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Conserved domains on  [gi|1677502126|ref|NP_055686|]
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PAN2-PAN3 deadenylation complex catalytic subunit PAN2 isoform 3 [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;
517-894 9.06e-115

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 359.28  E-value: 9.06e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  517 AGLEPHIPNAYCNCMIQVLYFLEPVRCLIQNHL---CQKEFCLACELGFLFHMLDLSRGDPCQGNNFLRAFRTIPEASAL 593
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLateCLKEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIPEASAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  594 GLIlADSDEASGKGNLARLIQRWNRFILTQLHQDMQELEIPQayrgaggssfcSSGDSVIGQLFSCEMENCSLC-RCGSE 672
Cdd:pfam13423   81 GLL-DEDRETNSAISLSSLIQSFNRFLLDQLSSEENSTPPNP-----------SPAESPLEQLFGIDAETTIRCsNCGHE 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  673 TVRASSTLLFTLSYP-----DDKTGKNYDFAQVLKRSICLDQNTQAWCDTCEKYQPTIQTRNIRHLPDILVINCEVNSSK 747
Cdd:pfam13423  149 SVRESSTHVLDLIYPrkpssNNKKPPNQTFSSILKSSLERETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  748 EADFWRmqaevafkmavkkhggeisknkefaladwkelgspegvlvcpsieelKNVWLPFSIRMKMTKNKGLDvcnwtdg 827
Cdd:pfam13423  229 WRQLWK-----------------------------------------------TPGWLPPEIGLTLSDDLQGD------- 254
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677502126  828 demqwgparaeeeHGVYVYDLMATVVHILDSRTGGSLVAHIKVGETYHqrkEGVTHQQWYLFNDFLI 894
Cdd:pfam13423  255 -------------NEIVKYELRGVVVHIGDSGTSGHLVSFVKVADSEL---EDPTESQWYLFNDFLV 305
PAN2_exo cd06143
DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonuclease PAN2; PAN2 is the catalytic ...
971-1144 1.49e-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: 1.49e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  971 VGLDAEFVTLNEEEAELRSDGTKSTIKPSQMSVARITCVRGQGPNEGIPFIDDYISTQEQVVDYLTQYSGIKPGDLDAKI 1050
Cdd:cd06143      1 VAIDAEFVKLKPEETEIRSDGTKSTIRPSQMSLARVSVVRGEGELEGVPFIDDYISTTEPVVDYLTRFSGIKPGDLDPKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126 1051 SSKHLTTLKSTYLKLRFLIDIGVKFVGHGLQKDFRVINLMVPKDQVLDTVYLFHMPRKRMISLRFLAWYFLDLKIQGETH 1130
Cdd:cd06143     81 SSKNLTTLKSAYLKLRLLVDLGCIFVGHGLAKDFRVINIQVPKEQVIDTVELFHLPGQRKLSLRFLAWYLLGEKIQSETH 160
                          170
                   ....*....|....
gi 1677502126 1131 DSIEDARTALQLYR 1144
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 9.02e-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: 9.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  204 QTNRFFFCGHTSGKVSLRDLRTFKVEHEFDAFSGSLSDFDVH--GNLLAACGfssrltglaCDRFLKVYDLRMMRAITPL 281
Cdd:cd00200    145 PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSpdGEKLLSSS---------SDGTIKLWDLSTGKCLGTL 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  282 QVHVDPA-FLRFIPtytSRLAIIS------------QSGQCQFCeptgLANpadifHVNPVGpllmTFDVSASKQALAFG 348
Cdd:cd00200    216 RGHENGVnSVAFSP---DGYLLASgsedgtirvwdlRTGECVQT----LSG-----HTNSVT----SLAWSPDGKRLASG 279

                   ....*....
gi 1677502126  349 DSEGCVHLW 357
Cdd:cd00200    280 SADGTIRIW 288
 
Name Accession Description Interval E-value
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
517-894 9.06e-115

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 359.28  E-value: 9.06e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  517 AGLEPHIPNAYCNCMIQVLYFLEPVRCLIQNHL---CQKEFCLACELGFLFHMLDLSRGDPCQGNNFLRAFRTIPEASAL 593
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLateCLKEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIPEASAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  594 GLIlADSDEASGKGNLARLIQRWNRFILTQLHQDMQELEIPQayrgaggssfcSSGDSVIGQLFSCEMENCSLC-RCGSE 672
Cdd:pfam13423   81 GLL-DEDRETNSAISLSSLIQSFNRFLLDQLSSEENSTPPNP-----------SPAESPLEQLFGIDAETTIRCsNCGHE 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  673 TVRASSTLLFTLSYP-----DDKTGKNYDFAQVLKRSICLDQNTQAWCDTCEKYQPTIQTRNIRHLPDILVINCEVNSSK 747
Cdd:pfam13423  149 SVRESSTHVLDLIYPrkpssNNKKPPNQTFSSILKSSLERETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  748 EADFWRmqaevafkmavkkhggeisknkefaladwkelgspegvlvcpsieelKNVWLPFSIRMKMTKNKGLDvcnwtdg 827
Cdd:pfam13423  229 WRQLWK-----------------------------------------------TPGWLPPEIGLTLSDDLQGD------- 254
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677502126  828 demqwgparaeeeHGVYVYDLMATVVHILDSRTGGSLVAHIKVGETYHqrkEGVTHQQWYLFNDFLI 894
Cdd:pfam13423  255 -------------NEIVKYELRGVVVHIGDSGTSGHLVSFVKVADSEL---EDPTESQWYLFNDFLV 305
PAN2_exo cd06143
DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonuclease PAN2; PAN2 is the catalytic ...
971-1144 1.49e-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: 1.49e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  971 VGLDAEFVTLNEEEAELRSDGTKSTIKPSQMSVARITCVRGQGPNEGIPFIDDYISTQEQVVDYLTQYSGIKPGDLDAKI 1050
Cdd:cd06143      1 VAIDAEFVKLKPEETEIRSDGTKSTIRPSQMSLARVSVVRGEGELEGVPFIDDYISTTEPVVDYLTRFSGIKPGDLDPKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126 1051 SSKHLTTLKSTYLKLRFLIDIGVKFVGHGLQKDFRVINLMVPKDQVLDTVYLFHMPRKRMISLRFLAWYFLDLKIQGETH 1130
Cdd:cd06143     81 SSKNLTTLKSAYLKLRLLVDLGCIFVGHGLAKDFRVINIQVPKEQVIDTVELFHLPGQRKLSLRFLAWYLLGEKIQSETH 160
                          170
                   ....*....|....
gi 1677502126 1131 DSIEDARTALQLYR 1144
Cdd:cd06143    161 DSIEDARTALKLYR 174
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
502-917 7.55e-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: 268.61  E-value: 7.55e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  502 GLEDFDFKHYNKTLFAGLEPHIPNAYCNCMIQVLYFLEPVRC--LIQNHLCQKEFCLACELGFLFhmldlsrgdpcqgnn 579
Cdd:cd02672      1 GTEDFDFEFYNKTNYAGLENHITNSYCNSLLQLLYFIPPFRNftAIILVACPKESCLLCELGYLF--------------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  580 flrafrtipeasalgliladsdeasgkgnlarliqrwnrfiltqlhqdmqeleipqayrgaggssfcssgdSVIGQLFSC 659
Cdd:cd02672     66 -----------------------------------------------------------------------STLIQNFTR 74
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  660 EMENCSLCRCG-----SETVRASSTLLFTLSYPDD--KTGKNYDFAQVLKRSICLDQNTQAWCDTCEKYQPTIQTRNIRH 732
Cdd:cd02672     75 FLLETISQDQLgtpfsCGTSRNSVSLLYTLSLPLGstKTSKESTFLQLLKRSLDLEKVTKAWCDTCCKYQPLEQTTSIRH 154
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  733 LPDILvincevnsskeadfwrmqaevafkmavkkhggeisknkefaladwkelgspegvlvcpsieelknvWLPFSIRMK 812
Cdd:cd02672    155 LPDIL------------------------------------------------------------------LLVLVINLS 168
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  813 MTKNKGLDV-CNWTDGDEMQWGPARAEEEH----------GVYVYDLMATVVHILDSrtggSLVAHIKVGETYHQRKegV 881
Cdd:cd02672    169 VTNGEFDDInVVLPSGKVMQNKVSPKAIDHdklvknrgqeSIYKYELVGYVCEINDS----SRGQHNVVFVIKVNEE--S 242
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1677502126  882 THQQWYLFNDFLIEPIDkheavqfdmnwKVPAILYY 917
Cdd:cd02672    243 THGRWYLFNDFLVTPVS-----------ELAYILLY 267
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
970-1148 3.51e-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: 3.51e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126   970 LVGLDAEFVTLNEEEAELrsdgtkstikpsqmsvARITCVRGQGPNEGIPFiDDYISTQEQVVDYLTQYSGIKPGDLDAK 1049
Cdd:smart00479    2 LVVIDCETTGLDPGKDEI----------------IEIAAVDVDGGEIIEVF-DTYVKPDRPITDYATEIHGITPEMLDDA 64
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  1050 IsskhltTLKSTYLKLRFLIDIGVKFVGHGLQKDFRVINLMVPK--------DQVLDTVYLFHM--PRKRMISLRFLAWY 1119
Cdd:smart00479   65 P------TFEEVLEELLEFLRGRILVAGNSAHFDLRFLKLEHPRlgikqppkLPVIDTLKLARAtnPGLPKYSLKKLAKR 138
                           170       180
                    ....*....|....*....|....*....
gi 1677502126  1120 FLdLKIQGETHDSIEDARTALQLYRKYLE 1148
Cdd:smart00479  139 LL-LEVIQRAHRALDDARATAKLFKKLLE 166
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
971-1143 9.39e-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: 9.39e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  971 VGLDAEFVTLNEEEAELrsdgtkstikpsqMSVARITCVRGQgpNEGIPFIDDYISTQE--QVVDYLTQYSGIKPGDLDA 1048
Cdd:pfam00929    1 VVIDLETTGLDPEKDEI-------------IEIAAVVIDGGE--NEIGETFHTYVKPTRlpKLTDECTKFTGITQAMLDN 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126 1049 KISSKH-LTTLKSTYLKLRFLIDIGVKF-VGHGLQKDFRVINLMVPK-DQVLDTVYLFHMPRKRM--ISLRFLAWYFlDL 1123
Cdd:pfam00929   66 KPSFEEvLEEFLEFLRKGNLLVAHNASFdVGFLRYDDKRFLKKPMPKlNPVIDTLILDKATYKELpgRSLDALAEKL-GL 144
                          170       180
                   ....*....|....*....|
gi 1677502126 1124 KIQGETHDSIEDARTALQLY 1143
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 9.02e-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: 9.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  204 QTNRFFFCGHTSGKVSLRDLRTFKVEHEFDAFSGSLSDFDVH--GNLLAACGfssrltglaCDRFLKVYDLRMMRAITPL 281
Cdd:cd00200    145 PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSpdGEKLLSSS---------SDGTIKLWDLSTGKCLGTL 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  282 QVHVDPA-FLRFIPtytSRLAIIS------------QSGQCQFCeptgLANpadifHVNPVGpllmTFDVSASKQALAFG 348
Cdd:cd00200    216 RGHENGVnSVAFSP---DGYLLASgsedgtirvwdlRTGECVQT----LSG-----HTNSVT----SLAWSPDGKRLASG 279

                   ....*....
gi 1677502126  349 DSEGCVHLW 357
Cdd:cd00200    280 SADGTIRIW 288
PRK07247 PRK07247
3'-5' exonuclease;
1123-1152 9.37e-03

3'-5' exonuclease;


Pssm-ID: 180906 [Multi-domain]  Cd Length: 195  Bit Score: 38.61  E-value: 9.37e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1677502126 1123 LKIQGETHDSIEDARTALQLYRKYLELSKN 1152
Cdd:PRK07247   142 LGIKGRGHNSLEDARMTARVYESFLESDQN 171
 
Name Accession Description Interval E-value
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
517-894 9.06e-115

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 359.28  E-value: 9.06e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  517 AGLEPHIPNAYCNCMIQVLYFLEPVRCLIQNHL---CQKEFCLACELGFLFHMLDLSRGDPCQGNNFLRAFRTIPEASAL 593
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLateCLKEHCLLCELGFLFDMLEKAKGKNCQASNFLRALSSIPEASAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  594 GLIlADSDEASGKGNLARLIQRWNRFILTQLHQDMQELEIPQayrgaggssfcSSGDSVIGQLFSCEMENCSLC-RCGSE 672
Cdd:pfam13423   81 GLL-DEDRETNSAISLSSLIQSFNRFLLDQLSSEENSTPPNP-----------SPAESPLEQLFGIDAETTIRCsNCGHE 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  673 TVRASSTLLFTLSYP-----DDKTGKNYDFAQVLKRSICLDQNTQAWCDTCEKYQPTIQTRNIRHLPDILVINCEVNSSK 747
Cdd:pfam13423  149 SVRESSTHVLDLIYPrkpssNNKKPPNQTFSSILKSSLERETTTKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  748 EADFWRmqaevafkmavkkhggeisknkefaladwkelgspegvlvcpsieelKNVWLPFSIRMKMTKNKGLDvcnwtdg 827
Cdd:pfam13423  229 WRQLWK-----------------------------------------------TPGWLPPEIGLTLSDDLQGD------- 254
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677502126  828 demqwgparaeeeHGVYVYDLMATVVHILDSRTGGSLVAHIKVGETYHqrkEGVTHQQWYLFNDFLI 894
Cdd:pfam13423  255 -------------NEIVKYELRGVVVHIGDSGTSGHLVSFVKVADSEL---EDPTESQWYLFNDFLV 305
PAN2_exo cd06143
DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonuclease PAN2; PAN2 is the catalytic ...
971-1144 1.49e-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: 1.49e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  971 VGLDAEFVTLNEEEAELRSDGTKSTIKPSQMSVARITCVRGQGPNEGIPFIDDYISTQEQVVDYLTQYSGIKPGDLDAKI 1050
Cdd:cd06143      1 VAIDAEFVKLKPEETEIRSDGTKSTIRPSQMSLARVSVVRGEGELEGVPFIDDYISTTEPVVDYLTRFSGIKPGDLDPKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126 1051 SSKHLTTLKSTYLKLRFLIDIGVKFVGHGLQKDFRVINLMVPKDQVLDTVYLFHMPRKRMISLRFLAWYFLDLKIQGETH 1130
Cdd:cd06143     81 SSKNLTTLKSAYLKLRLLVDLGCIFVGHGLAKDFRVINIQVPKEQVIDTVELFHLPGQRKLSLRFLAWYLLGEKIQSETH 160
                          170
                   ....*....|....
gi 1677502126 1131 DSIEDARTALQLYR 1144
Cdd:cd06143    161 DSIEDARTALKLYR 174
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
502-917 7.55e-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: 268.61  E-value: 7.55e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  502 GLEDFDFKHYNKTLFAGLEPHIPNAYCNCMIQVLYFLEPVRC--LIQNHLCQKEFCLACELGFLFhmldlsrgdpcqgnn 579
Cdd:cd02672      1 GTEDFDFEFYNKTNYAGLENHITNSYCNSLLQLLYFIPPFRNftAIILVACPKESCLLCELGYLF--------------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  580 flrafrtipeasalgliladsdeasgkgnlarliqrwnrfiltqlhqdmqeleipqayrgaggssfcssgdSVIGQLFSC 659
Cdd:cd02672     66 -----------------------------------------------------------------------STLIQNFTR 74
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  660 EMENCSLCRCG-----SETVRASSTLLFTLSYPDD--KTGKNYDFAQVLKRSICLDQNTQAWCDTCEKYQPTIQTRNIRH 732
Cdd:cd02672     75 FLLETISQDQLgtpfsCGTSRNSVSLLYTLSLPLGstKTSKESTFLQLLKRSLDLEKVTKAWCDTCCKYQPLEQTTSIRH 154
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  733 LPDILvincevnsskeadfwrmqaevafkmavkkhggeisknkefaladwkelgspegvlvcpsieelknvWLPFSIRMK 812
Cdd:cd02672    155 LPDIL------------------------------------------------------------------LLVLVINLS 168
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  813 MTKNKGLDV-CNWTDGDEMQWGPARAEEEH----------GVYVYDLMATVVHILDSrtggSLVAHIKVGETYHQRKegV 881
Cdd:cd02672    169 VTNGEFDDInVVLPSGKVMQNKVSPKAIDHdklvknrgqeSIYKYELVGYVCEINDS----SRGQHNVVFVIKVNEE--S 242
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1677502126  882 THQQWYLFNDFLIEPIDkheavqfdmnwKVPAILYY 917
Cdd:cd02672    243 THGRWYLFNDFLVTPVS-----------ELAYILLY 267
DEDDh_RNase cd06137
DEDDh 3'-5' exonuclease domain of the eukaryotic exoribonucleases PAN2, RNA exonuclease (REX) ...
971-1144 1.80e-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: 1.80e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  971 VGLDAEFVTLNEEeaelrsdgtkstikpsQMSVARITCVRGqgpNEGIPFIDDYISTQEQVVDYLTQYSGIKPGDL--DA 1048
Cdd:cd06137      1 VALDCEMVGLADG----------------DSEVVRISAVDV---LTGEVLIDSLVRPSVRVTDWRTRFSGVTPADLeeAA 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126 1049 KISSKHLTTLKSTYLKLRFlIDIGVKFVGHGLQKDFRVINLMvpKDQVLDTVYLFHMPRKRM-----ISLRFLAWYFLDL 1123
Cdd:cd06137     62 KAGKTIFGWEAARAALWKF-IDPDTILVGHSLQNDLDALRMI--HTRVVDTAILTREAVKGPlakrqWSLRTLCRDFLGL 138
                          170       180
                   ....*....|....*....|...
gi 1677502126 1124 KIQG--ETHDSIEDARTALQLYR 1144
Cdd:cd06137    139 KIQGggEGHDSLEDALAAREVVL 161
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
618-918 1.97e-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: 112.58  E-value: 1.97e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  618 RFILTQLHQDMQeleipqayRGAGGSSFCSSGDSVIGQLFSCEMENCSLC-RCGSETVRASSTLLFTLSYPDdKTGKNYD 696
Cdd:cd02257     30 LFLLDKLHEELK--------KSSKRTSDSSSLKSLIHDLFGGKLESTIVClECGHESVSTEPELFLSLPLPV-KGLPQVS 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  697 FAQVLKRSICLDQNTQAWCDTCE--KYQPTIQTRNIRHLPDILVINCEvnsskeadfwRmqaevaFKMAVKKHGGEISKN 774
Cdd:cd02257    101 LEDCLEKFFKEEILEGDNCYKCEkkKKQEATKRLKIKKLPPVLIIHLK----------R------FSFNEDGTKEKLNTK 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  775 KEFaladwkelgspegvlvcpsieelknvwlPFSIRMKMTKNKGLDVCNwtdgdemqwgparaeEEHGVYVYDLMATVVH 854
Cdd:cd02257    165 VSF----------------------------PLELDLSPYLSEGEKDSD---------------SDNGSYKYELVAVVVH 201
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677502126  855 ILDSRTGGSLVAHIKVGEtyhqrkegvtHQQWYLFNDFLIEPIDKHEAVQFDMNWKVPAILYYV 918
Cdd:cd02257    202 SGTSADSGHYVAYVKDPS----------DGKWYKFNDDKVTEVSEEEVLEFGSLSSSAYILFYE 255
EXOIII smart00479
exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other ...
970-1148 3.51e-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: 3.51e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126   970 LVGLDAEFVTLNEEEAELrsdgtkstikpsqmsvARITCVRGQGPNEGIPFiDDYISTQEQVVDYLTQYSGIKPGDLDAK 1049
Cdd:smart00479    2 LVVIDCETTGLDPGKDEI----------------IEIAAVDVDGGEIIEVF-DTYVKPDRPITDYATEIHGITPEMLDDA 64
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  1050 IsskhltTLKSTYLKLRFLIDIGVKFVGHGLQKDFRVINLMVPK--------DQVLDTVYLFHM--PRKRMISLRFLAWY 1119
Cdd:smart00479   65 P------TFEEVLEELLEFLRGRILVAGNSAHFDLRFLKLEHPRlgikqppkLPVIDTLKLARAtnPGLPKYSLKKLAKR 138
                           170       180
                    ....*....|....*....|....*....
gi 1677502126  1120 FLdLKIQGETHDSIEDARTALQLYRKYLE 1148
Cdd:smart00479  139 LL-LEVIQRAHRALDDARATAKLFKKLLE 166
REX1_like cd06145
DEDDh 3'-5' exonuclease domain of RNA exonuclease 1, -3 and similar eukaryotic proteins; This ...
1001-1142 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 1677502126 1001 MSVARITCVRGqgpnEGIPFIDDYISTQEQVVDYLTQYSGIKPGDLDAKIsskhlTTLKSTYLKLRFLIDIGVKFVGHGL 1080
Cdd:cd06145     14 LELTRVTVVDE----NGKVVLDELVKPDGEIVDYNTRFSGITEEMLENVT-----TTLEDVQKKLLSLISPDTILVGHSL 84
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677502126 1081 QKDFRVINLMVPKdqVLDTVYLFHMPRKRM--ISLRFLAWYFLDLKIQGET--HDSIEDARTALQL 1142
Cdd:cd06145     85 ENDLKALKLIHPR--VIDTAILFPHPRGPPykPSLKNLAKKYLGRDIQQGEggHDSVEDARAALEL 148
REX4_like cd06144
DEDDh 3'-5' exonuclease domain of RNA exonuclease 4, XPMC2, Interferon Stimulated Gene product ...
971-1144 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 1677502126  971 VGLDAEFVtlneeeaELRSDGTKStikpsqmSVARITCVrgqgpNE-GIPFIDDYISTQEQVVDYLTQYSGIKPGDLDAK 1049
Cdd:cd06144      1 VALDCEMV-------GVGPDGSES-------ALARVSIV-----NEdGNVVYDTYVKPQEPVTDYRTAVSGIRPEHLKDA 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126 1050 ISSKHLTTLKSTYLKLRFLidigvkfVGHGLQKDFRVINLMVPKDQVLDT---VYLFHMPRKRMISLRFLAWYFLDLKIQ 1126
Cdd:cd06144     62 PDFEEVQKKVAELLKGRIL-------VGHALKNDLKVLKLDHPKKLIRDTskyKPLRKTAKGKSPSLKKLAKQLLGLDIQ 134
                          170
                   ....*....|....*...
gi 1677502126 1127 GETHDSIEDARTALQLYR 1144
Cdd:cd06144    135 EGEHSSVEDARAAMRLYR 152
RNase_T pfam00929
Exonuclease; This family includes a variety of exonuclease proteins, such as ribonuclease T ...
971-1143 9.39e-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: 9.39e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  971 VGLDAEFVTLNEEEAELrsdgtkstikpsqMSVARITCVRGQgpNEGIPFIDDYISTQE--QVVDYLTQYSGIKPGDLDA 1048
Cdd:pfam00929    1 VVIDLETTGLDPEKDEI-------------IEIAAVVIDGGE--NEIGETFHTYVKPTRlpKLTDECTKFTGITQAMLDN 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126 1049 KISSKH-LTTLKSTYLKLRFLIDIGVKF-VGHGLQKDFRVINLMVPK-DQVLDTVYLFHMPRKRM--ISLRFLAWYFlDL 1123
Cdd:pfam00929   66 KPSFEEvLEEFLEFLRKGNLLVAHNASFdVGFLRYDDKRFLKKPMPKlNPVIDTLILDKATYKELpgRSLDALAEKL-GL 144
                          170       180
                   ....*....|....*....|
gi 1677502126 1124 KIQGETHDSIEDARTALQLY 1143
Cdd:pfam00929  145 EHIGRAHRALDDARATAKLF 164
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
527-917 8.91e-15

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 76.71  E-value: 8.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  527 YCNCMIQVLYFLEPVRCLIQN--HLC-----QKEFCLACELGFLFH-MLDLSRGDPCQGNNFLRAFRTIPEasalglila 598
Cdd:pfam00443   11 YMNSVLQSLFSIPPFRDYLLRisPLSedsryNKDINLLCALRDLFKaLQKNSKSSSVSPKMFKKSLGKLNP--------- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  599 dsDEASGKGNLArliQRWNRFILTQLHQDMQeleipqayrgaggSSFCSSGDSVIGQLFSCEMENCSLCR-CGSETVRAS 677
Cdd:pfam00443   82 --DFSGYKQQDA---QEFLLFLLDGLHEDLN-------------GNHSTENESLITDLFRGQLKSRLKCLsCGEVSETFE 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  678 STLLFTLSYPDDKT-----GKNYDFAQVLKRSIcLDQNTQAWCDTCEKYQPTIQTRNIRHLPDILVINcevnsSKEADFW 752
Cdd:pfam00443  144 PFSDLSLPIPGDSAelktaSLQICFLQFSKLEE-LDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIH-----LKRFSYN 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  753 RMqaevafkMAVKkhggeISKNKEFaladwkelgspegvlvcpsieelknvwlPFSIRMKMTKNKGLDvcnwtdgdemqw 832
Cdd:pfam00443  218 RS-------TWEK-----LNTEVEF----------------------------PLELDLSRYLAEELK------------ 245
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  833 gparaEEEHGVYVYDLMATVVHiLDSRTGGSLVAHIKVGEtyhqrkegvtHQQWYLFNDFLIEPIDKHEAVQFDMnwkvP 912
Cdd:pfam00443  246 -----PKTNNLQDYRLVAVVVH-SGSLSSGHYIAYIKAYE----------NNRWYKFDDEKVTEVDEETAVLSSS----A 305

                   ....*
gi 1677502126  913 AILYY 917
Cdd:pfam00443  306 YILFY 310
ISG20 cd06149
DEDDh 3'-5' exonuclease domain of Interferon Stimulated Gene product of 20 kDa, and similar ...
1022-1144 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 1677502126 1022 DDYISTQEQVVDYLTQYSGIKPGDLdakissKHLTTLKSTYLKLRFLIDiGVKFVGHGLQKDFRVINLMVPKDQVLDTVY 1101
Cdd:cd06149     34 DKYIRPEGPVTDYRTRWSGIRRQHL------VNATPFAVAQKEILKILK-GKVVVGHAIHNDFKALKYFHPKHMTRDTST 106
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1677502126 1102 ------LFHMPRKRMISLRFLAWYFLDLKIQG--ETHDSIEDARTALQLYR 1144
Cdd:cd06149    107 ipllnrKAGFPENCRVSLKVLAKRLLHRDIQVgrQGHSSVEDARATMELYK 157
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
828-899 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 1677502126  828 DEMQWGPARAEEEHGVYVYDLMATVVHILDSRTGGSLVAHIKVGETyhqrkegvthQQWYLFNDFLIEPIDK 899
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 9.02e-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: 9.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  204 QTNRFFFCGHTSGKVSLRDLRTFKVEHEFDAFSGSLSDFDVH--GNLLAACGfssrltglaCDRFLKVYDLRMMRAITPL 281
Cdd:cd00200    145 PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSpdGEKLLSSS---------SDGTIKLWDLSTGKCLGTL 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677502126  282 QVHVDPA-FLRFIPtytSRLAIIS------------QSGQCQFCeptgLANpadifHVNPVGpllmTFDVSASKQALAFG 348
Cdd:cd00200    216 RGHENGVnSVAFSP---DGYLLASgsedgtirvwdlRTGECVQT----LSG-----HTNSVT----SLAWSPDGKRLASG 279

                   ....*....
gi 1677502126  349 DSEGCVHLW 357
Cdd:cd00200    280 SADGTIRIW 288
PRK07247 PRK07247
3'-5' exonuclease;
1123-1152 9.37e-03

3'-5' exonuclease;


Pssm-ID: 180906 [Multi-domain]  Cd Length: 195  Bit Score: 38.61  E-value: 9.37e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1677502126 1123 LKIQGETHDSIEDARTALQLYRKYLELSKN 1152
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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