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Conserved domains on  [gi|528495786|ref|XP_005169520|]
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ubiquitin carboxyl-terminal hydrolase 42 isoform X1 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
113-412 0e+00

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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 543.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  113 GAGLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFCMMCTMQNHIIQVFANSGNVIKPISVLNELKRIGKH 192
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  193 FRFGSQEDAHEFLRYTVDAMQKSCLPGNK----LDRQTQATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKT 268
Cdd:cd02661    81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKklkaVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  269 AQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFNGGKITKDVRYAEHLDLRPFMSQ 348
Cdd:cd02661   161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528495786  349 SHGEPQIYALYAVLVHSGFSCHAGHYYCYIKASNGQWYQMNDSSVSLSDIRTVLNQQAYLLFYI 412
Cdd:cd02661   241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
U2AF_lg super family cl36941
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
844-940 9.33e-07

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


The actual alignment was detected with superfamily member TIGR01642:

Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 52.97  E-value: 9.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   844 EDRNRGSDRPHFSSTPKDRERYRHyRDHSdRSRSRYGHSYQDSRRSTSRER-YYRDRDLERHWDRFSHHRREHHYFQRRH 922
Cdd:TIGR01642    5 PDREREKSRGRDRDRSSERPRRRS-RDRS-RFRDRHRRSRERSYREDSRPRdRRRYDSRSPRSLRYSSVRRSRDRPRRRS 82
                           90
                   ....*....|....*...
gi 528495786   923 RDERDWNRDRRFGSDSYR 940
Cdd:TIGR01642   83 RSVRSIEQHRRRLRDRSP 100
SF-CC1 super family cl36939
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
896-1005 6.90e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


The actual alignment was detected with superfamily member TIGR01622:

Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 40.29  E-value: 6.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   896 YRDRDLERHWDRFSHHRREHHYFQRRHRDeRDWNRDRRFGSDSYRPSGyHNRNGYSNHSHRGMEEAHGRATHTVNGSKGR 975
Cdd:TIGR01622    2 YRDRERERLRDSSSAGDRDRRRDKGRERS-RDRSRDRERSRSRRRDRH-RDRDYYRGRERRSRSRRPNRRYRPREKRRRR 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 528495786   976 PSSphsvSPLPRHHKRKRSPSVDARESSDE 1005
Cdd:TIGR01622   80 GDS----YRRRRDDRRSRREKPRARDGTPE 105
 
Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
113-412 0e+00

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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 543.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  113 GAGLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFCMMCTMQNHIIQVFANSGNVIKPISVLNELKRIGKH 192
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  193 FRFGSQEDAHEFLRYTVDAMQKSCLPGNK----LDRQTQATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKT 268
Cdd:cd02661    81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKklkaVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  269 AQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFNGGKITKDVRYAEHLDLRPFMSQ 348
Cdd:cd02661   161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528495786  349 SHGEPQIYALYAVLVHSGFSCHAGHYYCYIKASNGQWYQMNDSSVSLSDIRTVLNQQAYLLFYI 412
Cdd:cd02661   241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
114-411 4.63e-78

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 259.30  E-value: 4.63e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   114 AGLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFC--MMCTMQNHIIQVFANS-GNVIKPISVLNELKRIG 190
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNSkSSSVSPKMFKKSLGKLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   191 KHFRFGSQEDAHEFLRYTVDAMQkSCLPGNKLDRQTQAttfVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKTAQ 270
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLH-EDLNGNHSTENESL---ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   271 TLSK------AFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTnFNGG---KITKDVRYAEHLD 341
Cdd:pfam00443  157 AELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFS-YNRStweKLNTEVEFPLELD 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528495786   342 LRPFMSQ----SHGEPQIYALYAVLVHSGfSCHAGHYYCYIKA-SNGQWYQMNDSSVSLSDIRT-VLNQQAYLLFY 411
Cdd:pfam00443  236 LSRYLAEelkpKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
115-413 7.88e-32

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 135.00  E-value: 7.88e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  115 GLHNLGNTCFLNSTLQCLTYTAPLAN--YMLTREHSKtchePGFCMMCTMQnhiiQVFANSGNVIKPISVLNELKRIG-- 190
Cdd:COG5077   195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPR----GRDSVALALQ----RLFYNLQTGEEPVDTTELTRSFGwd 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  191 --KHFrfgSQEDAHEFLRYTVDAMQKSClpgnkldRQTQATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKT 268
Cdd:COG5077   267 sdDSF---MQHDIQEFNRVLQDNLEKSM-------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  269 AQTLSKAFEQFVKPEQLDGDNAYKCSKcKKMVTASKRFTVHRSSNVLTISLKRFT-NFNGG---KITKDVRYAEHLDLRP 344
Cdd:COG5077   337 MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEyDFERDmmvKINDRYEFPLEIDLLP 415
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  345 FMS----QSHGEPQIYALYAVLVHSGfSCHAGHYYCYIKAS-NGQWYQMNDSSVSLSDIRTVLNQ--------------- 404
Cdd:COG5077   416 FLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdh 494
                         330
                  ....*....|....*.
gi 528495786  405 -------QAYLLFYIR 413
Cdd:COG5077   495 sgikrfmSAYMLVYLR 510
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
844-940 9.33e-07

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 52.97  E-value: 9.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   844 EDRNRGSDRPHFSSTPKDRERYRHyRDHSdRSRSRYGHSYQDSRRSTSRER-YYRDRDLERHWDRFSHHRREHHYFQRRH 922
Cdd:TIGR01642    5 PDREREKSRGRDRDRSSERPRRRS-RDRS-RFRDRHRRSRERSYREDSRPRdRRRYDSRSPRSLRYSSVRRSRDRPRRRS 82
                           90
                   ....*....|....*...
gi 528495786   923 RDERDWNRDRRFGSDSYR 940
Cdd:TIGR01642   83 RSVRSIEQHRRRLRDRSP 100
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
844-933 3.86e-04

Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region found at the C-terminus of plant and metazoan pre-mRNA-splicing factor 38 proteins. The function is not known.


Pssm-ID: 463734 [Multi-domain]  Cd Length: 98  Bit Score: 40.91  E-value: 3.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   844 EDRNRGSDRPHFSSTPKDRERYRHYRdhSDRSRSRYGHSyqdSRRSTSRERYYRDRDLERHWDRFSHHRRehhyfQRRHR 923
Cdd:pfam12871   20 EDEEASDESERASLSRKRRSRSRRRS--STRDRSRSRSR---SRSRDRRSRGTRDRRRDRDRDRYRSLRS-----RSRDR 89
                           90
                   ....*....|
gi 528495786   924 DeRDWNRDRR 933
Cdd:pfam12871   90 S-RDRDRDRR 98
PRK12678 PRK12678
transcription termination factor Rho; Provisional
836-941 2.37e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.20  E-value: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  836 SGDGWRSGEDRNRGSDRPHfsstpKDRERYRHYRDHSDRSRSRYGHSYQDSRRSTSRERYYRDRDLERHWDRfshHRREh 915
Cdd:PRK12678  193 REERGRDGDDRDRRDRREQ-----GDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRG---GRRG- 263
                          90       100
                  ....*....|....*....|....*.
gi 528495786  916 hyfqRRHRDERDWNRDRRFGSDSYRP 941
Cdd:PRK12678  264 ----RRFRDRDRRGRRGGDGGNEREP 285
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
896-1005 6.90e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 40.29  E-value: 6.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   896 YRDRDLERHWDRFSHHRREHHYFQRRHRDeRDWNRDRRFGSDSYRPSGyHNRNGYSNHSHRGMEEAHGRATHTVNGSKGR 975
Cdd:TIGR01622    2 YRDRERERLRDSSSAGDRDRRRDKGRERS-RDRSRDRERSRSRRRDRH-RDRDYYRGRERRSRSRRPNRRYRPREKRRRR 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 528495786   976 PSSphsvSPLPRHHKRKRSPSVDARESSDE 1005
Cdd:TIGR01622   80 GDS----YRRRRDDRRSRREKPRARDGTPE 105
 
Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
113-412 0e+00

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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 543.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  113 GAGLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFCMMCTMQNHIIQVFANSGNVIKPISVLNELKRIGKH 192
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  193 FRFGSQEDAHEFLRYTVDAMQKSCLPGNK----LDRQTQATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKT 268
Cdd:cd02661    81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKklkaVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  269 AQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFNGGKITKDVRYAEHLDLRPFMSQ 348
Cdd:cd02661   161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528495786  349 SHGEPQIYALYAVLVHSGFSCHAGHYYCYIKASNGQWYQMNDSSVSLSDIRTVLNQQAYLLFYI 412
Cdd:cd02661   241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
114-411 4.63e-78

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 259.30  E-value: 4.63e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   114 AGLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFC--MMCTMQNHIIQVFANS-GNVIKPISVLNELKRIG 190
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNSkSSSVSPKMFKKSLGKLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   191 KHFRFGSQEDAHEFLRYTVDAMQkSCLPGNKLDRQTQAttfVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKTAQ 270
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLH-EDLNGNHSTENESL---ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   271 TLSK------AFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTnFNGG---KITKDVRYAEHLD 341
Cdd:pfam00443  157 AELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFS-YNRStweKLNTEVEFPLELD 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528495786   342 LRPFMSQ----SHGEPQIYALYAVLVHSGfSCHAGHYYCYIKA-SNGQWYQMNDSSVSLSDIRT-VLNQQAYLLFY 411
Cdd:pfam00443  236 LSRYLAEelkpKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
115-412 3.67e-71

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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 240.74  E-value: 3.67e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  115 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCH--EPGFCMMCTMQNhIIQVFANSGNVIK--PISVLNELKRIG 190
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLscSPNSCLSCAMDE-IFQEFYYSGDRSPygPINLLYLSWKHS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  191 KHFRFGSQEDAHEFLRYTVDAMQKSCLPGNKLDRQT-QATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIK-- 267
Cdd:cd02660    81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDEsHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPnk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  268 -------------TAQTLSKAFEQFVKPEQLdGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFNGG---KIT 331
Cdd:cd02660   161 stpswalgesgvsGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKID 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  332 KDVRYAEHLDLRPFMSQSHGEPQ---------IYALYAVLVHSGfSCHAGHYYCYIKASNGQWYQMNDSSVSLSDIRTVL 402
Cdd:cd02660   240 TYVQFPLELNMTPYTSSSIGDTQdsnsldpdyTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVL 318
                         330
                  ....*....|
gi 528495786  403 NQQAYLLFYI 412
Cdd:cd02660   319 KSQAYLLFYH 328
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
115-412 7.53e-68

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: 228.52  E-value: 7.53e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  115 GLHNLGNTCFLNSTLQCLtytaplanymltrehsktchepgfcmmctmqnhiiqvfansgnvikpisvlnelkrigkhfr 194
Cdd:cd02257     1 GLNNLGNTCYLNSVLQAL-------------------------------------------------------------- 18
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  195 FGSQEDAHEFLRYTVDAMQKSCLPGNKLDR-QTQATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEI----KTA 269
Cdd:cd02257    19 FSEQQDAHEFLLFLLDKLHEELKKSSKRTSdSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  270 QTLSKAFEQFVKPEQLDGDNAYKCSKCKKmVTASKRFTVHRSSNVLTISLKRFT---NFNGGKITKDVRYAEHLDLRPFM 346
Cdd:cd02257    99 VSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYL 177
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528495786  347 SQ------SHGEPQIYALYAVLVHSGFSCHAGHYYCYIK-ASNGQWYQMNDSSVSLSDIRTVL-----NQQAYLLFYI 412
Cdd:cd02257   178 SEgekdsdSDNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
115-414 4.67e-57

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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 200.95  E-value: 4.67e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  115 GLHNLGNTCFLNSTLQCLTYTAPLANYML----TREHSKTCHEPgfcmmCTMQnhiiQVFANSGNVIKPISVLNELkriG 190
Cdd:cd02659     4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYsippTEDDDDNKSVP-----LALQ----RLFLFLQLSESPVKTTELT---D 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  191 KHFRFGS-------QEDAHEFLRYTVDAMQKsCLPGNKLDRqtqattFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDIS 263
Cdd:cd02659    72 KTRSFGWdslntfeQHDVQEFFRVLFDKLEE-KLKGTGQEG------LIKNLFGGKLVNYIICKECPHESEREEYFLDLQ 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  264 LEIKTAQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFT-NFNGG---KITKDVRYAEH 339
Cdd:cd02659   145 VAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfDFETMmriKINDRFEFPLE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  340 LDLRPFMSQS-----------HGEPQIYALYAVLVHSGfSCHAGHYYCYIK-ASNGQWYQMNDSSVSLSDIRTVLNQQ-- 405
Cdd:cd02659   225 LDMEPYTEKGlakkegdsekkDSESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECfg 303
                         330       340
                  ....*....|....*....|....*....
gi 528495786  406 --------------------AYLLFYIRS 414
Cdd:cd02659   304 geetqktydsgprafkrttnAYMLFYERK 332
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
115-411 5.61e-54

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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 189.91  E-value: 5.61e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  115 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTRehsktchepgfcmmctmqnhiiqvfansgnvikPISVLNELKRIGKHFR 194
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET---------------------------------PKELFSQVCRKAPQFK 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  195 FGSQEDAHEFLRYTVDAMQksclpgnkldrqtqatTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISL----EIKTAQ 270
Cdd:cd02667    48 GYQQQDSHELLRYLLDGLR----------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSEC 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  271 TLSKAFEQFVKPEQLDGDNAYKCSKCKKmvtASKRFTVHRSSNVLTISLKRFT---NFNGGKITKDVRYAEHLDLRPFMS 347
Cdd:cd02667   112 SIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQqprSANLRKVSRHVSFPEILDLAPFCD 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  348 QSHGEPQ-----IYALYAVLVHSGfSCHAGHYYCYIKASN----------------------GQWYQMNDSSVSLSDIRT 400
Cdd:cd02667   189 PKCNSSEdkssvLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVSLEE 267
                         330
                  ....*....|.
gi 528495786  401 VLNQQAYLLFY 411
Cdd:cd02667   268 VLKSEAYLLFY 278
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
115-412 5.64e-53

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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 185.18  E-value: 5.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  115 GLHNLGNTCFLNSTLQCLtytaplanymltrehsktchepgfcmmctmqnhiiqvfansgnvikpisvlnelkrigkhfr 194
Cdd:cd02674     1 GLRNLGNTCYMNSILQCL-------------------------------------------------------------- 18
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  195 FGSQEDAHEFLRYTVDamqksclpgnKLDRqtqattFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEI------KT 268
Cdd:cd02674    19 SADQQDAQEFLLFLLD----------GLHS------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdAP 82
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  269 AQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFNGG--KITKDVRYA-EHLDLRPF 345
Cdd:cd02674    83 KVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGStrKLTTPVTFPlNDLDLTPY 162
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528495786  346 -MSQSHGEPQIYALYAVLVHSGfSCHAGHYYCYIK-ASNGQWYQMNDSSVSLSDIRTVLNQQAYLLFYI 412
Cdd:cd02674   163 vDTRSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
115-411 2.26e-43

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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 160.17  E-value: 2.26e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  115 GLHNLGNTCFLNSTLQCLTYTAPLanymltrehskTCHEPGFCmmctmqnHIIQVFANSGnVIKPISVLNELKRIGKHFR 194
Cdd:cd02663     1 GLENFGNTCYCNSVLQALYFENLL-----------TCLKDLFE-------SISEQKKRTG-VISPKKFITRLKRENELFD 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  195 FGSQEDAHEFLRY-------TVDAMQKSCLPGNKLDRQTQA---TTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISL 264
Cdd:cd02663    62 NYMHQDAHEFLNFllneiaeILDAERKAEKANRKLNNNNNAepqPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  265 EIKTAQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFT-NFNGGKITK-DVRYAEHLDL 342
Cdd:cd02663   142 DVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKyDEQLNRYIKlFYRVVFPLEL 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528495786  343 RPFMSQSHGEP--QIYALYAVLVHSGFSCHAGHYYCYIKaSNGQWYQMNDSSVSLSDIRTVLN--------QQAYLLFY 411
Cdd:cd02663   222 RLFNTTDDAENpdRLYELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFY 299
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
115-420 8.70e-39

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: 147.57  E-value: 8.70e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  115 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTrehsktchepgfcmmCTMQNHIIQVFANSGNVIKPISVLNELKRIGKHFR 194
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE---------------CNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQ 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  195 FGS-------------------QEDAHEFLRYTVDAMQksclpgNKLDRQT--QATTFVHQIFGGYLRSRVKCLNCKAVS 253
Cdd:cd02668    66 FGNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLE------AKLSKSKnpDLKNIVQDLFRGEYSYVTQCSKCGRES 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  254 DTFDPYLDISLEIKTAQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFT----NFNGGK 329
Cdd:cd02668   140 SLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVfdrkTGAKKK 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  330 ITKDVRYAEHLDLRPFMSQSHGEPQIYALYAVLVHSGFSCHAGHYYCYIK-ASNGQWYQMNDSSVSLSDIRTVLNQQAYL 408
Cdd:cd02668   220 LNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDVEEMPGKPLKLGNSED 299
                         330
                  ....*....|..
gi 528495786  409 LFYIRSPDVKNG 420
Cdd:cd02668   300 PAKPRKSEIKKG 311
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
115-411 3.54e-33

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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 131.46  E-value: 3.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  115 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTchEPGFCMMCTMQNHIIQVFANSGNVIKPISVLNELKRiGKHFR 194
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRL--GDSQSVMKKLQLLQAHLMHTQRRAEAPPDYFLEASR-PPWFT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  195 FGSQEDAHEFLRYTVDamqksclpgnKLDrqtqatTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKTAQTLsk 274
Cdd:cd02664    78 PGSQQDCSEYLRYLLD----------RLH------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDL-- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  275 aFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRF-----TNFNgGKITKDV--------------- 334
Cdd:cd02664   140 -LNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFsydqkTHVR-EKIMDNVsinevlslpvrvesk 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  335 ----RYAEHLDLRPFMSQSHGEPQIYALYAVLVHSGFSCHAGHYYCYI---------------------KASNGQWYQMN 389
Cdd:cd02664   218 ssesPLEKKEEESGDDGELVTRQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNWYLFN 297
                         330       340
                  ....*....|....*....|....*....
gi 528495786  390 DSSVSLSDIRTVLN-------QQAYLLFY 411
Cdd:cd02664   298 DSRVTFSSFESVQNvtsrfpkDTPYILFY 326
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
115-413 7.88e-32

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 135.00  E-value: 7.88e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  115 GLHNLGNTCFLNSTLQCLTYTAPLAN--YMLTREHSKtchePGFCMMCTMQnhiiQVFANSGNVIKPISVLNELKRIG-- 190
Cdd:COG5077   195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPR----GRDSVALALQ----RLFYNLQTGEEPVDTTELTRSFGwd 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  191 --KHFrfgSQEDAHEFLRYTVDAMQKSClpgnkldRQTQATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKT 268
Cdd:COG5077   267 sdDSF---MQHDIQEFNRVLQDNLEKSM-------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  269 AQTLSKAFEQFVKPEQLDGDNAYKCSKcKKMVTASKRFTVHRSSNVLTISLKRFT-NFNGG---KITKDVRYAEHLDLRP 344
Cdd:COG5077   337 MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEyDFERDmmvKINDRYEFPLEIDLLP 415
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  345 FMS----QSHGEPQIYALYAVLVHSGfSCHAGHYYCYIKAS-NGQWYQMNDSSVSLSDIRTVLNQ--------------- 404
Cdd:COG5077   416 FLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdh 494
                         330
                  ....*....|....*.
gi 528495786  405 -------QAYLLFYIR 413
Cdd:COG5077   495 sgikrfmSAYMLVYLR 510
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
115-413 4.22e-30

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 121.06  E-value: 4.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  115 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTRehsktchePGFCMMCTMQ----NHIIQVFANSGNVIKPISVLNELKrIG 190
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILALYLPKLDELLDD--------LSKELKVLKNvirkPEPDLNQEEALKLFTALWSSKEHK-VG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  191 KHFRFGSQEDAHEFLRYTVDAMqksclpgnKLDRQTQATTFVHQIFGGYLRSrvkclnckAVSDTFDpyLDISLEIKTAQ 270
Cdd:COG5533    72 WIPPMGSQEDAHELLGKLLDEL--------KLDLVNSFTIRIFKTTKDKKKT--------STGDWFD--IIIELPDQTWV 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  271 TLSKAFEQFVKP--EQLD-------GDNAYKCSKCKKMVTASKRftvhRSSNVLTISLKRFTNFNGG-KITKDVRYAEHL 340
Cdd:COG5533   134 NNLKTLQEFIDNmeELVDdetgvkaKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANLGGNqKIDTEVDEKFEL 209
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528495786  341 DLRPFMSQSHGEPQIYALYAVLVHSGfSCHAGHYYCYIKaSNGQWYQMNDSSVSLSDIRTVLN---QQAYLLFYIR 413
Cdd:COG5533   210 PVKHDQILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
115-411 6.89e-29

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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 118.58  E-value: 6.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  115 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTC--HEPGFCMMCTM--------------QNHIIQVFANSGNVIK 178
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSdvVDPANDLNCQLikladgllsgryskPASLKSENDPYQVGIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  179 PISvlneLKR-IGK-HFRFGS--QEDAHEFLRYTVDAMQKSCLPGNKLDRQTqattfvhqIFGGYLRSRVKCLNCKAVSD 254
Cdd:cd02658    81 PSM----FKAlIGKgHPEFSTmrQQDALEFLLHLIDKLDRESFKNLGLNPND--------LFKFMIEDRLECLSCKKVKY 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  255 TFDPYLDISL--------------EIKTAQTLSKAFEQFVKPEQLDgdnaYKCSKCKKMVTASKRFTVHRSSNVLTISLK 320
Cdd:cd02658   149 TSELSEILSLpvpkdeatekeegeLVYEPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMK 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  321 RFT---NFNGGKITKDVRYAEHLDlrpfmsqshgePQIYALYAVLVHSGFSCHAGHYYCYIK---ASNGQWYQMNDSSVS 394
Cdd:cd02658   225 RFQlleNWVPKKLDVPIDVPEELG-----------PGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVV 293
                         330
                  ....*....|....*..
gi 528495786  395 LSDIRTVLNQQAYLLFY 411
Cdd:cd02658   294 ASQDPPEMKKLGYIYFY 310
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
114-411 1.90e-27

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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 114.60  E-value: 1.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  114 AGLHNLGNTCFLNSTLQCLTYtAP--LAN--YMLTREHSKTCHEPGFcmmctMQNHiiQVFANSGNVIKPISVLNELKRI 189
Cdd:cd02671    25 VGLNNLGNTCYLNSVLQVLYF-CPgfKHGlkHLVSLISSVEQLQSSF-----LLNP--EKYNDELANQAPRRLLNALREV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  190 GKHFRFGSQEDAHEFLRYTVDAMQKsclpgnkldrqtqattFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKTA 269
Cdd:cd02671    97 NPMYEGYLQHDAQEVLQCILGNIQE----------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQES 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  270 Q-------------------TLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFN---- 326
Cdd:cd02671   161 ElskseesseispdpktemkTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGsefd 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  327 -GGKITKDVRYAehldLRPFMSQSHG-----EPQIYALYAVLVHSGFSCHAGHYYCYIKasngqWYQMNDSSVSLSDIRT 400
Cdd:cd02671   241 cYGGLSKVNTPL----LTPLKLSLEEwstkpKNDVYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKD 311
                         330       340
                  ....*....|....*....|
gi 528495786  401 VLN---------QQAYLLFY 411
Cdd:cd02671   312 FLEalspntsstSTPYLLFY 331
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
115-394 4.13e-23

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 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: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 101.25  E-value: 4.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  115 GLHNLGNTCFLNSTLQCLtYTAP-----LANYMLTREHSKTCHEPGFCMMctmqNHIIQVFANSGNVIKPISVLNELKRI 189
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCL-RSVPelrdaLKNYNPARRGANQSSDNLTNAL----RDLFDTMDKKQEPVPPIEFLQLLRMA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  190 GKHF----RFG--SQEDAHEFLRYTVDAMQkSCLPGNKLDRQtqattFVHQIFGGYLRSRVKCL-NCKAVSDTFDP---- 258
Cdd:cd02657    76 FPQFaekqNQGgyAQQDAEECWSQLLSVLS-QKLPGAGSKGS-----FIDQLFGIELETKMKCTeSPDEEEVSTESeykl 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  259 --YLDISLEIKTAQT-LSKAF-EQFVKPEQLDGDNAykcskckkmvTASKRFTVHRSSNVLTISLKRF-----TNFNgGK 329
Cdd:cd02657   150 qcHISITTEVNYLQDgLKKGLeEEIEKHSPTLGRDA----------IYTKTSRISRLPKYLTVQFVRFfwkrdIQKK-AK 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528495786  330 ITKDVRYAEHLDLRPFMSQShgepQIYALYAVLVHSGFSCHAGHYYCYIKASN-GQWYQMNDSSVS 394
Cdd:cd02657   219 ILRKVKFPFELDLYELCTPS----GYYELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDDKVS 280
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
115-411 3.99e-20

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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 90.89  E-value: 3.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  115 GLHNLGNTCFLNSTLQCLtytAPLanymltrehsktchePGFcmmctmqnhiiqvfansgnvikpISVLNELKrigkhfr 194
Cdd:cd02662     1 GLVNLGNTCFMNSVLQAL---ASL---------------PSL-----------------------IEYLEEFL------- 32
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  195 fgSQEDAHEFLRYTVDAMQKSCLpgnkldrqtqattfvhQIFGGYLRSRVKCLNCKAVS-DTFDPYLDISL-----EIKT 268
Cdd:cd02662    33 --EQQDAHELFQVLLETLEQLLK----------------FPFDGLLASRIVCLQCGESSkVRYESFTMLSLpvpnqSSGS 94
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  269 AQTLSKAFEQFVKPEQLDGdnaYKCSKCKKMVTASKRftvhrssnVLTISLKRFTnFNG-GKITKD---VRYAEHLDlrp 344
Cdd:cd02662    95 GTTLEHCLDDFLSTEIIDD---YKCDRCQTVIVRLPQ--------ILCIHLSRSV-FDGrGTSTKNsckVSFPERLP--- 159
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  345 fmsqshgePQIYALYAVLVHSGfSCHAGHYYCY--------------------IKASN-GQWYQMNDSSVSLSDIRTVLN 403
Cdd:cd02662   160 --------KVLYRLRAVVVHYG-SHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTsHPWWRISDTTVKEVSESEVLE 230

                  ....*....
gi 528495786  404 Q-QAYLLFY 411
Cdd:cd02662   231 QkSAYMLFY 239
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
271-413 1.82e-18

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 91.48  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  271 TLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFNGG--KITKDVRYA-EHLDLRPFMS 347
Cdd:COG5560   676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFrdKIDDLVEYPiDDLDLSGVEY 755
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528495786  348 QSHGEPQIYALYAVLVHSGFScHAGHYYCYIK-ASNGQWYQMNDSSVSLSDIRTVLNQQAYLLFYIR 413
Cdd:COG5560   756 MVDDPRLIYDLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
115-274 2.71e-14

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 77.62  E-value: 2.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  115 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFCMM-----CTMQNHIIQVFANSGNVIKPISVLNELKRI 189
Cdd:COG5560   267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMhgsvaSAYADLIKQLYDGNLHAFTPSGFKKTIGSF 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  190 GKHFRFGSQEDAHEFLRYTVDAMQK--------------SCLPGNKLDRQTQAT-----------TFVHQIFGGYLRSRV 244
Cdd:COG5560   347 NEEFSGYDQQDSQEFIAFLLDGLHEdlnriikkpytskpDLSPGDDVVVKKKAKecwwehlkrndSIITDLFQGMYKSTL 426
                         170       180       190
                  ....*....|....*....|....*....|
gi 528495786  245 KCLNCKAVSDTFDPYLDISLEIKTAQTLSK 274
Cdd:COG5560   427 TCPGCGSVSITFDPFMDLTLPLPVSMVWKH 456
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
114-393 6.94e-12

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 67.68  E-value: 6.94e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   114 AGLHNLGNTCFLNSTLQCLTYTAPLANYMLtrEHSKTCHEPGFCMMC-------TMQNhiiqvfANSGNV-----IKPIS 181
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLAL--SHLATECLKEHCLLCelgflfdMLEK------AKGKNCqasnfLRALS 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   182 VLNELKRIGKHFRFGSQEDAHE-------FLRYTVDAMQKSCLPGNKldRQTQATTFVHQIFGGYLRSRVKCLNCKAVSD 254
Cdd:pfam13423   73 SIPEASALGLLDEDRETNSAISlssliqsFNRFLLDQLSSEENSTPP--NPSPAESPLEQLFGIDAETTIRCSNCGHESV 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   255 TFDPYLDISL------EIKTAQTLSKAFEQFVKpEQLDGDNAYK--CSKCKKMVTASKRFTVHRSSNVLTISLKrFTNFN 326
Cdd:pfam13423  151 RESSTHVLDLiyprkpSSNNKKPPNQTFSSILK-SSLERETTTKawCEKCKRYQPLESRRTVRNLPPVLSLNAA-LTNEE 228
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528495786   327 GGKITKDVRY-AEHLDLRPFM-SQSHGEPQIYALYAVLVHSGFSCHAGHYYCYIKASN--------GQWYQMNDSSV 393
Cdd:pfam13423  229 WRQLWKTPGWlPPEIGLTLSDdLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKVADseledpteSQWYLFNDFLV 305
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
116-411 6.70e-11

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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 64.09  E-value: 6.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  116 LHNLGNTCFLNSTLQCLTYTaplanymltrehsktchepgfcmmctmqNHIIQVFANSgnvikpisvlnelkrigkhfrf 195
Cdd:cd02673     2 LVNTGNSCYFNSTMQALSSI----------------------------GKINTEFDND---------------------- 31
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  196 gSQEDAHEFLRYTVDAMQKscLPGNKLDRQTQATTFVHQI-----FGGYLRSRVKCLNCK--AVSDTFDPYLDIS---LE 265
Cdd:cd02673    32 -DQQDAHEFLLTLLEAIDD--IMQVNRTNVPPSNIEIKRLnpleaFKYTIESSYVCIGCSfeENVSDVGNFLDVSmidNK 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  266 IKTAQTLSKAFEQFVKPEQldgdnayKCSKCK-KMVTASKRFTvhRSSNVLTISLKRFtnfnggkitkDVRYAEHLDL-- 342
Cdd:cd02673   109 LDIDELLISNFKTWSPIEK-------DCSSCKcESAISSERIM--TFPECLSINLKRY----------KLRIATSDYLkk 169
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528495786  343 -RPFMSQSHGEPQIYALYAVLVHSGFSCHAGHYYCYIKAS--NGQWYQMNDSS---VSLSDIRTVLNQQAYLLFY 411
Cdd:cd02673   170 nEEIMKKYCGTDAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEirpVSKNDVSTNARSSGYLIFY 244
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
115-394 1.59e-10

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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 64.65  E-value: 1.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  115 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFcmmctmqnHIIQVFA-------NSGN---VIKPISVLN 184
Cdd:cd02669   121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKS--------ELVKRLSelirkiwNPRNfkgHVSPHELLQ 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  185 EL-KRIGKHFRFGSQEDAHEFLRYTVDAMqKSCLPGNKLDRQTQattfVHQIFGGYLR--------------SRVKCLNC 249
Cdd:cd02669   193 AVsKVSKKKFSITEQSDPVEFLSWLLNTL-HKDLGGSKKPNSSI----IHDCFQGKVQietqkikphaeeegSKDKFFKD 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  250 KAVSDTFD-PYLDISLEIKTA-----QTLSKAFEQFVKPEQLDGdnaYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFT 323
Cdd:cd02669   268 SRVKKTSVsPFLLLTLDLPPPplfkdGNEENIIPQVPLKQLLKK---YDGKTETELKDSLKRYLISRLPKYLIFHIKRFS 344
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528495786  324 --NFNGGKITKDVRY-AEHLDLRPFMSQ---SHGEPQIYALYAVLVHSGFSCHAGHYYCYI-KASNGQWYQMNDSSVS 394
Cdd:cd02669   345 knNFFKEKNPTIVNFpIKNLDLSDYVHFdkpSLNLSTKYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQDLNVK 422
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
114-412 2.37e-08

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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 57.50  E-value: 2.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  114 AGLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTchepgfcmmcTMQNHIIQVFANSGNVIKPISVL------NELK 187
Cdd:cd02666     2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKA----------ELASDYPTERRIGGREVSRSELQrsnqfvYELR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  188 RIGKH-------------------FRfgsQEDAHE------FLRYTVDAMQKSCLPGNKLDRQTQATTFVHQIF-GGYLR 241
Cdd:cd02666    72 SLFNDlihsntrsvtpskelaylaLR---QQDVTEcidnvlFQLEVALEPISNAFAGPDTEDDKEQSDLIKRLFsGKTKQ 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  242 SRVKCLNCKAVSDTFDPYLDISLEIKT------------AQTLSKAFEQFVKPEQL-----DGDNAYKCSKCK-KMVTAS 303
Cdd:cd02666   149 QLVPESMGNQPSVRTKTERFLSLLVDVgkkgreivvllePKDLYDALDRYFDYDSLtklpqRSQVQAQLAQPLqRELISM 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  304 KRFTVHRSSN-VLTISLKRFTNFNGGKITKDVRYAEHLDLRPfmSQSHGEPQI-YALYAVLVHSGfSCHAGHYYCYIK-A 380
Cdd:cd02666   229 DRYELPSSIDdIDELIREAIQSESSLVRQAQNELAELKHEIE--KQFDDLKSYgYRLHAVFIHRG-EASSGHYWVYIKdF 305
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 528495786  381 SNGQWYQMNDSSVSLSDIRTVLNQ------QAYLLFYI 412
Cdd:cd02666   306 EENVWRKYNDETVTVVPASEVFLFtlgntaTPYFLVYV 343
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
844-940 9.33e-07

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 52.97  E-value: 9.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   844 EDRNRGSDRPHFSSTPKDRERYRHyRDHSdRSRSRYGHSYQDSRRSTSRER-YYRDRDLERHWDRFSHHRREHHYFQRRH 922
Cdd:TIGR01642    5 PDREREKSRGRDRDRSSERPRRRS-RDRS-RFRDRHRRSRERSYREDSRPRdRRRYDSRSPRSLRYSSVRRSRDRPRRRS 82
                           90
                   ....*....|....*...
gi 528495786   923 RDERDWNRDRRFGSDSYR 940
Cdd:TIGR01642   83 RSVRSIEQHRRRLRDRSP 100
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
845-937 2.61e-06

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 51.46  E-value: 2.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   845 DRNRGSDRPhfSSTPKDRERYRHYRDHSDRSRSRyghsyqDSRRSTSRER-YYRDRDLERHWDRFSHHRREHHYFQRRHR 923
Cdd:TIGR01622    4 DRERERLRD--SSSAGDRDRRRDKGRERSRDRSR------DRERSRSRRRdRHRDRDYYRGRERRSRSRRPNRRYRPREK 75
                           90
                   ....*....|....
gi 528495786   924 DERDWNRDRRFGSD 937
Cdd:TIGR01622   76 RRRRGDSYRRRRDD 89
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
314-412 2.61e-06

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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 49.86  E-value: 2.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  314 VLTISLKRFtNFNGGKITKdvryaEHLDLR-PFMSQSHGepqiYALYAVLVHSGfSCHAGHYYCYI-KASNGQWYQMNDS 391
Cdd:cd02665   131 VLTFELSRF-EFNQGRPEK-----IHDKLEfPQIIQQVP----YELHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYNDI 199
                          90       100
                  ....*....|....*....|....*....
gi 528495786  392 SVSLSDIRTV--------LNQQAYLLFYI 412
Cdd:cd02665   200 SVTESSWEEVerdsfgggRNPSAYCLMYI 228
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
860-949 6.95e-06

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 49.92  E-value: 6.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   860 KDRERYRHYRDHSDRSRSRyghsyqdsRRSTSREryyRDRDLERHWDRFSHHRREhhyfqrRHRDeRDWNRDRRFGSDSY 939
Cdd:TIGR01622    3 RDRERERLRDSSSAGDRDR--------RRDKGRE---RSRDRSRDRERSRSRRRD------RHRD-RDYYRGRERRSRSR 64
                           90
                   ....*....|
gi 528495786   940 RPSGYHNRNG 949
Cdd:TIGR01622   65 RPNRRYRPRE 74
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
883-1003 1.29e-05

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 49.12  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   883 YQDSRRSTSRERYyRDRDLERHWDRfshhRREHHYFQRRHRderdWNRDRRFGSDSyRPsgyHNRNGYSNHSHRGMEEAH 962
Cdd:TIGR01642    4 EPDREREKSRGRD-RDRSSERPRRR----SRDRSRFRDRHR----RSRERSYREDS-RP---RDRRRYDSRSPRSLRYSS 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 528495786   963 GRATHTVNGSKGRPSSPHSVSplpRHHKRKRSPSVDARESS 1003
Cdd:TIGR01642   71 VRRSRDRPRRRSRSVRSIEQH---RRRLRDRSPSNQWRKDD 108
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
860-957 3.69e-05

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 47.58  E-value: 3.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   860 KDRERYRHYRDHSDRSRSRYGHSYQDSRRSTSRERYYRDRDLERHWDRFSHHRREHHYFQRRHRDERDWNRDRrfgSDSY 939
Cdd:TIGR01642    1 RDEEPDREREKSRGRDRDRSSERPRRRSRDRSRFRDRHRRSRERSYREDSRPRDRRRYDSRSPRSLRYSSVRR---SRDR 77
                           90
                   ....*....|....*...
gi 528495786   940 RPSGYHNRNGYSNHSHRG 957
Cdd:TIGR01642   78 PRRRSRSVRSIEQHRRRL 95
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
860-953 4.22e-05

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 47.61  E-value: 4.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   860 KDRERYRHYRDHSDRSRSRYGHSYQDSRRSTSRERYyRDRDLERHWDRFSHHRREhhyfqRRHRDERDWNRDRRFGSDSY 939
Cdd:TIGR01622    5 RERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERS-RSRRRDRHRDRDYYRGRE-----RRSRSRRPNRRYRPREKRRR 78
                           90
                   ....*....|....
gi 528495786   940 RPSGYHNRNGYSNH 953
Cdd:TIGR01622   79 RGDSYRRRRDDRRS 92
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
823-933 2.16e-04

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 45.30  E-value: 2.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   823 SKEAKPSHSDKFGSGDGWRSGEDRNRGSDRPHFSSTPKDRERYRH-----YRDHSDRSRSRYGHSYQDSRRSTSR--ERY 895
Cdd:TIGR01622    4 DRERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRRRDRHrdrdyYRGRERRSRSRRPNRRYRPREKRRRrgDSY 83
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 528495786   896 YRDRDLERhwdrfshHRREHHYFQRRHRDE-RDWNRDRR 933
Cdd:TIGR01622   84 RRRRDDRR-------SRREKPRARDGTPEPlTEDERDRR 115
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
844-933 3.86e-04

Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region found at the C-terminus of plant and metazoan pre-mRNA-splicing factor 38 proteins. The function is not known.


Pssm-ID: 463734 [Multi-domain]  Cd Length: 98  Bit Score: 40.91  E-value: 3.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   844 EDRNRGSDRPHFSSTPKDRERYRHYRdhSDRSRSRYGHSyqdSRRSTSRERYYRDRDLERHWDRFSHHRRehhyfQRRHR 923
Cdd:pfam12871   20 EDEEASDESERASLSRKRRSRSRRRS--STRDRSRSRSR---SRSRDRRSRGTRDRRRDRDRDRYRSLRS-----RSRDR 89
                           90
                   ....*....|
gi 528495786   924 DeRDWNRDRR 933
Cdd:pfam12871   90 S-RDRDRDRR 98
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
819-904 9.65e-04

Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region found at the C-terminus of plant and metazoan pre-mRNA-splicing factor 38 proteins. The function is not known.


Pssm-ID: 463734 [Multi-domain]  Cd Length: 98  Bit Score: 39.76  E-value: 9.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   819 SEGESKEAKPSHSDKFGSGDGWRSGEDRNRGSDRPHFSSTPKDRERYRHYRDHSDRSRSRYgHSYQDSRRSTSRERyYRD 898
Cdd:pfam12871   15 EEDEEEDEEASDESERASLSRKRRSRSRRRSSTRDRSRSRSRSRSRDRRSRGTRDRRRDRD-RDRYRSLRSRSRDR-SRD 92

                   ....*.
gi 528495786   899 RDLERH 904
Cdd:pfam12871   93 RDRDRR 98
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
823-944 1.89e-03

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 42.19  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   823 SKEAKPSHSDKFGSGDGWRSGEDRNRGSDRPHFSSTPKDRERYRHYRDHSDRSRSRYGHSYQDSRRSTSRERyYRDRDLe 902
Cdd:TIGR01642    8 EREKSRGRDRDRSSERPRRRSRDRSRFRDRHRRSRERSYREDSRPRDRRRYDSRSPRSLRYSSVRRSRDRPR-RRSRSV- 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 528495786   903 rhwDRFSHHRREHHYFQRRHRDERDWNrdRRFGSDsYRPSGY 944
Cdd:TIGR01642   86 ---RSIEQHRRRLRDRSPSNQWRKDDK--KRSLWD-IKPPGY 121
PRK12678 PRK12678
transcription termination factor Rho; Provisional
836-941 2.37e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.20  E-value: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  836 SGDGWRSGEDRNRGSDRPHfsstpKDRERYRHYRDHSDRSRSRYGHSYQDSRRSTSRERYYRDRDLERHWDRfshHRREh 915
Cdd:PRK12678  193 REERGRDGDDRDRRDRREQ-----GDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRG---GRRG- 263
                          90       100
                  ....*....|....*....|....*.
gi 528495786  916 hyfqRRHRDERDWNRDRRFGSDSYRP 941
Cdd:PRK12678  264 ----RRFRDRDRRGRRGGDGGNEREP 285
PRK12678 PRK12678
transcription termination factor Rho; Provisional
819-937 3.88e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.43  E-value: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786  819 SEGESKEAKPSHSDKFGSGDGWRSGEDRNRGSDRphfsstpKDRERYRHYRDHSDRSRSRYGHSYQDSRRSTSRERYYRD 898
Cdd:PRK12678  167 EERDERRRRGDREDRQAEAERGERGRREERGRDG-------DDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDAR 239
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 528495786  899 RDLERHWDRFSHHRREHHYFQRRHRDERDWNRDRRFGSD 937
Cdd:PRK12678  240 GDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGD 278
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
896-1005 6.90e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 40.29  E-value: 6.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528495786   896 YRDRDLERHWDRFSHHRREHHYFQRRHRDeRDWNRDRRFGSDSYRPSGyHNRNGYSNHSHRGMEEAHGRATHTVNGSKGR 975
Cdd:TIGR01622    2 YRDRERERLRDSSSAGDRDRRRDKGRERS-RDRSRDRERSRSRRRDRH-RDRDYYRGRERRSRSRRPNRRYRPREKRRRR 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 528495786   976 PSSphsvSPLPRHHKRKRSPSVDARESSDE 1005
Cdd:TIGR01622   80 GDS----YRRRRDDRRSRREKPRARDGTPE 105
 
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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