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Conserved domains on  [gi|2031263991|ref|NP_001381631|]
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PAN2-PAN3 deadenylation complex catalytic subunit PAN2 isoform 4 [Homo sapiens]

Protein Classification

PAN2-PAN3 deadenylation complex catalytic subunit PAN2( domain architecture ID 13237162)

PAN2-PAN3 deadenylation complex catalytic subunit PAN2 is the catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
517-893 6.33e-115

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 359.66  E-value: 6.33e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  517 AGLEPHIPNAYCNCMIQVLYFLEPVRCLIQNHL---CQKEFCLACELGFLFHMLDLSRGDPCQGNNFLRAFRTIPEASAL 593
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLateCLKEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIPEASAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  594 GLIlADSDEASGKGNLARLIQRWNRFILTQLHQDMQELEIPQayrgaggsfcSSGDSVIGQLFSCEMENCSLC-RCGSET 672
Cdd:pfam13423   81 GLL-DEDRETNSAISLSSLIQSFNRFLLDQLSSEENSTPPNP----------SPAESPLEQLFGIDAETTIRCsNCGHES 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  673 VRASSTLLFTLSYP-----DDKTGKNYDFAQVLKRSICLDQNTQAWCDTCEKYQPTIQTRNIRHLPDILVINCEVNSSKE 747
Cdd:pfam13423  150 VRESSTHVLDLIYPrkpssNNKKPPNQTFSSILKSSLERETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEW 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  748 ADFWRmqaevafkmavkkhggeisknkefaladwkelgspegvlvcpsieelKNVWLPFSIRMKMTKNKGLDvcnwtdgd 827
Cdd:pfam13423  230 RQLWK-----------------------------------------------TPGWLPPEIGLTLSDDLQGD-------- 254
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2031263991  828 emqwgparaeeeHGVYVYDLMATVVHILDSRTGGSLVAHIKVGETYHqrkEGVTHQQWYLFNDFLI 893
Cdd:pfam13423  255 ------------NEIVKYELRGVVVHIGDSGTSGHLVSFVKVADSEL---EDPTESQWYLFNDFLV 305
PAN2_exo cd06143
DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonuclease PAN2; PAN2 is the catalytic ...
970-1143 1.50e-114

DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonuclease PAN2; PAN2 is the catalytic subunit of poly(A) nuclease (PAN), a Pab1p-dependent 3'-5' exoribonuclease which plays an important role in the posttranscriptional maturation of pre-mRNAs. PAN catalyzes the deadenylation of poly(A) tails, which are initially synthesized to default lengths of 70 to 90, to mRNA-specific lengths of 55 to 71. Pab1p and PAN also play a role in the export and decay of mRNA. PAN2 contains a DEDDh-type DnaQ-like 3'-5' exonuclease domain with three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis.


:

Pssm-ID: 99846  Cd Length: 174  Bit Score: 353.46  E-value: 1.50e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  970 VGLDAEFVTLNEEEAELRSDGTKSTIKPSQMSVARITCVRGQGPNEGIPFIDDYISTQEQVVDYLTQYSGIKPGDLDAKI 1049
Cdd:cd06143      1 VAIDAEFVKLKPEETEIRSDGTKSTIRPSQMSLARVSVVRGEGELEGVPFIDDYISTTEPVVDYLTRFSGIKPGDLDPKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991 1050 SSKHLTTLKSTYLKLRFLIDIGVKFVGHGLQKDFRVINLMVPKDQVLDTVYLFHMPRKRMISLRFLAWYFLDLKIQGETH 1129
Cdd:cd06143     81 SSKNLTTLKSAYLKLRLLVDLGCIFVGHGLAKDFRVINIQVPKEQVIDTVELFHLPGQRKLSLRFLAWYLLGEKIQSETH 160
                          170
                   ....*....|....
gi 2031263991 1130 DSIEDARTALQLYR 1143
Cdd:cd06143    161 DSIEDARTALKLYR 174
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
204-357 9.01e-04

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 42.71  E-value: 9.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  204 QTNRFFFCGHTSGKVSLRDLRTFKVEHEFDAFSGSLSDFDVH--GNLLAACGfssrltglaCDRFLKVYDLRMMRAITPL 281
Cdd:cd00200    145 PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSpdGEKLLSSS---------SDGTIKLWDLSTGKCLGTL 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  282 QVHVDPA-FLRFIPtytSRLAIIS------------QSGQCQFCeptgLANpadifHVNPVGpllmTFDVSASKQALAFG 348
Cdd:cd00200    216 RGHENGVnSVAFSP---DGYLLASgsedgtirvwdlRTGECVQT----LSG-----HTNSVT----SLAWSPDGKRLASG 279

                   ....*....
gi 2031263991  349 DSEGCVHLW 357
Cdd:cd00200    280 SADGTIRIW 288
 
Name Accession Description Interval E-value
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
517-893 6.33e-115

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 359.66  E-value: 6.33e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  517 AGLEPHIPNAYCNCMIQVLYFLEPVRCLIQNHL---CQKEFCLACELGFLFHMLDLSRGDPCQGNNFLRAFRTIPEASAL 593
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLateCLKEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIPEASAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  594 GLIlADSDEASGKGNLARLIQRWNRFILTQLHQDMQELEIPQayrgaggsfcSSGDSVIGQLFSCEMENCSLC-RCGSET 672
Cdd:pfam13423   81 GLL-DEDRETNSAISLSSLIQSFNRFLLDQLSSEENSTPPNP----------SPAESPLEQLFGIDAETTIRCsNCGHES 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  673 VRASSTLLFTLSYP-----DDKTGKNYDFAQVLKRSICLDQNTQAWCDTCEKYQPTIQTRNIRHLPDILVINCEVNSSKE 747
Cdd:pfam13423  150 VRESSTHVLDLIYPrkpssNNKKPPNQTFSSILKSSLERETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEW 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  748 ADFWRmqaevafkmavkkhggeisknkefaladwkelgspegvlvcpsieelKNVWLPFSIRMKMTKNKGLDvcnwtdgd 827
Cdd:pfam13423  230 RQLWK-----------------------------------------------TPGWLPPEIGLTLSDDLQGD-------- 254
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2031263991  828 emqwgparaeeeHGVYVYDLMATVVHILDSRTGGSLVAHIKVGETYHqrkEGVTHQQWYLFNDFLI 893
Cdd:pfam13423  255 ------------NEIVKYELRGVVVHIGDSGTSGHLVSFVKVADSEL---EDPTESQWYLFNDFLV 305
PAN2_exo cd06143
DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonuclease PAN2; PAN2 is the catalytic ...
970-1143 1.50e-114

DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonuclease PAN2; PAN2 is the catalytic subunit of poly(A) nuclease (PAN), a Pab1p-dependent 3'-5' exoribonuclease which plays an important role in the posttranscriptional maturation of pre-mRNAs. PAN catalyzes the deadenylation of poly(A) tails, which are initially synthesized to default lengths of 70 to 90, to mRNA-specific lengths of 55 to 71. Pab1p and PAN also play a role in the export and decay of mRNA. PAN2 contains a DEDDh-type DnaQ-like 3'-5' exonuclease domain with three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis.


Pssm-ID: 99846  Cd Length: 174  Bit Score: 353.46  E-value: 1.50e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  970 VGLDAEFVTLNEEEAELRSDGTKSTIKPSQMSVARITCVRGQGPNEGIPFIDDYISTQEQVVDYLTQYSGIKPGDLDAKI 1049
Cdd:cd06143      1 VAIDAEFVKLKPEETEIRSDGTKSTIRPSQMSLARVSVVRGEGELEGVPFIDDYISTTEPVVDYLTRFSGIKPGDLDPKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991 1050 SSKHLTTLKSTYLKLRFLIDIGVKFVGHGLQKDFRVINLMVPKDQVLDTVYLFHMPRKRMISLRFLAWYFLDLKIQGETH 1129
Cdd:cd06143     81 SSKNLTTLKSAYLKLRLLVDLGCIFVGHGLAKDFRVINIQVPKEQVIDTVELFHLPGQRKLSLRFLAWYLLGEKIQSETH 160
                          170
                   ....*....|....
gi 2031263991 1130 DSIEDARTALQLYR 1143
Cdd:cd06143    161 DSIEDARTALKLYR 174
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
502-916 5.34e-82

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 269.00  E-value: 5.34e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  502 GLEDFDFKHYNKTLFAGLEPHIPNAYCNCMIQVLYFLEPVRC--LIQNHLCQKEFCLACELGFLFhmldlsrgdpcqgnn 579
Cdd:cd02672      1 GTEDFDFEFYNKTNYAGLENHITNSYCNSLLQLLYFIPPFRNftAIILVACPKESCLLCELGYLF--------------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  580 flrafrtipeasalgliladsdeasgkgnlarliqrwnrfiltqlhqdmqeleipqayrgaggsfcssgdSVIGQLFSCE 659
Cdd:cd02672     66 ----------------------------------------------------------------------STLIQNFTRF 75
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  660 MENCSLCRCG-----SETVRASSTLLFTLSYPDD--KTGKNYDFAQVLKRSICLDQNTQAWCDTCEKYQPTIQTRNIRHL 732
Cdd:cd02672     76 LLETISQDQLgtpfsCGTSRNSVSLLYTLSLPLGstKTSKESTFLQLLKRSLDLEKVTKAWCDTCCKYQPLEQTTSIRHL 155
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  733 PDILvincevnsskeadfwrmqaevafkmavkkhggeisknkefaladwkelgspegvlvcpsieelknvWLPFSIRMKM 812
Cdd:cd02672    156 PDIL------------------------------------------------------------------LLVLVINLSV 169
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  813 TKNKGLDV-CNWTDGDEMQWGPARAEEEH----------GVYVYDLMATVVHILDSrtggSLVAHIKVGETYHQRKegVT 881
Cdd:cd02672    170 TNGEFDDInVVLPSGKVMQNKVSPKAIDHdklvknrgqeSIYKYELVGYVCEINDS----SRGQHNVVFVIKVNEE--ST 243
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 2031263991  882 HQQWYLFNDFLIEPIDkheavqfdmnwKVPAILYY 916
Cdd:cd02672    244 HGRWYLFNDFLVTPVS-----------ELAYILLY 267
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
969-1147 3.72e-26

exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;


Pssm-ID: 214685 [Multi-domain]  Cd Length: 169  Bit Score: 106.23  E-value: 3.72e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991   969 LVGLDAEFVTLNEEEAELrsdgtkstikpsqmsvARITCVRGQGPNEGIPFiDDYISTQEQVVDYLTQYSGIKPGDLDAK 1048
Cdd:smart00479    2 LVVIDCETTGLDPGKDEI----------------IEIAAVDVDGGEIIEVF-DTYVKPDRPITDYATEIHGITPEMLDDA 64
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  1049 IsskhltTLKSTYLKLRFLIDIGVKFVGHGLQKDFRVINLMVPK--------DQVLDTVYLFHM--PRKRMISLRFLAWY 1118
Cdd:smart00479   65 P------TFEEVLEELLEFLRGRILVAGNSAHFDLRFLKLEHPRlgikqppkLPVIDTLKLARAtnPGLPKYSLKKLAKR 138
                           170       180
                    ....*....|....*....|....*....
gi 2031263991  1119 FLdLKIQGETHDSIEDARTALQLYRKYLE 1147
Cdd:smart00479  139 LL-LEVIQRAHRALDDARATAKLFKKLLE 166
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
970-1142 9.94e-19

Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T and the epsilon subunit of DNA polymerase III.;


Pssm-ID: 395743 [Multi-domain]  Cd Length: 164  Bit Score: 84.71  E-value: 9.94e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  970 VGLDAEFVTLNEEEAELrsdgtkstikpsqMSVARITCVRGQgpNEGIPFIDDYISTQE--QVVDYLTQYSGIKPGDLDA 1047
Cdd:pfam00929    1 VVIDLETTGLDPEKDEI-------------IEIAAVVIDGGE--NEIGETFHTYVKPTRlpKLTDECTKFTGITQAMLDN 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991 1048 KISSKH-LTTLKSTYLKLRFLIDIGVKF-VGHGLQKDFRVINLMVPK-DQVLDTVYLFHMPRKRM--ISLRFLAWYFlDL 1122
Cdd:pfam00929   66 KPSFEEvLEEFLEFLRKGNLLVAHNASFdVGFLRYDDKRFLKKPMPKlNPVIDTLILDKATYKELpgRSLDALAEKL-GL 144
                          170       180
                   ....*....|....*....|
gi 2031263991 1123 KIQGETHDSIEDARTALQLY 1142
Cdd:pfam00929  145 EHIGRAHRALDDARATAKLF 164
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
204-357 9.01e-04

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 42.71  E-value: 9.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  204 QTNRFFFCGHTSGKVSLRDLRTFKVEHEFDAFSGSLSDFDVH--GNLLAACGfssrltglaCDRFLKVYDLRMMRAITPL 281
Cdd:cd00200    145 PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSpdGEKLLSSS---------SDGTIKLWDLSTGKCLGTL 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  282 QVHVDPA-FLRFIPtytSRLAIIS------------QSGQCQFCeptgLANpadifHVNPVGpllmTFDVSASKQALAFG 348
Cdd:cd00200    216 RGHENGVnSVAFSP---DGYLLASgsedgtirvwdlRTGECVQT----LSG-----HTNSVT----SLAWSPDGKRLASG 279

                   ....*....
gi 2031263991  349 DSEGCVHLW 357
Cdd:cd00200    280 SADGTIRIW 288
PRK07247 PRK07247
3'-5' exonuclease;
1122-1151 9.36e-03

3'-5' exonuclease;


Pssm-ID: 180906 [Multi-domain]  Cd Length: 195  Bit Score: 38.61  E-value: 9.36e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2031263991 1122 LKIQGETHDSIEDARTALQLYRKYLELSKN 1151
Cdd:PRK07247   142 LGIKGRGHNSLEDARMTARVYESFLESDQN 171
 
Name Accession Description Interval E-value
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
517-893 6.33e-115

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 359.66  E-value: 6.33e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  517 AGLEPHIPNAYCNCMIQVLYFLEPVRCLIQNHL---CQKEFCLACELGFLFHMLDLSRGDPCQGNNFLRAFRTIPEASAL 593
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLateCLKEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIPEASAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  594 GLIlADSDEASGKGNLARLIQRWNRFILTQLHQDMQELEIPQayrgaggsfcSSGDSVIGQLFSCEMENCSLC-RCGSET 672
Cdd:pfam13423   81 GLL-DEDRETNSAISLSSLIQSFNRFLLDQLSSEENSTPPNP----------SPAESPLEQLFGIDAETTIRCsNCGHES 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  673 VRASSTLLFTLSYP-----DDKTGKNYDFAQVLKRSICLDQNTQAWCDTCEKYQPTIQTRNIRHLPDILVINCEVNSSKE 747
Cdd:pfam13423  150 VRESSTHVLDLIYPrkpssNNKKPPNQTFSSILKSSLERETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEW 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  748 ADFWRmqaevafkmavkkhggeisknkefaladwkelgspegvlvcpsieelKNVWLPFSIRMKMTKNKGLDvcnwtdgd 827
Cdd:pfam13423  230 RQLWK-----------------------------------------------TPGWLPPEIGLTLSDDLQGD-------- 254
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2031263991  828 emqwgparaeeeHGVYVYDLMATVVHILDSRTGGSLVAHIKVGETYHqrkEGVTHQQWYLFNDFLI 893
Cdd:pfam13423  255 ------------NEIVKYELRGVVVHIGDSGTSGHLVSFVKVADSEL---EDPTESQWYLFNDFLV 305
PAN2_exo cd06143
DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonuclease PAN2; PAN2 is the catalytic ...
970-1143 1.50e-114

DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonuclease PAN2; PAN2 is the catalytic subunit of poly(A) nuclease (PAN), a Pab1p-dependent 3'-5' exoribonuclease which plays an important role in the posttranscriptional maturation of pre-mRNAs. PAN catalyzes the deadenylation of poly(A) tails, which are initially synthesized to default lengths of 70 to 90, to mRNA-specific lengths of 55 to 71. Pab1p and PAN also play a role in the export and decay of mRNA. PAN2 contains a DEDDh-type DnaQ-like 3'-5' exonuclease domain with three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis.


Pssm-ID: 99846  Cd Length: 174  Bit Score: 353.46  E-value: 1.50e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  970 VGLDAEFVTLNEEEAELRSDGTKSTIKPSQMSVARITCVRGQGPNEGIPFIDDYISTQEQVVDYLTQYSGIKPGDLDAKI 1049
Cdd:cd06143      1 VAIDAEFVKLKPEETEIRSDGTKSTIRPSQMSLARVSVVRGEGELEGVPFIDDYISTTEPVVDYLTRFSGIKPGDLDPKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991 1050 SSKHLTTLKSTYLKLRFLIDIGVKFVGHGLQKDFRVINLMVPKDQVLDTVYLFHMPRKRMISLRFLAWYFLDLKIQGETH 1129
Cdd:cd06143     81 SSKNLTTLKSAYLKLRLLVDLGCIFVGHGLAKDFRVINIQVPKEQVIDTVELFHLPGQRKLSLRFLAWYLLGEKIQSETH 160
                          170
                   ....*....|....
gi 2031263991 1130 DSIEDARTALQLYR 1143
Cdd:cd06143    161 DSIEDARTALKLYR 174
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
502-916 5.34e-82

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 269.00  E-value: 5.34e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  502 GLEDFDFKHYNKTLFAGLEPHIPNAYCNCMIQVLYFLEPVRC--LIQNHLCQKEFCLACELGFLFhmldlsrgdpcqgnn 579
Cdd:cd02672      1 GTEDFDFEFYNKTNYAGLENHITNSYCNSLLQLLYFIPPFRNftAIILVACPKESCLLCELGYLF--------------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  580 flrafrtipeasalgliladsdeasgkgnlarliqrwnrfiltqlhqdmqeleipqayrgaggsfcssgdSVIGQLFSCE 659
Cdd:cd02672     66 ----------------------------------------------------------------------STLIQNFTRF 75
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  660 MENCSLCRCG-----SETVRASSTLLFTLSYPDD--KTGKNYDFAQVLKRSICLDQNTQAWCDTCEKYQPTIQTRNIRHL 732
Cdd:cd02672     76 LLETISQDQLgtpfsCGTSRNSVSLLYTLSLPLGstKTSKESTFLQLLKRSLDLEKVTKAWCDTCCKYQPLEQTTSIRHL 155
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  733 PDILvincevnsskeadfwrmqaevafkmavkkhggeisknkefaladwkelgspegvlvcpsieelknvWLPFSIRMKM 812
Cdd:cd02672    156 PDIL------------------------------------------------------------------LLVLVINLSV 169
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  813 TKNKGLDV-CNWTDGDEMQWGPARAEEEH----------GVYVYDLMATVVHILDSrtggSLVAHIKVGETYHQRKegVT 881
Cdd:cd02672    170 TNGEFDDInVVLPSGKVMQNKVSPKAIDHdklvknrgqeSIYKYELVGYVCEINDS----SRGQHNVVFVIKVNEE--ST 243
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 2031263991  882 HQQWYLFNDFLIEPIDkheavqfdmnwKVPAILYY 916
Cdd:cd02672    244 HGRWYLFNDFLVTPVS-----------ELAYILLY 267
DEDDh_RNase cd06137
DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonucleases PAN2, RNA exonuclease (REX) ...
970-1143 1.83e-45

DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonucleases PAN2, RNA exonuclease (REX)-1,-3, and -4, ISG20, and similar proteins; This group is composed of eukaryotic exoribonucleases that include PAN2, RNA exonuclease 1 (REX1 or Rex1p), REX3 (Rex3p), REX4 (or Rex4p), ISG20, and similar proteins. They are DEDDh-type DnaQ-like 3'-5' exonucleases containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. PAN2 is the catalytic subunit of poly(A) nuclease (PAN), a Pab1p-dependent 3'-5' exoribonuclease which plays an important role in the posttranscriptional maturation of pre-mRNAs. REX proteins are required for the processing and maturation of many RNA species, and ISG20 is an interferon-induced antiviral exonuclease with a strong preference for single-stranded RNA.


Pssm-ID: 99840  Cd Length: 161  Bit Score: 161.29  E-value: 1.83e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  970 VGLDAEFVTLNEEeaelrsdgtkstikpsQMSVARITCVRGqgpNEGIPFIDDYISTQEQVVDYLTQYSGIKPGDL--DA 1047
Cdd:cd06137      1 VALDCEMVGLADG----------------DSEVVRISAVDV---LTGEVLIDSLVRPSVRVTDWRTRFSGVTPADLeeAA 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991 1048 KISSKHLTTLKSTYLKLRFlIDIGVKFVGHGLQKDFRVINLMvpKDQVLDTVYLFHMPRKRM-----ISLRFLAWYFLDL 1122
Cdd:cd06137     62 KAGKTIFGWEAARAALWKF-IDPDTILVGHSLQNDLDALRMI--HTRVVDTAILTREAVKGPlakrqWSLRTLCRDFLGL 138
                          170       180
                   ....*....|....*....|...
gi 2031263991 1123 KIQG--ETHDSIEDARTALQLYR 1143
Cdd:cd06137    139 KIQGggEGHDSLEDALAAREVVL 161
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
618-917 6.43e-27

Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 111.04  E-value: 6.43e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  618 RFILTQLHQDMQELEipqayrgAGGSFCSSGDSVIGQLFSCEMENCSLC-RCGSETVRASSTLLFTLSYPDdKTGKNYDF 696
Cdd:cd02257     30 LFLLDKLHEELKKSS-------KRTSDSSSLKSLIHDLFGGKLESTIVClECGHESVSTEPELFLSLPLPV-KGLPQVSL 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  697 AQVLKRSICLDQNTQAWCDTCE--KYQPTIQTRNIRHLPDILVINCEvnsskeadfwRmqaevaFKMAVKKHGGEISKNK 774
Cdd:cd02257    102 EDCLEKFFKEEILEGDNCYKCEkkKKQEATKRLKIKKLPPVLIIHLK----------R------FSFNEDGTKEKLNTKV 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  775 EFaladwkelgspegvlvcpsieelknvwlPFSIRMKMTKNKGLDVCNwtdgdemqwgparaeEEHGVYVYDLMATVVHI 854
Cdd:cd02257    166 SF----------------------------PLELDLSPYLSEGEKDSD---------------SDNGSYKYELVAVVVHS 202
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2031263991  855 LDSRTGGSLVAHIKVGEtyhqrkegvtHQQWYLFNDFLIEPIDKHEAVQFDMNWKVPAILYYV 917
Cdd:cd02257    203 GTSADSGHYVAYVKDPS----------DGKWYKFNDDKVTEVSEEEVLEFGSLSSSAYILFYE 255
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
969-1147 3.72e-26

exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases;


Pssm-ID: 214685 [Multi-domain]  Cd Length: 169  Bit Score: 106.23  E-value: 3.72e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991   969 LVGLDAEFVTLNEEEAELrsdgtkstikpsqmsvARITCVRGQGPNEGIPFiDDYISTQEQVVDYLTQYSGIKPGDLDAK 1048
Cdd:smart00479    2 LVVIDCETTGLDPGKDEI----------------IEIAAVDVDGGEIIEVF-DTYVKPDRPITDYATEIHGITPEMLDDA 64
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  1049 IsskhltTLKSTYLKLRFLIDIGVKFVGHGLQKDFRVINLMVPK--------DQVLDTVYLFHM--PRKRMISLRFLAWY 1118
Cdd:smart00479   65 P------TFEEVLEELLEFLRGRILVAGNSAHFDLRFLKLEHPRlgikqppkLPVIDTLKLARAtnPGLPKYSLKKLAKR 138
                           170       180
                    ....*....|....*....|....*....
gi 2031263991  1119 FLdLKIQGETHDSIEDARTALQLYRKYLE 1147
Cdd:smart00479  139 LL-LEVIQRAHRALDDARATAKLFKKLLE 166
REX1_like cd06145
DEDDh 3'-5' exonuclease domain of RNA exonuclease 1, -3 and similar eukaryotic proteins; This ...
1000-1141 2.99e-25

DEDDh 3'-5' exonuclease domain of RNA exonuclease 1, -3 and similar eukaryotic proteins; This subfamily is composed of RNA exonuclease 1 (REX1 or Rex1p), REX3 (or Rex3p), and similar eukaryotic proteins. In yeast, REX1 and REX3 are required for 5S rRNA and MRP (mitochondrial RNA processing) RNA maturation, respectively. They are DEDDh-type DnaQ-like 3'-5' exonucleases containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. REX1 is the major exonuclease responsible for pre-tRNA trail trimming and may also be involved in nuclear CCA turnover. REX proteins function in the processing and maturation of many RNA species, similar to the function of Escherichia coli RNase T.


Pssm-ID: 99848  Cd Length: 150  Bit Score: 102.95  E-value: 2.99e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991 1000 MSVARITCVRGqgpnEGIPFIDDYISTQEQVVDYLTQYSGIKPGDLDAKIsskhlTTLKSTYLKLRFLIDIGVKFVGHGL 1079
Cdd:cd06145     14 LELTRVTVVDE----NGKVVLDELVKPDGEIVDYNTRFSGITEEMLENVT-----TTLEDVQKKLLSLISPDTILVGHSL 84
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2031263991 1080 QKDFRVINLMVPKdqVLDTVYLFHMPRKRM--ISLRFLAWYFLDLKIQGET--HDSIEDARTALQL 1141
Cdd:cd06145     85 ENDLKALKLIHPR--VIDTAILFPHPRGPPykPSLKNLAKKYLGRDIQQGEggHDSVEDARAALEL 148
REX4_like cd06144
DEDDh 3'-5' exonuclease domain of RNA exonuclease 4, XPMC2, Interferon Stimulated Gene product ...
970-1143 6.16e-25

DEDDh 3'-5' exonuclease domain of RNA exonuclease 4, XPMC2, Interferon Stimulated Gene product of 20 kDa, and similar proteins; This subfamily is composed of RNA exonuclease 4 (REX4 or Rex4p), XPMC2, Interferon (IFN) Stimulated Gene product of 20 kDa (ISG20), and similar proteins. REX4 is involved in pre-rRNA processing. It controls the ratio between the two forms of 5.8S rRNA in yeast. XPMC2 is a Xenopus gene which was identified through its ability to correct a mitotic defect in fission yeast. The human homolog of XPMC2 (hPMC2) may be involved in angiotensin II-induced adrenal cell cycle progression and cell proliferation. ISG20 is an IFN-induced antiviral exonuclease with a strong preference for single-stranded RNA and minor activity towards single-stranded DNA. These proteins are DEDDh-type DnaQ-like 3'-5' exonucleases containing three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. REX proteins function in the processing and maturation of many RNA species, similar to the function of Escherchia coli RNase T.


Pssm-ID: 99847  Cd Length: 152  Bit Score: 101.82  E-value: 6.16e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  970 VGLDAEFVtlneeeaELRSDGTKStikpsqmSVARITCVrgqgpNE-GIPFIDDYISTQEQVVDYLTQYSGIKPGDLDAK 1048
Cdd:cd06144      1 VALDCEMV-------GVGPDGSES-------ALARVSIV-----NEdGNVVYDTYVKPQEPVTDYRTAVSGIRPEHLKDA 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991 1049 ISSKHLTTLKSTYLKLRFLidigvkfVGHGLQKDFRVINLMVPKDQVLDT---VYLFHMPRKRMISLRFLAWYFLDLKIQ 1125
Cdd:cd06144     62 PDFEEVQKKVAELLKGRIL-------VGHALKNDLKVLKLDHPKKLIRDTskyKPLRKTAKGKSPSLKKLAKQLLGLDIQ 134
                          170
                   ....*....|....*...
gi 2031263991 1126 GETHDSIEDARTALQLYR 1143
Cdd:cd06144    135 EGEHSSVEDARAAMRLYR 152
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
970-1142 9.94e-19

Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T and the epsilon subunit of DNA polymerase III.;


Pssm-ID: 395743 [Multi-domain]  Cd Length: 164  Bit Score: 84.71  E-value: 9.94e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  970 VGLDAEFVTLNEEEAELrsdgtkstikpsqMSVARITCVRGQgpNEGIPFIDDYISTQE--QVVDYLTQYSGIKPGDLDA 1047
Cdd:pfam00929    1 VVIDLETTGLDPEKDEI-------------IEIAAVVIDGGE--NEIGETFHTYVKPTRlpKLTDECTKFTGITQAMLDN 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991 1048 KISSKH-LTTLKSTYLKLRFLIDIGVKF-VGHGLQKDFRVINLMVPK-DQVLDTVYLFHMPRKRM--ISLRFLAWYFlDL 1122
Cdd:pfam00929   66 KPSFEEvLEEFLEFLRKGNLLVAHNASFdVGFLRYDDKRFLKKPMPKlNPVIDTLILDKATYKELpgRSLDALAEKL-GL 144
                          170       180
                   ....*....|....*....|
gi 2031263991 1123 KIQGETHDSIEDARTALQLY 1142
Cdd:pfam00929  145 EHIGRAHRALDDARATAKLF 164
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
527-916 5.56e-15

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 77.10  E-value: 5.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  527 YCNCMIQVLYFLEPVRCLIQN--HLC-----QKEFCLACELGFLFH-MLDLSRGDPCQGNNFLRAFRTIPEasalglila 598
Cdd:pfam00443   11 YMNSVLQSLFSIPPFRDYLLRisPLSedsryNKDINLLCALRDLFKaLQKNSKSSSVSPKMFKKSLGKLNP--------- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  599 dsDEASGKGNLArliQRWNRFILTQLHQDMQeleipqayrgagGSFCSSGDSVIGQLFSCEMENCSLCR-CGSETVRASS 677
Cdd:pfam00443   82 --DFSGYKQQDA---QEFLLFLLDGLHEDLN------------GNHSTENESLITDLFRGQLKSRLKCLsCGEVSETFEP 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  678 TLLFTLSYPDDKT-----GKNYDFAQVLKRSIcLDQNTQAWCDTCEKYQPTIQTRNIRHLPDILVINcevnsSKEADFWR 752
Cdd:pfam00443  145 FSDLSLPIPGDSAelktaSLQICFLQFSKLEE-LDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIH-----LKRFSYNR 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  753 MqaevafkMAVKkhggeISKNKEFaladwkelgspegvlvcpsieelknvwlPFSIRMKMTKNKGLDvcnwtdgdemqwg 832
Cdd:pfam00443  219 S-------TWEK-----LNTEVEF----------------------------PLELDLSRYLAEELK------------- 245
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  833 paraEEEHGVYVYDLMATVVHiLDSRTGGSLVAHIKVGEtyhqrkegvtHQQWYLFNDFLIEPIDKHEAVQFDMnwkvPA 912
Cdd:pfam00443  246 ----PKTNNLQDYRLVAVVVH-SGSLSSGHYIAYIKAYE----------NNRWYKFDDEKVTEVDEETAVLSSS----AY 306

                   ....
gi 2031263991  913 ILYY 916
Cdd:pfam00443  307 ILFY 310
ISG20 cd06149
DEDDh 3'-5' exonuclease domain of Interferon Stimulated Gene product of 20 kDa, and similar ...
1021-1143 4.71e-14

DEDDh 3'-5' exonuclease domain of Interferon Stimulated Gene product of 20 kDa, and similar proteins; Interferon (IFN) Stimulated Gene product of 20 kDa (ISG20) is an IFN-induced antiviral exonuclease with a strong preference for single-stranded RNA and minor activity towards single-stranded DNA. It was also independently identified by its response to estrogen and was called HEM45 (human estrogen regulated transcript). ISG20 is a DEDDh-type DnaQ-like 3'-5' exonuclease containing three conserved sequence motifs termed ExoI, ExoII and ExoIII with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. ISG20 may be a major effector of innate immunity against pathogens including viruses, bacteria, and parasites. It is located in promyelocytic leukemia (PML) nuclear bodies, sites for oncogenic DNA viral transcription and replication. It may carry out its function by degrading viral RNAs as part of the IFN-regulated antiviral response.


Pssm-ID: 99852  Cd Length: 157  Bit Score: 70.93  E-value: 4.71e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991 1021 DDYISTQEQVVDYLTQYSGIKPGDLdakissKHLTTLKSTYLKLRFLIDiGVKFVGHGLQKDFRVINLMVPKDQVLDTVY 1100
Cdd:cd06149     34 DKYIRPEGPVTDYRTRWSGIRRQHL------VNATPFAVAQKEILKILK-GKVVVGHAIHNDFKALKYFHPKHMTRDTST 106
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2031263991 1101 ------LFHMPRKRMISLRFLAWYFLDLKIQG--ETHDSIEDARTALQLYR 1143
Cdd:cd06149    107 ipllnrKAGFPENCRVSLKVLAKRLLHRDIQVgrQGHSSVEDARATMELYK 157
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
827-898 3.74e-04

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 43.95  E-value: 3.74e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2031263991  827 DEMQWGPARAEEEHGVYVYDLMATVVHILDSRTGGSLVAHIKVGETyhqrkegvthQQWYLFNDFLIEPIDK 898
Cdd:cd02668    228 EILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQT----------GEWYKFNDEDVEEMPG 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
204-357 9.01e-04

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 42.71  E-value: 9.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  204 QTNRFFFCGHTSGKVSLRDLRTFKVEHEFDAFSGSLSDFDVH--GNLLAACGfssrltglaCDRFLKVYDLRMMRAITPL 281
Cdd:cd00200    145 PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSpdGEKLLSSS---------SDGTIKLWDLSTGKCLGTL 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031263991  282 QVHVDPA-FLRFIPtytSRLAIIS------------QSGQCQFCeptgLANpadifHVNPVGpllmTFDVSASKQALAFG 348
Cdd:cd00200    216 RGHENGVnSVAFSP---DGYLLASgsedgtirvwdlRTGECVQT----LSG-----HTNSVT----SLAWSPDGKRLASG 279

                   ....*....
gi 2031263991  349 DSEGCVHLW 357
Cdd:cd00200    280 SADGTIRIW 288
PRK07247 PRK07247
3'-5' exonuclease;
1122-1151 9.36e-03

3'-5' exonuclease;


Pssm-ID: 180906 [Multi-domain]  Cd Length: 195  Bit Score: 38.61  E-value: 9.36e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2031263991 1122 LKIQGETHDSIEDARTALQLYRKYLELSKN 1151
Cdd:PRK07247   142 LGIKGRGHNSLEDARMTARVYESFLESDQN 171
 
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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