIIRALPSRPKRVAV--TASTGIAACNIGGTTLHSFAGI 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2513 PTNVSLPYQPLKEEK-VNTLRAALRDLKILIIDEISMVDHKLLAYIHGRVRQIKQSGDfaPFGNVSVIAVGDFYQLPPVK 2591
Cdd:cd18037     68 GLGSEPAEDLLERVKrSPYLVQRWRKCDVLIIDEISMLDADLFDKLDRVAREVRGSDK--PFGGIQLILCGDFLQLPPVT 145

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1708930973 2592 GKPL---YTDQAGI------DLW-GSTFKHVELTEIVR 2619
Cdd:cd18037    146 KNSErqaFFFRGDQqfcfeaKSWeRCIFLTVELTKVFR 183
Helitron_like_N pfam14214
Helitron helicase-like domain at N-terminus; This family is found in Helitrons, recently ...
 1706-1900 1.02e-31

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: 124.31  E-value: 1.02e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1706 RILNADGRFGSNVEYIFYAQYLSEINQVVSNVSIALRkgHHGGE--SSQITSSML-----ASTDFVNNVLRCDMGYKFLK 1778
Cdd:pfam14214    4 RLQHHDGRFARHPRFLFVAFNLFQQARAESRRLSFIR--VNQKElrAESYTGERLrdaleEETDDPEVLALLGSIVILPS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1779 PIRGTPVFWQRVQKDLFAMVKQLGIPTWFCSFSSADLrWTELMQTFMEVQNVQGNVDEMDWsqkCNLLNNNPVTAARMFD 1858
Cdd:pfam14214   82 SVPGSPRYMLQLRQDAMAIVRRLGKPDLFITFTPNDL-WPEIKRELARYREWKLPGAQTRL---RRLASDRPDIVARVFH 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1708930973 1859 HRFRSFLHDVIMSPAQPIGKIIDYFYRVEFQQRGSPHTHCLF 1900
Cdd:pfam14214  158 RKLELFLKDLLRFKEGVFGNVSAYVYTVEFQKRGLPHAHGLL 199
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
 1017-1140 1.73e-28

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: 112.53  E-value: 1.73e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1017 TTIDIQGDGNCFFRSLSYVFSGLESHHRTVRLAVVKHVEQNPDVYRNVVREQFT---SVQQYVNdsRMKYVGTWATEVEI 1093
Cdd:cd22744      1 RVVDVPGDGNCLFRALAHALYGDQESHRELRQEVVDYLRENPDLYEPAELADEDdgeDFDEYLQ--RMRKPGTWGGELEL 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1094 QAAANLFNVDIYTYSEQKWLKYGSS---GAAARNKAIYIKHCNECHYEPI 1140
Cdd:cd22744     79 QALANALNVPIVVYSEDGGFLPVSVfgpGPGPSGRPIHLLYTGGNHYDAL 128
DUF6570 pfam20209
Domain of unknown function (DUF6570); This entry represents a presumed domain of unknown ...
 1470-1595 1.85e-25

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: 103.95  E-value: 1.85e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1470 GKVPDQSVINNLQLDPIPQELNTLNPLEQHLIAPHIPFMKLVAL--PKGGQNGVHGPVTCVPSNTNAVNVLPR-LENQDL 1546
Cdd:pfam20209    2 GKLPKFSLANGLWIGEVPEELQDLTFVEELLIARVRPRVYVVKLrpKSGGQRGLRGNVIAFPQDVGKLSVLPRpPEDLDD 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1708930973 1547 MIRVKLKR-KLSYKGHYEYQY-VNTSKVHSALENLKQNNKWYKDVEINTDW 1595
Cdd:pfam20209   82 VIAVLFIGpKKPTKEWLKKPFrVRRAKVRAALRWLKANNPLYRDIEIDEEN 132
PIF1 pfam05970
PIF1-like helicase; This family includes homologs of the PIF1 helicase, which inhibits ...
 2422-2751 6.34e-24

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: 106.31  E-value: 6.34e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2422 LNELQSQVFYTIqkwcLDTVNGHNPAPFhvFLSGGAGTGKSHLIKALyyeatrlLARLshNPDAVHVLLTAPTGVAAYNI 2501
Cdd:pfam05970    1 LNDEQKKVFDAI----IESVINNKGGVF--FVYGYGGTGKTFLWKAI-------ITSL--RSEGKIVLAVASSGVAALLL 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2502 -NATTIHNTFAIPTNVSlPYQPLKEEKVNTLRAALRDLKILIIDEISMVDHKLLAYIHGRVRQIKQSGDFAPFGNVSVIA 2580
Cdd:pfam05970   66 pGGRTAHSRFGIPLDID-ELSTCKIKRGSKLAELLEKTSLIVWDEAPMTHRHCFEALDRTLRDILSETDDKPFGGKTVVL 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2581 VGDFYQLPPV--KGKPLYTDQAGID---LWGStFKHVELTEIVRQKN-----------QDFAVTLNRIRKHKKGDKLNAQ 2644
Cdd:pfam05970  145 GGDFRQILPVipKGSRPEIVNASITnsyLWKH-VKVLELTKNMRLLAdsldqteakelQDFSDWLLAIGDGKINDENERE 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2645 ------DEKLLKQCQTG--------VGD------DTEDLHIFA----TNSDVDAHNFKMLHKVCSDVVQIKAQDfeknpq 2700
Cdd:pfam05970  224 qlidipIDILLNTGGDPieaivsevYPDilqnstDPNYLEERAilcpTNEDVDEINNYRLSQLPGEEKEYLSSD------ 297

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1708930973 2701 tgRFAQKTTSHAFNKHTHLSALLSIA----PN--------ARVMLIKNIDTCDGLVNGVLGTV 2751
Cdd:pfam05970  298 --SISKSDNDSEIDALYPTEFLNSLNanglPNhvlklkvgAPVMLLRNLDQSRGLCNGTRLIV 358
OTU_232R-like cd22758
OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase ...
 1019-1137 7.86e-23

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: 96.57  E-value: 7.86e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1019 IDIQGDGNCFFRSLSYVFS--GLESHHRTVRLAVVKHVEQNPDVYRNVVREQFT---SVQQYVNdsRMKYVGTWATEVEI 1093
Cdd:cd22758      9 RDVPGDGNCFFHAVSDQLYgnGIEHSHKELRQQAVNYLRENPELYDGFFLSEFDeeeSWEEYLN--RMSKDGTWGDHIIL 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1708930973 1094 QAAANLFNVDIYTYS-----EQKWLKygsSGAAARNKAIYIKHCNECHY 1137
Cdd:cd22758     87 QAAANLFNVRIVIISsdgsdETTIIE---PGNSKNGRTIYLGHIGENHY 132
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 2451-2618 2.92e-21

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: 92.62  E-value: 2.92e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2451 VFLSGGAGTGKSHLIKAL--YYEATRLlarlshnpdavHVLLTAPTGVAA------YNINATTIHntfaiptnvSLPYQP 2522
Cdd:cd17933     15 SVLTGGAGTGKTTTLKALlaALEAEGK-----------RVVLAAPTGKAAkrlsesTGIEASTIH---------RLLGIN 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2523 LKEEKVNTLRAALRDLKILIIDEISMVD----HKLLAYIHGRVRqikqsgdfapfgnvsVIAVGDFYQLPPV-KGKPLYT 2597
Cdd:cd17933     75 PGGGGFYYNEENPLDADLLIVDEASMVDtrlmAALLSAIPAGAR---------------LILVGDPDQLPSVgAGNVLRD 139

                          170       180
                   ....*....|....*....|.
gi 1708930973 2598 DQAGIDlwgstFKHVELTEIV 2618
Cdd:cd17933    140 LIASKG-----VPTVELTEVF 155
OTU_P87_VP80-like cd22757
OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The ...
 1019-1111 7.98e-21

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: 90.73  E-value: 7.98e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1019 IDIQGDGNCFFRSLSYVFSGLESHHRTVRLAVVKHVEQNPDVYRNVVREQ----FTSVQQYVNDsrMKYVGTWATEVEIQ 1094
Cdd:cd22757      4 IPIPGDGACLFRALSYLLYGTQSRHLEVRKEVVDYVVNNWDEFSIYTHDSegnnYKSAEEYRAD--MSKPGTYGTLCELV 81

                           90
                   ....*....|....*..
gi 1708930973 1095 AAANLFNVDIYTYSEQK 1111
Cdd:cd22757     82 AAAELYPFHFEVYRNGK 98
OTU_OTUD3-like cd22756
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This ...
 1018-1107 1.14e-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: 90.31  E-value: 1.14e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1018 TIDIQGDGNCFFRSLSYVFSGLESHHRTVRLAVVKHVEQNPDVYRNVVR-----EQFTSVQQYVNdsRMKYVGTWATEVE 1092
Cdd:cd22756      2 AKDITGDGNCLFRALSDQLYGDPDRHLEIRAEVVEYMRANPDDFKPFSEaatfaEDDEAFEDYLA--RMAKDGTYGDNLE 79

                           90
                   ....*....|....*
gi 1708930973 1093 IQAAANLFNVDIYTY 1107
Cdd:cd22756     80 IVAFARAYNVDVKVY 94
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 2451-2646 1.47e-20

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: 91.86  E-value: 1.47e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2451 VFLSGGAGTGKSHLIKALyyeaTRLLARLSHnpdavHVLLTAPTGVAA------YNINATTIHntfaiptnvslpyqplK 2524
Cdd:pfam13604   21 AVLVGPAGTGKTTALKAL----REAWEAAGY-----RVIGLAPTGRAAkvlgeeLGIPADTIA----------------K 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2525 EEKVNTLRAALRDLKILIIDEISMVDHKLLAYIHGRVRQikqsgdfapfGNVSVIAVGDFYQLPPVK-GKPLYtdqagiD 2603
Cdd:pfam13604   76 LLHRLGGRAGLDPGTLLIVDEAGMVGTRQMARLLKLAED----------AGARVILVGDPRQLPSVEaGGAFR------D 139

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1708930973 2604 LWGSTFKHVELTEIVRQKNQDFAVTLNRIRKHKKGDKLNAQDE 2646
Cdd:pfam13604  140 LLAAGIGTAELTEIVRQRDPWQRAASLALRDGDPAEALDALAD 182
OTU_plant_OTU7-like cd22771
OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar ...
 1020-1137 1.88e-20

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: 89.53  E-value: 1.88e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1020 DIQGDGNCFFRSLSYVFSGLESHHRTVRLAVVKHVEQNPDVYRNVVrEQFTSVQQYVndSRMKYVGTWATEVEIQAAANL 1099
Cdd:cd22771      6 DVEGDGNCLFRALADQLYGDEERHAELRKKVVDYMEAHEEDFEPFF-EDDETFEDYV--SRMREDGTWGGNLELQAASLV 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1708930973 1100 FNVDI--YTYSEQKW-LKYGSsgaAARNKAIYIKHCNECHY 1137
Cdd:cd22771     83 YRVNIvvHQLGQPRWeIENFP---DKGARTIHLSYHDGEHY 120
OTU_plant_OTU9-like cd22751
OTU (ovarian tumor) domain of plant deubiquitinating enzyme OTU9 and similar proteins; This ...
 1019-1137 4.34e-19

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: 85.67  E-value: 4.34e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1019 IDIQGDGNCFFRSLSYVFSGLESHHRTVRLAVVKHVEQNPDV-YRNVVREQFtsvQQYVNdsRMKYVGTWATEVEIQAAA 1097
Cdd:cd22751     13 RKVEGDGNCQFRALSDQLFGTQDHHAEVRELVVKQLRAHPELyYEFYVPEEY---DEYLK--KMSKDGEWGDELTLQAAA 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1708930973 1098 NLFNVDIY---TYSEQKWLKYGSSGAAARNKAIYIKHCNECHY 1137
Cdd:cd22751     88 DAFGVKIHvitSFEDNWFLEIEPRGLVRSKRVLFLSYWAEVHY 130
OTU_OTUD5-like cd22752
OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU ...
 1019-1140 9.67e-15

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: 72.97  E-value: 9.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1019 IDIQGDGNCFFRSLSYVFSGLESHHRTVRLAVVKHVEQNPDVYRNVVREQFTSvqqYVNdsRMKYVGTWATEVEIQAAAN 1098
Cdd:cd22752      5 KEMEEDGNCLFRAVADQVYGDQEMHDVVRKHCMDYMEKNRDYFSQFVTEDFEE---YIN--RKRQDGVWGNHIEIQAMSE 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1708930973 1099 LFN--VDIYTYSeqkwlkygssgaaarNKAIYIKHC-NECHYEPI 1140
Cdd:cd22752     80 LYNrpIEVYAYS---------------TEPINTFHEaSSSDNEPI 109
OTU_ALG13-like cd22753
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 1024-1140 9.78e-13

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: 67.57  E-value: 9.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1024 DGNCFFRSLSYVFSGLESHHRTVRLAVVKHVEQNPDVYRNVVreqFTSVQQYVNdsRMKYVGTWATEVEIQAAANLFNVD 1103
Cdd:cd22753     18 DGSCLFRAVSEQLFFTQSYHQQVRQACVEYLEKNREEFEKFS---EISFDDYLE--RLSDPKEWGGLLELEALSLLYKVD 92

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1708930973 1104 IYTYSEQKWLKYGSSGaAARNKAIYIKHCNECHYEPI 1140
Cdd:cd22753     93 FIVYSIPDQPPSNITN-NGYPKKIMLCYSGGNHYDSV 128
AAA_19 pfam13245
AAA domain;
2450-2590 1.79e-12

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 66.86  E-value: 1.79e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2450 HVFLSGGAGTGKSHLIKALyyeaTRLLARLshNPDAVHVLLTAPTGVAAYNIN------ATTIHntfAIPTNVSLPYQPL 2523
Cdd:pfam13245   13 VVLLTGGPGTGKTTTIRHI----VALLVAL--GGVSFPILLAAPTGRAAKRLSertglpASTIH---RLLGFDDLEAGGF 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1708930973 2524 KEEKVNTLRAALrdlkiLIIDEISMVDhKLLAYihGRVRQIKQsgdfapfgNVSVIAVGDFYQLPPV 2590
Cdd:pfam13245   84 LRDEEEPLDGDL-----LIVDEFSMVD-LPLAY--RLLKALPD--------GAQLLLVGDPDQLPSV 134
recD_rel TIGR01448
helicase, putative, RecD/TraA family; This model describes a family similar to RecD, the ...
 2433-2828 2.88e-12

helicase, putative, RecD/TraA family; This model describes a family similar to RecD, the exodeoxyribonuclease V alpha chain of TIGR01447. Members of this family, however, are not found in a context of RecB and RecC and are longer by about 200 amino acids at the amino end. Chlamydia muridarum has both a member of this family and a RecD. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273632 [Multi-domain]  Cd Length: 720  Bit Score: 72.89  E-value: 2.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2433 IQKWCLDTVNGHNPapfhVFLSGGAGTGKSHLIKA---LYYEATRLLArlshnpdavhVLLTAPTGVAAYNIN------A 2503
Cdd:TIGR01448  327 EQKQALDTAIQHKV----VILTGGPGTGKTTITRAiieLAEELGGLLP----------VGLAAPTGRAAKRLGevtgltA 392

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2504 TTIHNTfaiptnvsLPYQPlKEEKVNTLRAALrDLKILIIDEISMVD----HKLLAYI--HGRVrqikqsgdfapfgnvs 2577
Cdd:TIGR01448  393 STIHRL--------LGYGP-DTFRHNHLEDPI-DCDLLIVDESSMMDtwlaLSLLAALpdHARL---------------- 446

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2578 vIAVGDFYQLPPV-KGKPLytdqagIDLWGStfKHVE---LTEIVRQKNQD----FAVTLNRIRKHKKGDKLNAQDEKLL 2649
Cdd:TIGR01448  447 -LLVGDTDQLPSVgPGQVL------KDLILS--QAIPvtrLTKVYRQAAGSpiitLAHGILHGEAPAWGDFKFLNLTRSE 517

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2650 KQCQTG-VGDDTEDLHIFATNSDVDAHNFKMLHKVCSDVVQIKA-----QDFEKNPQTGRFAQKTTSHAFNkhthlsall 2723
Cdd:TIGR01448  518 PEGAARhIPLMVEKIVGMARVGGIPGADIQVLAPMYKGPLGIDAlnqhlQALLNPYQKGQGGIEIAEGEYR--------- 588

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2724 siaPNARVMLIKNiDTCDGLVNGVLGTVSLIKCDEKTKVPKLIyVKFDDDRIgsklrakfpcTVPGLQnatpvgldedkv 2803
Cdd:TIGR01448  589 ---KGDRVMQTKN-DYNNEIFNGDLGMIVKIEGAKQGKKDQVV-VDFDGNEV----------ELTRAE------------ 641

                          410       420
                   ....*....|....*....|....*
gi 1708930973 2804 pyrggirrQFPLRLAWACTIHKVQG 2828
Cdd:TIGR01448  642 --------LFNLTLAYATSIHKSQG 658
OTU_VRTN cd22791
OTU (ovarian tumor) domain of vertnin and similar proteins; Vertnin (VRTN) is an OTU ...
 1019-1107 2.41e-11

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: 63.78  E-value: 2.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1019 IDIQGDGNCFFRSLSYVFSGLESHHRTVRLAVVKHVEQNPDVYRNVVReqftsvqQYVNDSRMKyvGTWATEVEIQAAAN 1098
Cdd:cd22791      4 LRVTGDGNCLFRAASLLLFGDESLHLELRLRTVLELVLNSEFYEAIYE-------AEIKATCKP--GSYSGIWHIYALSS 74


                   ....*....
gi 1708930973 1099 LFNVDIYTY 1107
Cdd:cd22791     75 VLQRPIFSV 83
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 72-234 4.59e-10

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 61.58  E-value: 4.59e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973   72 ILVVGDShlraLVDGFVQMPEGC----LSFGFMST---------PGASAAQLRTEVEHAVLPQIPEAVCLLAPGNDLTAS 138
Cdd:COG2755     11 IVALGDS----ITAGYGASRERGwpalLARRLAAAdvrvvnagiSGATTADLLARLDRDLLALKPDLVVIELGTNDLLRG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  139 Q--TIEEAAKEFRRLLYSICKRWPN--VCVLD-FPRRLTMTM-DHQKLLSQEYHRVAARMGIRYLDTDSHFPTCHR--EL 210
Cdd:COG2755     87 LgvSPEEFRANLEALIDRLRAAGPGarVVLVTpPPRLRPNYLnERIEAYNAAIRELAAEYGVPLVDLYAALRDAGDlpDL 166

                          170       180
                   ....*....|....*....|....
gi 1708930973  211 WCSDGVHLSDsDGMPILSQLLWTA 234
Cdd:COG2755    167 LTADGLHPNA-AGYRLIAEAVLPA 189
OTU_plant_OTU6-like cd22796
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; ...
 1023-1108 2.84e-09

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: 57.44  E-value: 2.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1023 GDGNCFFRSLSYVFSGLESHHRTVRLAVVKHVEQNPDVYRNVVREQFTsvqQYVndSRMKYVGTWATEVEIQAAANLFN- 1101
Cdd:cd22796     12 GDGNCLFRAVADQVYGDQEMHDEVREMCMDYMEKERDHFSQFVTEDFT---QYV--KRKRRDRVFGNNLEIQAMSEIYNr 86


                   ....*...
gi 1708930973 1102 -VDIYTYS 1108
Cdd:cd22796     87 pIEVYSYS 94
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 72-234 4.28e-09

SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.


Pssm-ID: 238141 [Multi-domain]  Cd Length: 187  Bit Score: 58.58  E-value: 4.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973   72 ILVVGDSHLR-----ALVDGFVQMPEGCLSFGFM-------STPGASAAQL--RTEVEHAVLPQIPEAVCLLAPGNDLTA 137
Cdd:cd00229      1 ILVIGDSITAgygasSGSTFYSLLLYLLLLAGGPgvevinlGVSGATTADAlrRLGLRLALLKDKPDLVIIELGTNDLGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  138 SQ--TIEEAAKEFRRLLYSICKRWPNVCVL-----DFPRRLTMTMDHQKLLSQEYHRVAARM----GIRYLDTDSHFPTC 206
Cdd:cd00229     81 GGdtSIDEFKANLEELLDALRERAPGAKVIlitppPPPPREGLLGRALPRYNEAIKAVAAENpapsGVDLVDLAALLGDE 160

                          170       180
                   ....*....|....*....|....*...
gi 1708930973  207 HRELWCSDGVHLSDsDGMPILSQLLWTA 234
Cdd:cd00229    161 DKSLYSPDGIHPNP-AGHKLIAEALASA 187
SF1_C_RecD cd18809
C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11. ...
 2817-2862 1.01e-08

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: 54.49  E-value: 1.01e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1708930973 2817 LAWACTIHKVQGLTLEKAVV---SFKKIFSAGQAYVALSRVTSIENLII 2862
Cdd:cd18809     32 QAYAMTIHKSQGSEFDRVIVvlpTSHPMLSRGLLYTALTRARKLLTLVG 80
OTU_RDRP-like cd22792
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ...
 1017-1141 1.37e-08

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: 54.92  E-value: 1.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1017 TTIDIQGDGNCFFRSLSYvFSGLEshHRTVRLAVVKHVEQNPDVYRNVVREqftsvqqyvndsrMKYvGTWATEVEIQAA 1096
Cdd:cd22792      1 KVVPVPGDGNCFWHSLGH-FLGLS--ALELKKLLRDSLFDDPELDEELDEQ-------------LEP-GVYAEDEAIAAA 63

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1708930973 1097 ANLFNVDI--YTYSEQKWLKYGSSGAaarNKAIYIKHCNEcHYEPIE 1141
Cdd:cd22792     64 AKLFGVNIcvHDPDEGVLYTFTPNES---SKSIHLLLENE-HFEPLV 106
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
 2387-2590 5.99e-08

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: 58.62  E-value: 5.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2387 ERDVIPDLQPETTPVSIEFPKQKMSHSEAQTIMrslNELQSQVFYTIQKWCLdtvnghnpapfhVFLSGGAGTGKSHLIK 2466
Cdd:TIGR01447  113 EEKLAAKLRTLLEARKRTAPSAILENLFPLLNE---QNWRKTAVALALKSNF------------SLITGGPGTGKTTTVA 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2467 ALyyeaTRLLARLSHNPDAVHVLLTAPTGVAAYNIN----------ATTIHNTFAIPTNVSLPYQPLKEEKVNTLRAALR 2536
Cdd:TIGR01447  178 RL----LLALVKQSPKQGKLRIALAAPTGKAAARLAeslrkavknlAAAEALIAALPSEAVTIHRLLGIKPDTKRFRHHE 253

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1708930973 2537 D----LKILIIDEISMVDHKLLAYIHGRVRqikqsgdfapfGNVSVIAVGDFYQLPPV 2590
Cdd:TIGR01447  254 RnplpLDVLVVDEASMVDLPLMAKLLKALP-----------PNTKLILLGDKNQLPSV 300
TraA_Ti TIGR02768
Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a ...
 2455-2853 8.34e-08

Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a single strand exonuclease (N-terminus, MobA/MobL, pfam03389) as well as a helicase domain (central region, homologous to the corresponding region of the F-type relaxase TraI, TIGR02760). This protein likely fills the same role as TraI(F), nicking (at the oriT site) and unwinding the coiled plasmid prior to conjugative transfer.


Pssm-ID: 274289 [Multi-domain]  Cd Length: 744  Bit Score: 58.28  E-value: 8.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2455 GGAGTGKSHLIKAlyyeatrllARLSHNPDAVHVLLTAPTGVAAYNINATT-IHNTfaipTNVSLPYQpLKEEkvntlRA 2533
Cdd:TIGR02768  375 GRAGTGKSTMLKA---------AREAWEAAGYRVIGAALSGKAAEGLQAESgIESR----TLASLEYA-WANG-----RD 435

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2534 ALRDLKILIIDEISMVDHKLLAYIhgrVRQIKQSGdfapfgnVSVIAVGDFYQLPPV-KGKPL--YTDQAGidlwgstfk 2610
Cdd:TIGR02768  436 LLSDKDVLVIDEAGMVGSRQMARV---LKEAEEAG-------AKVVLVGDPEQLQPIeAGAAFraIAERIG--------- 496

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2611 HVELTEIVRQKNQ-DFAVTLNrIRKHKKGDKLNA-QDEKLLKQCQTG-------VGDDTEDLH---------IFA-TNSD 2671
Cdd:TIGR02768  497 YAELETIRRQREAwARQASLE-LARGDVEKALAAyRDHGHITIHDTReeaieqvVADWKQDLReanpagsqiMLAhTRKD 575

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2672 VDAHNfkmlhkvcsDVVQIKAQDFEKNPQTGRFAQKTTSHAFnkhthlsallsiAPNARVMLIKNiDTCDGLVNGVLGTV 2751
Cdd:TIGR02768  576 VRALN---------EAAREALIERGELGESILFQTARGERKF------------AAGDRIVFLEN-NRDLGVKNGMLGTV 633

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2752 SLIkcdektkvpkliyvkfDDDRIGSKLrakfpctvpGLQNATPVGLDE-DKVPYrggirrqfplrlAWACTIHKVQGLT 2830
Cdd:TIGR02768  634 EEI----------------EDGRLVVQL---------DSGELVIIPQAEyDALDH------------GYATTIHKSQGVT 676

                          410       420
                   ....*....|....*....|...
gi 1708930973 2831 LEKAVVSFKKIFSAGQAYVALSR 2853
Cdd:TIGR02768  677 VDRAFVLASKSMDRHLAYVAMTR 699
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
 1019-1139 2.13e-07

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: 52.60  E-value: 2.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1019 IDIQGDGNCFFRSLSYVFSGLESHHRTVRLAVVKHVEQNPDVYRNVVReQFTSVQQYVNDSrMKyVGTWA--TEVEIQAA 1096
Cdd:cd21880     25 ERVPGDGNCFFRSIAELLFDTEDEWRLVKNTIESYARANWDECPEARL-YYLSLEEYLRDA-MK-DGYWGgsLEAEILSK 101

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1708930973 1097 AnlFNVDIYTYSE--QKWL----KYGSSGAAArnkAIYIKHCNEcHYEP 1139
Cdd:cd21880    102 A--LGITIIIWVVddSDWVtaavRFGDGDVST---SLNLLHSGG-HFDA 144
OTU_fungi_OTU2-like cd22762
OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; ...
 1020-1131 2.81e-07

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: 52.23  E-value: 2.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1020 DIQGDGNCFFRS----LSYVFSGLESHHRTVRLAVVKHVEQNPDVYRNVVREQFTSVQ---QYVNdsRMKYVGTWATEVE 1092
Cdd:cd22762     11 DIKPDGHCLFAAiadqLQLRGSEINLDYKELRKLAAEYIRKHPDDFEPFLFEETDELEdidEYCK--KIENTAEWGGELE 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1708930973 1093 IQAAANLFNVDIYTY-SEQKWLKYGSSGaAARNKAIYI---KH 1131
Cdd:cd22762     89 LLALAKAFGVPIHVVqAEGRVIKINEEG-DSDKPELWLayyKH 130
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 103-220 3.56e-07

GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are similar to pfam00657.


Pssm-ID: 463889  Cd Length: 176  Bit Score: 52.93  E-value: 3.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  103 PGASAAQLRTEVEHAVLPQIPEAVCLLAPGNDLTASQTIEEAAKEFRRLLYSICKRWPNVCVLD---------FPRRLTM 173
Cdd:pfam13472   42 SGATTRLDLLERLDDVLRLKPDLVVILLGTNDLGRGVSAARAAANLEALIDALRAAGPDARVLLigplpvgppPPLDERR 121

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1708930973  174 TMDHQKLLSQEYHRVAARMGIRYLDTDSHF---PTCHRELWCSDGVHLSD 220
Cdd:pfam13472  122 LNARIAEYNAAIREVAAERGVPYVDLWDALrddGGWLPDLLADDGLHPNA 171
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 2904-3059 5.35e-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: 52.61  E-value: 5.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2904 NIQGLQAHIADLKHDRRML-------DADLLCLTETWLQHNTAQGNIDMAGWTFHCKARSQSYSNQgafsalqkqqhGGV 2976
Cdd:pfam03372    4 NVNGGNADAAGDDRKLDALaalirayDPDVVALQETDDDDASRLLLALLAYGGFLSYGGPGGGGGG-----------GGV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2977 GFYHKNHIISNIIN---------LPCSELEAIIFNIQPMNHNYIVLYRPPSYQISLFKQNLSAVVSHFNALSGGKIIMGD 3047
Cdd:pfam03372   73 AILSRYPLSSVILVdlgefgdpaLRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGD 152

                          170
                   ....*....|...
gi 1708930973 3048 FN-DNAVVSKSME 3059
Cdd:pfam03372  153 FNaDYILVSGGLT 165
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
 1021-1109 6.67e-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: 50.83  E-value: 6.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1021 IQGDGNCFFRSLSYVFSGLESHHRTVRLAVVKHVEQNPDVYrnvvrEQF--TSVQQYVndSRMKYVGTWATEVEIQAAAN 1098
Cdd:cd22794     15 IAKDGSCLFRAVAEQVFHTQSRHLEVRKACVDYLRRNREKF-----EAFieGPFEQYL--KNLENPKEWAGQVEISALSL 87

                           90
                   ....*....|.
gi 1708930973 1099 LFNVDIYTYSE 1109
Cdd:cd22794     88 MYKRDFIIYQE 98
OTU_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
 1020-1123 1.99e-06

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: 49.87  E-value: 1.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1020 DIQGDGNCFFRSLSYVF-----SGLESHHRTVRLAVVKHVEQNPDVYRNVVREQFTS------VQQYVNdsRMKYVGTWA 1088
Cdd:cd22748     10 EIPPDGHCLYRAIADQLklrggSEEPYSYKELRKLAADYMRAHRDDFLPFLTNDDGDlmteeeFEEYCD--KIENTAEWG 87

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1708930973 1089 TEVEIQAAANLFNVDIYTY-SEQKWLKYGSSGAAAR 1123
Cdd:cd22748     88 GQLELRALSKALKRPIHVYqAGSPPLVIGEEFDSGE 123
OTU_OTUD3 cd22770
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU ...
 1020-1147 1.19e-05

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: 47.67  E-value: 1.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1020 DIQGDGNCFFRSLSYVFSGLESHHRTVRLAVVKHVEQNPDVYRNVVrEQFTSVQQYVNDsrMKYVGTWATEVEIQAAANL 1099
Cdd:cd22770     18 DIPGDGNCLFRALGDQLEGHSRNHLKHRQETVQYMIEHREDFEPFV-EDDVPFDKHVAN--LSKPGTYAGNDAIVAFARL 94

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1100 --FNVDIYTYSEQKWLKYGSSGAAARNkaIYIKHCNECHYEPIECVKDIS 1147
Cdd:cd22770     95 hqVNVVIHQLNAPLWQIRGTEKSSSRE--LHISYHNGDHYSSVRKLGDNS 142
COG5539 COG5539
Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, ...
 1008-1131 2.24e-05

Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227826 [Multi-domain]  Cd Length: 306  Bit Score: 49.10  E-value: 2.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1008 LDIEQPQPCTTI---DIQGDGNCFFRSLSyvfSGLESHHRTVRLAVVKHVEQNPDVYRNVVREQFTS------------V 1072
Cdd:COG5539    160 LEIDVIAYATWIvkpDSQGDGCIEIAIIS---DQLPVRIHVVDVDKDSEDRYNSHPYVQRISILFTGihfdeetlamvlW 236

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1073 QQYVNDsrMKYVGTWATEVEIQAAANLFNVDIYTY-SEQKWLKYGSSGAAARNKAIYIKH 1131
Cdd:COG5539    237 DTYVNE--VLFDASDGITIEIQQLASLLKNPHYYTnTASPSIKCNICGTGFVGEKDYYAH 294
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 2450-2581 2.95e-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: 46.60  E-value: 2.95e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  2450 HVFLSGGAGTGKSHLIKAlyyeatrlLARLShNPDAVHVLLTAPTGVAAYNINATTIHNTFAIPTNVSlpyqplKEEKVN 2529
Cdd:smart00382    4 VILIVGPPGSGKTTLARA--------LAREL-GPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS------GELRLR 68

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1708930973  2530 TLRAALR--DLKILIIDEISMVDHKLLAYIHGRVRQIKQSGDFAPFGNVSVIAV 2581
Cdd:smart00382   69 LALALARklKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILT 122
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 2445-2581 3.55e-05

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: 46.37  E-value: 3.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2445 NPAPFHVFLSGGAGTGKSHLIKALYYEATRLLARLshnpdavhvlltaptgvaaYNINATTIHNTFAIptnvsLPYQPLK 2524
Cdd:cd00009     16 LPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPF-------------------LYLNASDLLEGLVV-----AELFGHF 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1708930973 2525 EEKVNTLRAALRDLKILIIDEIsmvdHKLLAYIHGRVRQI--KQSGDFAPFGNVSVIAV 2581
Cdd:cd00009     72 LVRLLFELAEKAKPGVLFIDEI----DSLSRGAQNALLRVleTLNDLRIDRENVRVIGA 126
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
 2803-2853 7.40e-05

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: 43.97  E-value: 7.40e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1708930973 2803 VPYRGGIRR-----------QFPLRLAWACTIHKVQGLTLEKA--VVSFKKIFSAGQAYVALSR 2853
Cdd:cd18786     17 TPYHRDRAYlnqylqglsldEFDLQLVGAITIDSSQGLTFDVVtlYLPTANSLTPRRLYVALTR 80
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 1022-1161 8.18e-05

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: 44.75  E-value: 8.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1022 QGDGNCFFRSLS----YVFSGLESH-HRTVRLAVVkhveqnpdvyrNVVREQFTSVQQYVNDSRMKYV------GTWATE 1090
Cdd:pfam02338    1 PGDGNCLYRSIShqlwGVHDVLRKMlVQELRETLA-----------EYMREHKEEFEPFLEDDETGDIieieqtGAWGGE 69

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708930973 1091 VEIQAAANLFNVDIYTYseqkwlkYGSSGAAARNKAIYiKHCNECHYEPIECVKdisgkcfSLRTLGETNH 1161
Cdd:pfam02338   70 IEIFALAHILRRPIIVY-------KSEGGEELGGLKEY-GIYLPLGWDPSLCLV-------YPRHLYYLGG 125
PHA03311 PHA03311
helicase-primase subunit BBLF4; Provisional
 2820-2862 1.05e-04

helicase-primase subunit BBLF4; Provisional


Pssm-ID: 223040  Cd Length: 782  Bit Score: 47.98  E-value: 1.05e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1708930973 2820 ACTIHKVQGLTLEKAVVSF---KKIfSAGQAYVALSRVTSIENLII 2862
Cdd:PHA03311   706 AMTIAKSQGLSLDKVAICFgnhKNL-KLSHVYVAMSRVTSSNFLVM 750
AAA_22 pfam13401
AAA domain;
2450-2558 1.15e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 44.25  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2450 HVFLSGGAGTGKSHLIKalyyeatRLLARL-SHNPDAVHVLLTAPTGVAAYninATTIHNTFAIPTNVSLPYQPLKEEKV 2528
Cdd:pfam13401    7 ILVLTGESGTGKTTLLR-------RLLEQLpEVRDSVVFVDLPSGTSPKDL---LRALLRALGLPLSGRLSKEELLAALQ 76

                           90       100       110
                   ....*....|....*....|....*....|
gi 1708930973 2529 NTLRaALRDLKILIIDEISMVDHKLLAYIH 2558
Cdd:pfam13401   77 QLLL-ALAVAVVLIIDEAQHLSLEALEELR 105
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
2368-2582 2.45e-04

Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 46.38  E-value: 2.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2368 LERLESVEEMTANKDLfpterdvipdLQPETTPVSIEfpkqkmsHSEAQtimrsLNELQSQVfytiqkwcLDTVNGHNPa 2447
Cdd:COG1474      3 FEDLLWDESIFRDREV----------LSPDYVPDRLP-------HREEE-----IEELASAL--------RPALRGERP- 51

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2448 pFHVFLSGGAGTGKSHLIKALYYEATRLLARLSHNPDAVHVlltaptgvaayniNATTIHNTFAI--------PTNVSLP 2519
Cdd:COG1474     52 -SNVLIYGPTGTGKTAVAKYVLEELEEEAEERGVDVRVVYV-------------NCRQASTRYRVlsrileelGSGEDIP 117

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1708930973 2520 YQPL-KEEKVNTLRAALRDLK---ILIIDEISMVDHKLLAYIhgrVRQIKQSGDFAPFGNVSVIAVG 2582
Cdd:COG1474    118 STGLsTDELFDRLYEALDERDgvlVVVLDEIDYLVDDEGDDL---LYQLLRANEELEGARVGVIGIS 181
OTU_OTUD1 cd22747
OTU (ovarian tumor) domain of OTU domain-containing protein 1 and similar proteins; OTU ...
 1021-1105 3.22e-04

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: 43.65  E-value: 3.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1021 IQGDGNCFFRSLSYVFSGLESHHRTVRLAVVKHVEQNPDVYRNVVReqfTSVQQYVNDSRMKyvGTWATEVEIQAAANLF 1100
Cdd:cd22747     26 IIPDGNCLYRAVSKAVYGDQALHRELREQTVHYIADHLDEFNPIIE---GDVGEFLIKAAQD--GAWAGYPELLAMGQML 100


                   ....*
gi 1708930973 1101 NVDIY 1105
Cdd:cd22747    101 NVNIR 105
Herpes_Helicase pfam02689
Helicase; This family consists of Helicases from the Herpes viruses. Helicases are responsible ...
 2820-2862 5.18e-04

Helicase; This family consists of Helicases from the Herpes viruses. Helicases are responsible for the unwinding of DNA and are essential for replication and completion of the viral life cycle.


Pssm-ID: 280797  Cd Length: 809  Bit Score: 45.86  E-value: 5.18e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1708930973 2820 ACTIHKVQGLTLEKAVVSF---KKIfSAGQAYVALSRVTSIENLII 2862
Cdd:pfam02689  733 AMTIAKSQGLSLDKVAICFgnhPNL-KLSHVYVAMSRATDPNHLVM 777
SGNH_hydrolase_like_7 cd04502
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 72-231 5.77e-04

Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.


Pssm-ID: 239946  Cd Length: 171  Bit Score: 43.43  E-value: 5.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973   72 ILVVGDSHLR---ALVDGFVQMPEGCLSFGfmstpGASAAQLRTEVEHAVLPQIPEAVCLLAPGNDLTASQTIEEAAKEF 148
Cdd:cd04502      2 ILFYGSSSIRlwdTLADDLAPLPVVNRGFG-----GSTLADCLHYFDRLVLPYQPRRVVLYAGDNDLASGRTPEEVLRDF 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  149 RRLLYSICKRWPNVCVLDF-----PRRLTMTMDHQKL--LSQEYhrVAARMGIRYLDTDSHFPT----CHRELWCSDGVH 217
Cdd:cd04502     77 RELVNRIRAKLPDTPIAIIsikpsPARWALRPKIRRFnaLLKEL--AETRPNLTYIDVASPMLDadgkPRAELFQEDGLH 154

                          170
                   ....*....|....
gi 1708930973  218 LSDSdGMPILSQLL 231
Cdd:cd04502    155 LNDA-GYALWRKVI 167
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
 2458-2590 6.86e-04

DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong to 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: 438708 [Multi-domain]  Cd Length: 121  Bit Score: 41.84  E-value: 6.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2458 GTGKSHLIKALyyeatrlLARLSHNPDAVHVLLTAPTGVAayninattihntfaiptnvslpyqplkeekVNTLRaalrd 2537
Cdd:cd17934      9 GTGKTTTIAAI-------VLQLLKGLRGKRVLVTAQSNVA------------------------------VDNVD----- 46

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1708930973 2538 lkILIIDEISMVDH-KLLAYIHgRVRQikqsgdfapfgnvsVIAVGDFYQLPPV 2590
Cdd:cd17934     47 --VVIIDEASQITEpELLIALI-RAKK--------------VVLVGDPKQLPPV 83
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 104-234 1.10e-03

Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. Myxobacterial members of this subfamily have been reported to be involved in adventurous gliding motility.


Pssm-ID: 238870  Cd Length: 185  Bit Score: 42.64  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  104 GASAAQLRTEVEHAVLPQIPEAVCLLAPGND-LTASQTIEEAAKEFRRLLYSICKRWPNVCVLDFP------RRLTMTMD 176
Cdd:cd01832     49 GRRTAQILAEQLPAALALRPDLVTLLAGGNDiLRPGTDPDTYRADLEEAVRRLRAAGARVVVFTIPdpavlePFRRRVRA 128

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1708930973  177 HQKLLSQEYHRVAARMGIRYLDTDSHFPTCHRELWCSDGVHLSdSDGMPILSQLLWTA 234
Cdd:cd01832    129 RLAAYNAVIRAVAARYGAVHVDLWEHPEFADPRLWASDRLHPS-AAGHARLAALVLAA 185
SGNH pfam19040
SGNH domain (fused to AT3 domains); This entry include SGNH domains that are found fused to ...
 67-221 1.13e-03

SGNH domain (fused to AT3 domains); This entry include SGNH domains that are found fused to membrane domains from the AT3 families pfam01757.


Pssm-ID: 436916  Cd Length: 245  Bit Score: 43.44  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973   67 PDKKFILVVGDSHLRALVDGFVQMPE------------GCLSFGFMSTPGASAAQLRTEVEH-AVLPQIPEAVCLLA--- 130
Cdd:pfam19040   22 AGPPSVLLWGDSHAAALAPGLDEAAKergvsvlqitrsGCPPLLLRLPDAACAAFNAAILEAlALLPSKPDTVVLAArws 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  131 ----------PGNDLTASQTIEEAAKEFRR-------------LLYSI--CKRWPNVCV--LDFPRRLTMTMDHQKLLSQ 183
Cdd:pfam19040  102 lylegpafndEGIGRDLSNTIAAFAAALRAtvaalaaagkkvvLLGPVpeYVPRNARCLarAGGLLRDPLCSIPRAEYRA 181

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1708930973  184 EYHRVAARM--------GIRYLDTDSHFptCHRELWCS---------DGVHLSDS 221
Cdd:pfam19040  182 RNARVNAALdelaakpgKVRVIDPSPLF--CDDGGRCSaldgtplyfDDNHLSPA 234
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
2445-2546 1.68e-03

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


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 43.26  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2445 NPapfhVFLSGGAGTGKSHLIKALYYEAtrllarLSHNPDAVHVLLTAPTGVAAYnINAttihntfaiptnvslpyqpLK 2524
Cdd:COG0593     35 NP----LFLYGGVGLGKTHLLHAIGNEA------LENNPGARVVYLTAEEFTNDF-INA-------------------IR 84

                           90       100
                   ....*....|....*....|..
gi 1708930973 2525 EEKVNTLRAALRDLKILIIDEI 2546
Cdd:COG0593     85 NNTIEEFKEKYRSVDVLLIDDI 106
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 123-220 1.72e-03

sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.


Pssm-ID: 238866  Cd Length: 169  Bit Score: 41.88  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  123 PEAVCLLAPGNDLTASQTIEEAAKEFRRLLYSICKRWPN----VCVLdFPRRLTMTMDHQKL--LSQEYHRVAARMGIRY 196
Cdd:cd01828     49 PKAIFIMIGINDLAQGTSDEDIVANYRTILEKLRKHFPNikivVQSI-LPVGELKSIPNEQIeeLNRQLAQLAQQEGVTF 127

                           90       100
                   ....*....|....*....|....*..
gi 1708930973  197 LDTDSHFPTCHREL---WCSDGVHLSD 220
Cdd:cd01828    128 LDLWAVFTNADGDLkneFTTDGLHLNA 154
L1-EN cd09076
Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; ...
 2900-3056 2.20e-03

Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; This family contains the endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains, including the endonuclease of Xenopus laevis Tx1. These retrotranspons belong to the subtype 2, L1-clade. LINES can be classified into two subtypes. Subtype 2 has two ORFs: the second (ORF2) encodes a modular protein consisting of an N-terminal apurine/apyrimidine endonuclease domain (EN), a central reverse transcriptase, and a zinc-finger-like domain at the C-terminus. LINE-1/L1 elements (full length and truncated) comprise about 17% of the human genome. This endonuclease nicks the genomic DNA at the consensus target sequence 5'TTTT-AA3' producing a ribose 3'-hydroxyl end as a primer for reverse transcription of associated template RNA. This subgroup also includes the endonuclease of Xenopus laevis Tx1, another member of the L1-clade. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197310 [Multi-domain]  Cd Length: 236  Bit Score: 42.34  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2900 VCLLNIQGL--QAHIADLKHDRRMLDADLLCLTETWLQHNTAQGNIDMAGWTFhckarsqsysnqgaFSALQKQQHGGVG 2977
Cdd:cd09076      1 IGTLNVRGLrsPGKRAQLLEELKRKKLDILGLQETHWTGEGELKKKREGGTIL--------------YSGSDSGKSRGVA 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 2978 FYHKNHIISNIINLPCSELEAII---FNIQPMNHNYIVLYRPPSYQ---ISLFKQNLSAVVSHFNAlSGGKIIMGDFndN 3051
Cdd:cd09076     67 ILLSKTAANKLLEYTKVVSGRIImvrFKIKGKRLTIINVYAPTARDeeeKEEFYDQLQDVLDKVPR-HDTLIIGGDF--N 143


                   ....*
gi 1708930973 3052 AVVSK 3056
Cdd:cd09076    144 AVLGP 148
OTU_OTU1 cd22745
OTU (ovarian tumor) domain of ubiquitin thioesterase OTU1 and similar proteins; Ubiquitin ...
 1024-1106 2.50e-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: 41.32  E-value: 2.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1024 DGNCFFRSLSYVFSG-LESHHRTVRLAVVKHVEQNPDVYRNVVREQftSVQQYVN-----DSrmkyvgtWATEVEIQAAA 1097
Cdd:cd22745     11 DNSCLFTSISYLLEGgLLDSAPELREIVADAILSDPDTYNEAILGK--PPDEYCAwilkpDS-------WGGAIELSILS 81


                   ....*....
gi 1708930973 1098 NLFNVDIYT 1106
Cdd:cd22745     82 KHFGVEICV 90
OTU_ALG13 cd22795
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 1024-1107 3.03e-03

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: 40.18  E-value: 3.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973 1024 DGNCFFRSLSYVFSGLESHHRTVRLAVVKHVEQNPDVYRNVVREQFTSVQQYVNDSRmkyvgTWATEVEIQAAANLFNVD 1103
Cdd:cd22795     18 DASCLFRAVSEQLFLCQIHHLEIRKACVSYMRANQCNFESYVEGSFEKYLERLEDPK-----ESAGQLEISALSLIYNRD 92


                   ....
gi 1708930973 1104 IYTY 1107
Cdd:cd22795     93 FILY 96
Herpes_teg_N pfam04843
Herpesvirus tegument protein, N-terminal conserved region;
702-877 7.83e-03

Herpesvirus tegument protein, N-terminal conserved region;


Pssm-ID: 461453 [Multi-domain]  Cd Length: 183  Bit Score: 40.18  E-value: 7.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  702 SFNQGNPRFGENKGKQCATNSITAVMTNVLKSAWTWTTTD-LDNVLVNGNDLYTyvkDKHKVSVLEGKGYILVKELPtEY 780
Cdd:pfam04843    1 SRNQFDCKFGPRAGSQCLSNCVSFLHSSYLNGINPVLSREaLDAVLEEGARLDT---LLRTSGRLPPRQYAQLHEIP-GI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708930973  781 ELLDKKFCLEYMES----LSGHIDVEEYHPAVQDYVMPLDVAFQRAMLNADA------CLLNIKKNICAVLKQRDQFAVF 850
Cdd:pfam04843   77 IITGAWGCLIYRSSeiygLLGHELSRNFNGTPQTGDIDTQMPAGIFFRYAKAkrrpsyTLIICNSLAMAIVIKDKTYYLF 156

                          170       180
                   ....*....|....*....|....*..
gi 1708930973  851 DPHArgadgglQHDGTSIVACYDTLDA 877
Cdd:pfam04843  157 DPHC-------TPEGNSTAAVIVTVDA 176
 
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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