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Conserved domains on  [gi|28502773|gb|AAH47168|]
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Usp42 protein, partial [Danio rerio]

Protein Classification

ubiquitin carboxyl-terminal hydrolase family protein( domain architecture ID 10119183)

ubiquitin carboxyl-terminal hydrolase family protein is a C19 family peptidase that may deubiquitinate polyubiquitinated target proteins

CATH:  3.90.70.10
EC:  3.4.19.12
Gene Ontology:  GO:0016579|GO:0004843
MEROPS:  C19
PubMed:  7845226|11517925
SCOP:  4003158

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 ...
82-381 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: 542.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   82 GAGLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFCMMCTMQNHIIQVFANSGNVIKPISVLNELKRIGKH 161
Cdd:cd02661    1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  162 FRFGSQEDAHEFLRYTVDAMQKSCLPGNK----LDRQTQATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKT 237
Cdd:cd02661   81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKklkaVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  238 AQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFNGGKITKDVRYAEHLDLRPFMSQ 317
Cdd:cd02661  161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28502773  318 SHGEPQIYALYAVLVHSGFSCHAGHYYCYIKASNGQWYQMNDSSVSLSDIRTVLNQQAYLLFYI 381
Cdd:cd02661  241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
U2AF_lg super family cl36941
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
813-909 6.97e-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: 6.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    813 EDRNRGSDRPHFSSTPKDRERYRHyRDHSdRSRSRYGHSYQDSRRSTSRER-YYRDRDLERHWDRFSHHRREHHYFQRRH 891
Cdd:TIGR01642    5 PDREREKSRGRDRDRSSERPRRRS-RDRS-RFRDRHRRSRERSYREDSRPRdRRRYDSRSPRSLRYSSVRRSRDRPRRRS 82
                           90
                   ....*....|....*...
gi 28502773    892 RDERDWNRDRRFGSDSYR 909
Cdd:TIGR01642   83 RSVRSIEQHRRRLRDRSP 100
SF-CC1 super family cl36939
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
865-974 5.13e-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: 40.67  E-value: 5.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    865 YRDRDLERHWDRFSHHRREHHYFQRRHRDeRDWNRDRRFGSDSYRPSGyHNRNGYSNHSHRGMEEAHGRATHTVNGSKGR 944
Cdd:TIGR01622    2 YRDRERERLRDSSSAGDRDRRRDKGRERS-RDRSRDRERSRSRRRDRH-RDRDYYRGRERRSRSRRPNRRYRPREKRRRR 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 28502773    945 PSSphsvSPLPRHHKRKRSPSVDARESSDE 974
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 ...
82-381 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: 542.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   82 GAGLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFCMMCTMQNHIIQVFANSGNVIKPISVLNELKRIGKH 161
Cdd:cd02661    1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  162 FRFGSQEDAHEFLRYTVDAMQKSCLPGNK----LDRQTQATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKT 237
Cdd:cd02661   81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKklkaVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  238 AQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFNGGKITKDVRYAEHLDLRPFMSQ 317
Cdd:cd02661  161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28502773  318 SHGEPQIYALYAVLVHSGFSCHAGHYYCYIKASNGQWYQMNDSSVSLSDIRTVLNQQAYLLFYI 381
Cdd:cd02661  241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
83-380 1.89e-78

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 258.91  E-value: 1.89e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773     83 AGLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFC--MMCTMQNHIIQVFANS-GNVIKPISVLNELKRIG 159
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNSkSSSVSPKMFKKSLGKLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    160 KHFRFGSQEDAHEFLRYTVDAMQkSCLPGNKLDRQTQAttfVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKTAQ 239
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLH-EDLNGNHSTENESL---ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    240 TLSK------AFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTnFNGG---KITKDVRYAEHLD 310
Cdd:pfam00443  157 AELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFS-YNRStweKLNTEVEFPLELD 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28502773    311 LRPFMSQ----SHGEPQIYALYAVLVHSGfSCHAGHYYCYIKA-SNGQWYQMNDSSVSLSDIRT-VLNQQAYLLFY 380
Cdd:pfam00443  236 LSRYLAEelkpKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
84-382 4.34e-32

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 135.38  E-value: 4.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   84 GLHNLGNTCFLNSTLQCLTYTAPLAN--YMLTREHSKtchePGFCMMCTMQnhiiQVFANSGNVIKPISVLNELKRIG-- 159
Cdd:COG5077  195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPR----GRDSVALALQ----RLFYNLQTGEEPVDTTELTRSFGwd 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  160 --KHFrfgSQEDAHEFLRYTVDAMQKSClpgnkldRQTQATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKT 237
Cdd:COG5077  267 sdDSF---MQHDIQEFNRVLQDNLEKSM-------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  238 AQTLSKAFEQFVKPEQLDGDNAYKCSKcKKMVTASKRFTVHRSSNVLTISLKRFT-NFNGG---KITKDVRYAEHLDLRP 313
Cdd:COG5077  337 MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEyDFERDmmvKINDRYEFPLEIDLLP 415
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  314 FMS----QSHGEPQIYALYAVLVHSGfSCHAGHYYCYIKAS-NGQWYQMNDSSVSLSDIRTVLNQ--------------- 373
Cdd:COG5077  416 FLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdh 494
                        330
                 ....*....|....*.
gi 28502773  374 -------QAYLLFYIR 382
Cdd:COG5077  495 sgikrfmSAYMLVYLR 510
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
813-909 6.97e-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: 6.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    813 EDRNRGSDRPHFSSTPKDRERYRHyRDHSdRSRSRYGHSYQDSRRSTSRER-YYRDRDLERHWDRFSHHRREHHYFQRRH 891
Cdd:TIGR01642    5 PDREREKSRGRDRDRSSERPRRRS-RDRS-RFRDRHRRSRERSYREDSRPRdRRRYDSRSPRSLRYSSVRRSRDRPRRRS 82
                           90
                   ....*....|....*...
gi 28502773    892 RDERDWNRDRRFGSDSYR 909
Cdd:TIGR01642   83 RSVRSIEQHRRRLRDRSP 100
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
813-902 1.39e-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: 42.07  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    813 EDRNRGSDRPHFSSTPKDRERYRHYRdhSDRSRSRYGHSyqdSRRSTSRERYYRDRDLERHWDRFSHHRRehhyfQRRHR 892
Cdd:pfam12871   20 EDEEASDESERASLSRKRRSRSRRRS--STRDRSRSRSR---SRSRDRRSRGTRDRRRDRDRDRYRSLRS-----RSRDR 89
                           90
                   ....*....|
gi 28502773    893 DeRDWNRDRR 902
Cdd:pfam12871   90 S-RDRDRDRR 98
PRK12678 PRK12678
transcription termination factor Rho; Provisional
805-910 1.79e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.20  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   805 SGDGWRSGEDRNRGSDRPHfsstpKDRERYRHYRDHSDRSRSRYGHSYQDSRRSTSRERYYRDRDLERHWDRfshHRREh 884
Cdd:PRK12678  193 REERGRDGDDRDRRDRREQ-----GDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRG---GRRG- 263
                          90       100
                  ....*....|....*....|....*.
gi 28502773   885 hyfqRRHRDERDWNRDRRFGSDSYRP 910
Cdd:PRK12678  264 ----RRFRDRDRRGRRGGDGGNEREP 285
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
865-974 5.13e-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: 40.67  E-value: 5.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    865 YRDRDLERHWDRFSHHRREHHYFQRRHRDeRDWNRDRRFGSDSYRPSGyHNRNGYSNHSHRGMEEAHGRATHTVNGSKGR 944
Cdd:TIGR01622    2 YRDRERERLRDSSSAGDRDRRRDKGRERS-RDRSRDRERSRSRRRDRH-RDRDYYRGRERRSRSRRPNRRYRPREKRRRR 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 28502773    945 PSSphsvSPLPRHHKRKRSPSVDARESSDE 974
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 ...
82-381 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: 542.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   82 GAGLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFCMMCTMQNHIIQVFANSGNVIKPISVLNELKRIGKH 161
Cdd:cd02661    1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  162 FRFGSQEDAHEFLRYTVDAMQKSCLPGNK----LDRQTQATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKT 237
Cdd:cd02661   81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKklkaVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  238 AQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFNGGKITKDVRYAEHLDLRPFMSQ 317
Cdd:cd02661  161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28502773  318 SHGEPQIYALYAVLVHSGFSCHAGHYYCYIKASNGQWYQMNDSSVSLSDIRTVLNQQAYLLFYI 381
Cdd:cd02661  241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
83-380 1.89e-78

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 258.91  E-value: 1.89e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773     83 AGLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFC--MMCTMQNHIIQVFANS-GNVIKPISVLNELKRIG 159
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNSkSSSVSPKMFKKSLGKLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    160 KHFRFGSQEDAHEFLRYTVDAMQkSCLPGNKLDRQTQAttfVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKTAQ 239
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLH-EDLNGNHSTENESL---ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    240 TLSK------AFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTnFNGG---KITKDVRYAEHLD 310
Cdd:pfam00443  157 AELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFS-YNRStweKLNTEVEFPLELD 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28502773    311 LRPFMSQ----SHGEPQIYALYAVLVHSGfSCHAGHYYCYIKA-SNGQWYQMNDSSVSLSDIRT-VLNQQAYLLFY 380
Cdd:pfam00443  236 LSRYLAEelkpKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
84-381 1.15e-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: 241.12  E-value: 1.15e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   84 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCH--EPGFCMMCTMQNhIIQVFANSGNVIK--PISVLNELKRIG 159
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLscSPNSCLSCAMDE-IFQEFYYSGDRSPygPINLLYLSWKHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  160 KHFRFGSQEDAHEFLRYTVDAMQKSCLPGNKLDRQT-QATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIK-- 236
Cdd:cd02660   81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDEsHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPnk 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  237 -------------TAQTLSKAFEQFVKPEQLdGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFNGG---KIT 300
Cdd:cd02660  161 stpswalgesgvsGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKID 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  301 KDVRYAEHLDLRPFMSQSHGEPQ---------IYALYAVLVHSGfSCHAGHYYCYIKASNGQWYQMNDSSVSLSDIRTVL 371
Cdd:cd02660  240 TYVQFPLELNMTPYTSSSIGDTQdsnsldpdyTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVL 318
                        330
                 ....*....|
gi 28502773  372 NQQAYLLFYI 381
Cdd:cd02660  319 KSQAYLLFYH 328
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
84-381 3.53e-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: 3.53e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   84 GLHNLGNTCFLNSTLQCLtytaplanymltrehsktchepgfcmmctmqnhiiqvfansgnvikpisvlnelkrigkhfr 163
Cdd:cd02257    1 GLNNLGNTCYLNSVLQAL-------------------------------------------------------------- 18
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  164 FGSQEDAHEFLRYTVDAMQKSCLPGNKLDR-QTQATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEI----KTA 238
Cdd:cd02257   19 FSEQQDAHEFLLFLLDKLHEELKKSSKRTSdSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  239 QTLSKAFEQFVKPEQLDGDNAYKCSKCKKmVTASKRFTVHRSSNVLTISLKRFT---NFNGGKITKDVRYAEHLDLRPFM 315
Cdd:cd02257   99 VSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYL 177
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28502773  316 SQ------SHGEPQIYALYAVLVHSGFSCHAGHYYCYIK-ASNGQWYQMNDSSVSLSDIRTVL-----NQQAYLLFYI 381
Cdd:cd02257  178 SEgekdsdSDNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
84-383 2.73e-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: 2.73e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   84 GLHNLGNTCFLNSTLQCLTYTAPLANYML----TREHSKTCHEPgfcmmCTMQnhiiQVFANSGNVIKPISVLNELkriG 159
Cdd:cd02659    4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYsippTEDDDDNKSVP-----LALQ----RLFLFLQLSESPVKTTELT---D 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  160 KHFRFGS-------QEDAHEFLRYTVDAMQKsCLPGNKLDRqtqattFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDIS 232
Cdd:cd02659   72 KTRSFGWdslntfeQHDVQEFFRVLFDKLEE-KLKGTGQEG------LIKNLFGGKLVNYIICKECPHESEREEYFLDLQ 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  233 LEIKTAQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFT-NFNGG---KITKDVRYAEH 308
Cdd:cd02659  145 VAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfDFETMmriKINDRFEFPLE 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  309 LDLRPFMSQS-----------HGEPQIYALYAVLVHSGfSCHAGHYYCYIK-ASNGQWYQMNDSSVSLSDIRTVLNQQ-- 374
Cdd:cd02659  225 LDMEPYTEKGlakkegdsekkDSESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECfg 303
                        330       340
                 ....*....|....*....|....*....
gi 28502773  375 --------------------AYLLFYIRS 383
Cdd:cd02659  304 geetqktydsgprafkrttnAYMLFYERK 332
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
84-380 5.42e-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: 189.52  E-value: 5.42e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   84 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTRehsktchepgfcmmctmqnhiiqvfansgnvikPISVLNELKRIGKHFR 163
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET---------------------------------PKELFSQVCRKAPQFK 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  164 FGSQEDAHEFLRYTVDAMQksclpgnkldrqtqatTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISL----EIKTAQ 239
Cdd:cd02667   48 GYQQQDSHELLRYLLDGLR----------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSEC 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  240 TLSKAFEQFVKPEQLDGDNAYKCSKCKKmvtASKRFTVHRSSNVLTISLKRFT---NFNGGKITKDVRYAEHLDLRPFMS 316
Cdd:cd02667  112 SIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQqprSANLRKVSRHVSFPEILDLAPFCD 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  317 QSHGEPQ-----IYALYAVLVHSGfSCHAGHYYCYIKASN----------------------GQWYQMNDSSVSLSDIRT 369
Cdd:cd02667  189 PKCNSSEdkssvLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVSLEE 267
                        330
                 ....*....|.
gi 28502773  370 VLNQQAYLLFY 380
Cdd:cd02667  268 VLKSEAYLLFY 278
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
84-381 5.20e-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: 5.20e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   84 GLHNLGNTCFLNSTLQCLtytaplanymltrehsktchepgfcmmctmqnhiiqvfansgnvikpisvlnelkrigkhfr 163
Cdd:cd02674    1 GLRNLGNTCYMNSILQCL-------------------------------------------------------------- 18
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  164 FGSQEDAHEFLRYTVDamqksclpgnKLDRqtqattFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEI------KT 237
Cdd:cd02674   19 SADQQDAQEFLLFLLD----------GLHS------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdAP 82
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  238 AQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFNGG--KITKDVRYA-EHLDLRPF 314
Cdd:cd02674   83 KVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGStrKLTTPVTFPlNDLDLTPY 162
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28502773  315 -MSQSHGEPQIYALYAVLVHSGfSCHAGHYYCYIK-ASNGQWYQMNDSSVSLSDIRTVLNQQAYLLFYI 381
Cdd:cd02674  163 vDTRSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
84-380 1.64e-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: 1.64e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   84 GLHNLGNTCFLNSTLQCLTYTAPLanymltrehskTCHEPGFCmmctmqnHIIQVFANSGnVIKPISVLNELKRIGKHFR 163
Cdd:cd02663    1 GLENFGNTCYCNSVLQALYFENLL-----------TCLKDLFE-------SISEQKKRTG-VISPKKFITRLKRENELFD 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  164 FGSQEDAHEFLRY-------TVDAMQKSCLPGNKLDRQTQA---TTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISL 233
Cdd:cd02663   62 NYMHQDAHEFLNFllneiaeILDAERKAEKANRKLNNNNNAepqPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSI 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  234 EIKTAQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFT-NFNGGKITK-DVRYAEHLDL 311
Cdd:cd02663  142 DVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKyDEQLNRYIKlFYRVVFPLEL 221
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28502773  312 RPFMSQSHGEP--QIYALYAVLVHSGFSCHAGHYYCYIKaSNGQWYQMNDSSVSLSDIRTVLN--------QQAYLLFY 380
Cdd:cd02663  222 RLFNTTDDAENpdRLYELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFY 299
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
84-389 9.21e-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: 147.18  E-value: 9.21e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   84 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTrehsktchepgfcmmCTMQNHIIQVFANSGNVIKPISVLNELKRIGKHFR 163
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE---------------CNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  164 FGS-------------------QEDAHEFLRYTVDAMQksclpgNKLDRQT--QATTFVHQIFGGYLRSRVKCLNCKAVS 222
Cdd:cd02668   66 FGNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLE------AKLSKSKnpDLKNIVQDLFRGEYSYVTQCSKCGRES 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  223 DTFDPYLDISLEIKTAQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFT----NFNGGK 298
Cdd:cd02668  140 SLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVfdrkTGAKKK 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  299 ITKDVRYAEHLDLRPFMSQSHGEPQIYALYAVLVHSGFSCHAGHYYCYIK-ASNGQWYQMNDSSVSLSDIRTVLNQQAYL 377
Cdd:cd02668  220 LNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDVEEMPGKPLKLGNSED 299
                        330
                 ....*....|..
gi 28502773  378 LFYIRSPDVKNG 389
Cdd:cd02668  300 PAKPRKSEIKKG 311
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
84-380 3.64e-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: 131.07  E-value: 3.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   84 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTchEPGFCMMCTMQNHIIQVFANSGNVIKPISVLNELKRiGKHFR 163
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRL--GDSQSVMKKLQLLQAHLMHTQRRAEAPPDYFLEASR-PPWFT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  164 FGSQEDAHEFLRYTVDamqksclpgnKLDrqtqatTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKTAQTLsk 243
Cdd:cd02664   78 PGSQQDCSEYLRYLLD----------RLH------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDL-- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  244 aFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRF-----TNFNgGKITKDV--------------- 303
Cdd:cd02664  140 -LNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFsydqkTHVR-EKIMDNVsinevlslpvrvesk 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  304 ----RYAEHLDLRPFMSQSHGEPQIYALYAVLVHSGFSCHAGHYYCYI---------------------KASNGQWYQMN 358
Cdd:cd02664  218 ssesPLEKKEEESGDDGELVTRQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNWYLFN 297
                        330       340
                 ....*....|....*....|....*....
gi 28502773  359 DSSVSLSDIRTVLN-------QQAYLLFY 380
Cdd:cd02664  298 DSRVTFSSFESVQNvtsrfpkDTPYILFY 326
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
84-382 4.34e-32

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 135.38  E-value: 4.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   84 GLHNLGNTCFLNSTLQCLTYTAPLAN--YMLTREHSKtchePGFCMMCTMQnhiiQVFANSGNVIKPISVLNELKRIG-- 159
Cdd:COG5077  195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPR----GRDSVALALQ----RLFYNLQTGEEPVDTTELTRSFGwd 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  160 --KHFrfgSQEDAHEFLRYTVDAMQKSClpgnkldRQTQATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKT 237
Cdd:COG5077  267 sdDSF---MQHDIQEFNRVLQDNLEKSM-------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  238 AQTLSKAFEQFVKPEQLDGDNAYKCSKcKKMVTASKRFTVHRSSNVLTISLKRFT-NFNGG---KITKDVRYAEHLDLRP 313
Cdd:COG5077  337 MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEyDFERDmmvKINDRYEFPLEIDLLP 415
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  314 FMS----QSHGEPQIYALYAVLVHSGfSCHAGHYYCYIKAS-NGQWYQMNDSSVSLSDIRTVLNQ--------------- 373
Cdd:COG5077  416 FLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdh 494
                        330
                 ....*....|....*.
gi 28502773  374 -------QAYLLFYIR 382
Cdd:COG5077  495 sgikrfmSAYMLVYLR 510
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
84-382 3.55e-30

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 121.06  E-value: 3.55e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   84 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTRehsktchePGFCMMCTMQ----NHIIQVFANSGNVIKPISVLNELKrIG 159
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILALYLPKLDELLDD--------LSKELKVLKNvirkPEPDLNQEEALKLFTALWSSKEHK-VG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  160 KHFRFGSQEDAHEFLRYTVDAMqksclpgnKLDRQTQATTFVHQIFGGYLRSrvkclnckAVSDTFDpyLDISLEIKTAQ 239
Cdd:COG5533   72 WIPPMGSQEDAHELLGKLLDEL--------KLDLVNSFTIRIFKTTKDKKKT--------STGDWFD--IIIELPDQTWV 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  240 TLSKAFEQFVKP--EQLD-------GDNAYKCSKCKKMVTASKRftvhRSSNVLTISLKRFTNFNGG-KITKDVRYAEHL 309
Cdd:COG5533  134 NNLKTLQEFIDNmeELVDdetgvkaKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANLGGNqKIDTEVDEKFEL 209
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28502773  310 DLRPFMSQSHGEPQIYALYAVLVHSGfSCHAGHYYCYIKaSNGQWYQMNDSSVSLSDIRTVLN---QQAYLLFYIR 382
Cdd:COG5533  210 PVKHDQILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
84-380 8.11e-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: 117.81  E-value: 8.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   84 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCH--EPGFCMMCTM--------------QNHIIQVFANSGNVIK 147
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDvvDPANDLNCQLikladgllsgryskPASLKSENDPYQVGIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  148 PISvlneLKR-IGK-HFRFGS--QEDAHEFLRYTVDAMQKSCLPGNKLDRQTqattfvhqIFGGYLRSRVKCLNCKAVSD 223
Cdd:cd02658   81 PSM----FKAlIGKgHPEFSTmrQQDALEFLLHLIDKLDRESFKNLGLNPND--------LFKFMIEDRLECLSCKKVKY 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  224 TFDPYLDISL--------------EIKTAQTLSKAFEQFVKPEQLDgdnaYKCSKCKKMVTASKRFTVHRSSNVLTISLK 289
Cdd:cd02658  149 TSELSEILSLpvpkdeatekeegeLVYEPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMK 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  290 RFT---NFNGGKITKDVRYAEHLDlrpfmsqshgePQIYALYAVLVHSGFSCHAGHYYCYIK---ASNGQWYQMNDSSVS 363
Cdd:cd02658  225 RFQlleNWVPKKLDVPIDVPEELG-----------PGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVV 293
                        330
                 ....*....|....*..
gi 28502773  364 LSDIRTVLNQQAYLLFY 380
Cdd:cd02658  294 ASQDPPEMKKLGYIYFY 310
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
83-380 1.72e-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: 1.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   83 AGLHNLGNTCFLNSTLQCLTYtAP--LAN--YMLTREHSKTCHEPGFcmmctMQNHiiQVFANSGNVIKPISVLNELKRI 158
Cdd:cd02671   25 VGLNNLGNTCYLNSVLQVLYF-CPgfKHGlkHLVSLISSVEQLQSSF-----LLNP--EKYNDELANQAPRRLLNALREV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  159 GKHFRFGSQEDAHEFLRYTVDAMQKsclpgnkldrqtqattFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKTA 238
Cdd:cd02671   97 NPMYEGYLQHDAQEVLQCILGNIQE----------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQES 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  239 Q-------------------TLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFN---- 295
Cdd:cd02671  161 ElskseesseispdpktemkTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGsefd 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  296 -GGKITKDVRYAehldLRPFMSQSHG-----EPQIYALYAVLVHSGFSCHAGHYYCYIKasngqWYQMNDSSVSLSDIRT 369
Cdd:cd02671  241 cYGGLSKVNTPL----LTPLKLSLEEwstkpKNDVYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKD 311
                        330       340
                 ....*....|....*....|
gi 28502773  370 VLN---------QQAYLLFY 380
Cdd:cd02671  312 FLEalspntsstSTPYLLFY 331
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
84-363 4.07e-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: 4.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   84 GLHNLGNTCFLNSTLQCLtYTAP-----LANYMLTREHSKTCHEPGFCMMctmqNHIIQVFANSGNVIKPISVLNELKRI 158
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCL-RSVPelrdaLKNYNPARRGANQSSDNLTNAL----RDLFDTMDKKQEPVPPIEFLQLLRMA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  159 GKHF----RFG--SQEDAHEFLRYTVDAMQkSCLPGNKLDRQtqattFVHQIFGGYLRSRVKCL-NCKAVSDTFDP---- 227
Cdd:cd02657   76 FPQFaekqNQGgyAQQDAEECWSQLLSVLS-QKLPGAGSKGS-----FIDQLFGIELETKMKCTeSPDEEEVSTESeykl 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  228 --YLDISLEIKTAQT-LSKAF-EQFVKPEQLDGDNAykcskckkmvTASKRFTVHRSSNVLTISLKRF-----TNFNgGK 298
Cdd:cd02657  150 qcHISITTEVNYLQDgLKKGLeEEIEKHSPTLGRDA----------IYTKTSRISRLPKYLTVQFVRFfwkrdIQKK-AK 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28502773  299 ITKDVRYAEHLDLRPFMSQShgepQIYALYAVLVHSGFSCHAGHYYCYIKASN-GQWYQMNDSSVS 363
Cdd:cd02657  219 ILRKVKFPFELDLYELCTPS----GYYELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDDKVS 280
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
84-380 4.90e-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: 90.50  E-value: 4.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   84 GLHNLGNTCFLNSTLQCLtytAPLanymltrehsktchePGFcmmctmqnhiiqvfansgnvikpISVLNELKrigkhfr 163
Cdd:cd02662    1 GLVNLGNTCFMNSVLQAL---ASL---------------PSL-----------------------IEYLEEFL------- 32
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  164 fgSQEDAHEFLRYTVDAMQKSCLpgnkldrqtqattfvhQIFGGYLRSRVKCLNCKAVS-DTFDPYLDISL-----EIKT 237
Cdd:cd02662   33 --EQQDAHELFQVLLETLEQLLK----------------FPFDGLLASRIVCLQCGESSkVRYESFTMLSLpvpnqSSGS 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  238 AQTLSKAFEQFVKPEQLDGdnaYKCSKCKKMVTASKRftvhrssnVLTISLKRFTnFNG-GKITKD---VRYAEHLDlrp 313
Cdd:cd02662   95 GTTLEHCLDDFLSTEIIDD---YKCDRCQTVIVRLPQ--------ILCIHLSRSV-FDGrGTSTKNsckVSFPERLP--- 159
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  314 fmsqshgePQIYALYAVLVHSGfSCHAGHYYCY--------------------IKASN-GQWYQMNDSSVSLSDIRTVLN 372
Cdd:cd02662  160 --------KVLYRLRAVVVHYG-SHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTsHPWWRISDTTVKEVSESEVLE 230

                 ....*....
gi 28502773  373 Q-QAYLLFY 380
Cdd:cd02662  231 QkSAYMLFY 239
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
240-382 1.57e-18

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 91.10  E-value: 1.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  240 TLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFNGG--KITKDVRYA-EHLDLRPFMS 316
Cdd:COG5560  676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFrdKIDDLVEYPiDDLDLSGVEY 755
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28502773  317 QSHGEPQIYALYAVLVHSGFScHAGHYYCYIK-ASNGQWYQMNDSSVSLSDIRTVLNQQAYLLFYIR 382
Cdd:COG5560  756 MVDDPRLIYDLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
84-243 2.32e-14

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 77.62  E-value: 2.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   84 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFCMM-----CTMQNHIIQVFANSGNVIKPISVLNELKRI 158
Cdd:COG5560  267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMhgsvaSAYADLIKQLYDGNLHAFTPSGFKKTIGSF 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  159 GKHFRFGSQEDAHEFLRYTVDAMQK--------------SCLPGNKLDRQTQAT-----------TFVHQIFGGYLRSRV 213
Cdd:COG5560  347 NEEFSGYDQQDSQEFIAFLLDGLHEdlnriikkpytskpDLSPGDDVVVKKKAKecwwehlkrndSIITDLFQGMYKSTL 426
                        170       180       190
                 ....*....|....*....|....*....|
gi 28502773  214 KCLNCKAVSDTFDPYLDISLEIKTAQTLSK 243
Cdd:COG5560  427 TCPGCGSVSITFDPFMDLTLPLPVSMVWKH 456
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
83-362 6.78e-12

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 67.68  E-value: 6.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773     83 AGLHNLGNTCFLNSTLQCLTYTAPLANYMLtrEHSKTCHEPGFCMMC-------TMQNhiiqvfANSGNV-----IKPIS 150
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLAL--SHLATECLKEHCLLCelgflfdMLEK------AKGKNCqasnfLRALS 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    151 VLNELKRIGKHFRFGSQEDAHE-------FLRYTVDAMQKSCLPGNKldRQTQATTFVHQIFGGYLRSRVKCLNCKAVSD 223
Cdd:pfam13423   73 SIPEASALGLLDEDRETNSAISlssliqsFNRFLLDQLSSEENSTPP--NPSPAESPLEQLFGIDAETTIRCSNCGHESV 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    224 TFDPYLDISL------EIKTAQTLSKAFEQFVKpEQLDGDNAYK--CSKCKKMVTASKRFTVHRSSNVLTISLKrFTNFN 295
Cdd:pfam13423  151 RESSTHVLDLiyprkpSSNNKKPPNQTFSSILK-SSLERETTTKawCEKCKRYQPLESRRTVRNLPPVLSLNAA-LTNEE 228
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28502773    296 GGKITKDVRY-AEHLDLRPFM-SQSHGEPQIYALYAVLVHSGFSCHAGHYYCYIKASN--------GQWYQMNDSSV 362
Cdd:pfam13423  229 WRQLWKTPGWlPPEIGLTLSDdLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKVADseledpteSQWYLFNDFLV 305
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
85-380 5.64e-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: 5.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   85 LHNLGNTCFLNSTLQCLTYTaplanymltrehsktchepgfcmmctmqNHIIQVFANSgnvikpisvlnelkrigkhfrf 164
Cdd:cd02673    2 LVNTGNSCYFNSTMQALSSI----------------------------GKINTEFDND---------------------- 31
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  165 gSQEDAHEFLRYTVDAMQKscLPGNKLDRQTQATTFVHQI-----FGGYLRSRVKCLNCK--AVSDTFDPYLDIS---LE 234
Cdd:cd02673   32 -DQQDAHEFLLTLLEAIDD--IMQVNRTNVPPSNIEIKRLnpleaFKYTIESSYVCIGCSfeENVSDVGNFLDVSmidNK 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  235 IKTAQTLSKAFEQFVKPEQldgdnayKCSKCK-KMVTASKRFTvhRSSNVLTISLKRFtnfnggkitkDVRYAEHLDL-- 311
Cdd:cd02673  109 LDIDELLISNFKTWSPIEK-------DCSSCKcESAISSERIM--TFPECLSINLKRY----------KLRIATSDYLkk 169
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28502773  312 -RPFMSQSHGEPQIYALYAVLVHSGFSCHAGHYYCYIKAS--NGQWYQMNDSS---VSLSDIRTVLNQQAYLLFY 380
Cdd:cd02673  170 nEEIMKKYCGTDAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEirpVSKNDVSTNARSSGYLIFY 244
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
84-363 1.48e-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: 1.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   84 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFcmmctmqnHIIQVFA-------NSGN---VIKPISVLN 153
Cdd:cd02669  121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKS--------ELVKRLSelirkiwNPRNfkgHVSPHELLQ 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  154 EL-KRIGKHFRFGSQEDAHEFLRYTVDAMqKSCLPGNKLDRQTQattfVHQIFGGYLR--------------SRVKCLNC 218
Cdd:cd02669  193 AVsKVSKKKFSITEQSDPVEFLSWLLNTL-HKDLGGSKKPNSSI----IHDCFQGKVQietqkikphaeeegSKDKFFKD 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  219 KAVSDTFD-PYLDISLEIKTA-----QTLSKAFEQFVKPEQLDGdnaYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFT 292
Cdd:cd02669  268 SRVKKTSVsPFLLLTLDLPPPplfkdGNEENIIPQVPLKQLLKK---YDGKTETELKDSLKRYLISRLPKYLIFHIKRFS 344
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28502773  293 --NFNGGKITKDVRY-AEHLDLRPFMSQ---SHGEPQIYALYAVLVHSGFSCHAGHYYCYI-KASNGQWYQMNDSSVS 363
Cdd:cd02669  345 knNFFKEKNPTIVNFpIKNLDLSDYVHFdkpSLNLSTKYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQDLNVK 422
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
83-381 1.79e-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: 1.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   83 AGLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTchepgfcmmcTMQNHIIQVFANSGNVIKPISVL------NELK 156
Cdd:cd02666    2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKA----------ELASDYPTERRIGGREVSRSELQrsnqfvYELR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  157 RIGKH-------------------FRfgsQEDAHE------FLRYTVDAMQKSCLPGNKLDRQTQATTFVHQIF-GGYLR 210
Cdd:cd02666   72 SLFNDlihsntrsvtpskelaylaLR---QQDVTEcidnvlFQLEVALEPISNAFAGPDTEDDKEQSDLIKRLFsGKTKQ 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  211 SRVKCLNCKAVSDTFDPYLDISLEIKT------------AQTLSKAFEQFVKPEQL-----DGDNAYKCSKCK-KMVTAS 272
Cdd:cd02666  149 QLVPESMGNQPSVRTKTERFLSLLVDVgkkgreivvllePKDLYDALDRYFDYDSLtklpqRSQVQAQLAQPLqRELISM 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  273 KRFTVHRSSN-VLTISLKRFTNFNGGKITKDVRYAEHLDLRPfmSQSHGEPQI-YALYAVLVHSGfSCHAGHYYCYIK-A 349
Cdd:cd02666  229 DRYELPSSIDdIDELIREAIQSESSLVRQAQNELAELKHEIE--KQFDDLKSYgYRLHAVFIHRG-EASSGHYWVYIKdF 305
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 28502773  350 SNGQWYQMNDSSVSLSDIRTVLNQ------QAYLLFYI 381
Cdd:cd02666  306 EENVWRKYNDETVTVVPASEVFLFtlgntaTPYFLVYV 343
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
813-909 6.97e-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: 6.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    813 EDRNRGSDRPHFSSTPKDRERYRHyRDHSdRSRSRYGHSYQDSRRSTSRER-YYRDRDLERHWDRFSHHRREHHYFQRRH 891
Cdd:TIGR01642    5 PDREREKSRGRDRDRSSERPRRRS-RDRS-RFRDRHRRSRERSYREDSRPRdRRRYDSRSPRSLRYSSVRRSRDRPRRRS 82
                           90
                   ....*....|....*...
gi 28502773    892 RDERDWNRDRRFGSDSYR 909
Cdd:TIGR01642   83 RSVRSIEQHRRRLRDRSP 100
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
814-906 1.97e-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: 1.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    814 DRNRGSDRPhfSSTPKDRERYRHYRDHSDRSRSRyghsyqDSRRSTSRER-YYRDRDLERHWDRFSHHRREHHYFQRRHR 892
Cdd:TIGR01622    4 DRERERLRD--SSSAGDRDRRRDKGRERSRDRSR------DRERSRSRRRdRHRDRDYYRGRERRSRSRRPNRRYRPREK 75
                           90
                   ....*....|....
gi 28502773    893 DERDWNRDRRFGSD 906
Cdd:TIGR01622   76 RRRRGDSYRRRRDD 89
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
283-381 2.33e-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: 2.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773  283 VLTISLKRFtNFNGGKITKdvryaEHLDLR-PFMSQSHGepqiYALYAVLVHSGfSCHAGHYYCYI-KASNGQWYQMNDS 360
Cdd:cd02665  131 VLTFELSRF-EFNQGRPEK-----IHDKLEfPQIIQQVP----YELHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYNDI 199
                         90       100
                 ....*....|....*....|....*....
gi 28502773  361 SVSLSDIRTV--------LNQQAYLLFYI 381
Cdd:cd02665  200 SVTESSWEEVerdsfgggRNPSAYCLMYI 228
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
829-918 5.21e-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: 50.30  E-value: 5.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    829 KDRERYRHYRDHSDRSRSRyghsyqdsRRSTSREryyRDRDLERHWDRFSHHRREhhyfqrRHRDeRDWNRDRRFGSDSY 908
Cdd:TIGR01622    3 RDRERERLRDSSSAGDRDR--------RRDKGRE---RSRDRSRDRERSRSRRRD------RHRD-RDYYRGRERRSRSR 64
                           90
                   ....*....|
gi 28502773    909 RPSGYHNRNG 918
Cdd:TIGR01622   65 RPNRRYRPRE 74
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
852-972 1.00e-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: 49.51  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    852 YQDSRRSTSRERYyRDRDLERHWDRfshhRREHHYFQRRHRderdWNRDRRFGSDSyRPsgyHNRNGYSNHSHRGMEEAH 931
Cdd:TIGR01642    4 EPDREREKSRGRD-RDRSSERPRRR----SRDRSRFRDRHR----RSRERSYREDS-RP---RDRRRYDSRSPRSLRYSS 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 28502773    932 GRATHTVNGSKGRPSSPHSVSplpRHHKRKRSPSVDARESS 972
Cdd:TIGR01642   71 VRRSRDRPRRRSRSVRSIEQH---RRRLRDRSPSNQWRKDD 108
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
829-926 2.81e-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: 47.97  E-value: 2.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    829 KDRERYRHYRDHSDRSRSRYGHSYQDSRRSTSRERYYRDRDLERHWDRFSHHRREHHYFQRRHRDERDWNRDRrfgSDSY 908
Cdd:TIGR01642    1 RDEEPDREREKSRGRDRDRSSERPRRRSRDRSRFRDRHRRSRERSYREDSRPRDRRRYDSRSPRSLRYSSVRR---SRDR 77
                           90
                   ....*....|....*...
gi 28502773    909 RPSGYHNRNGYSNHSHRG 926
Cdd:TIGR01642   78 PRRRSRSVRSIEQHRRRL 95
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
829-922 3.34e-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: 3.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    829 KDRERYRHYRDHSDRSRSRYGHSYQDSRRSTSRERYyRDRDLERHWDRFSHHRREhhyfqRRHRDERDWNRDRRFGSDSY 908
Cdd:TIGR01622    5 RERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERS-RSRRRDRHRDRDYYRGRE-----RRSRSRRPNRRYRPREKRRR 78
                           90
                   ....*....|....
gi 28502773    909 RPSGYHNRNGYSNH 922
Cdd:TIGR01622   79 RGDSYRRRRDDRRS 92
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
813-902 1.39e-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: 42.07  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    813 EDRNRGSDRPHFSSTPKDRERYRHYRdhSDRSRSRYGHSyqdSRRSTSRERYYRDRDLERHWDRFSHHRRehhyfQRRHR 892
Cdd:pfam12871   20 EDEEASDESERASLSRKRRSRSRRRS--STRDRSRSRSR---SRSRDRRSRGTRDRRRDRDRDRYRSLRS-----RSRDR 89
                           90
                   ....*....|
gi 28502773    893 DeRDWNRDRR 902
Cdd:pfam12871   90 S-RDRDRDRR 98
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
792-902 1.75e-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: 1.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    792 SKEAKPSHSDKFGSGDGWRSGEDRNRGSDRPHFSSTPKDRERYRH-----YRDHSDRSRSRYGHSYQDSRRSTSR--ERY 864
Cdd:TIGR01622    4 DRERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRRRDRHrdrdyYRGRERRSRSRRPNRRYRPREKRRRrgDSY 83
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 28502773    865 YRDRDLERhwdrfshHRREHHYFQRRHRDE-RDWNRDRR 902
Cdd:TIGR01622   84 RRRRDDRR-------SRREKPRARDGTPEPlTEDERDRR 115
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
788-873 4.22e-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: 40.53  E-value: 4.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    788 SEGESKEAKPSHSDKFGSGDGWRSGEDRNRGSDRPHFSSTPKDRERYRHYRDHSDRSRSRYgHSYQDSRRSTSRERyYRD 867
Cdd:pfam12871   15 EEDEEEDEEASDESERASLSRKRRSRSRRRSSTRDRSRSRSRSRSRDRRSRGTRDRRRDRD-RDRYRSLRSRSRDR-SRD 92

                   ....*.
gi 28502773    868 RDLERH 873
Cdd:pfam12871   93 RDRDRR 98
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
792-913 1.49e-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: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    792 SKEAKPSHSDKFGSGDGWRSGEDRNRGSDRPHFSSTPKDRERYRHYRDHSDRSRSRYGHSYQDSRRSTSRERyYRDRDLe 871
Cdd:TIGR01642    8 EREKSRGRDRDRSSERPRRRSRDRSRFRDRHRRSRERSYREDSRPRDRRRYDSRSPRSLRYSSVRRSRDRPR-RRSRSV- 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 28502773    872 rhwDRFSHHRREHHYFQRRHRDERDWNrdRRFGSDsYRPSGY 913
Cdd:TIGR01642   86 ---RSIEQHRRRLRDRSPSNQWRKDDK--KRSLWD-IKPPGY 121
PRK12678 PRK12678
transcription termination factor Rho; Provisional
805-910 1.79e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.20  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   805 SGDGWRSGEDRNRGSDRPHfsstpKDRERYRHYRDHSDRSRSRYGHSYQDSRRSTSRERYYRDRDLERHWDRfshHRREh 884
Cdd:PRK12678  193 REERGRDGDDRDRRDRREQ-----GDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRG---GRRG- 263
                          90       100
                  ....*....|....*....|....*.
gi 28502773   885 hyfqRRHRDERDWNRDRRFGSDSYRP 910
Cdd:PRK12678  264 ----RRFRDRDRRGRRGGDGGNEREP 285
PRK12678 PRK12678
transcription termination factor Rho; Provisional
788-906 3.01e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.43  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773   788 SEGESKEAKPSHSDKFGSGDGWRSGEDRNRGSDRphfsstpKDRERYRHYRDHSDRSRSRYGHSYQDSRRSTSRERYYRD 867
Cdd:PRK12678  167 EERDERRRRGDREDRQAEAERGERGRREERGRDG-------DDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDAR 239
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 28502773   868 RDLERHWDRFSHHRREHHYFQRRHRDERDWNRDRRFGSD 906
Cdd:PRK12678  240 GDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGD 278
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
865-974 5.13e-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: 40.67  E-value: 5.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28502773    865 YRDRDLERHWDRFSHHRREHHYFQRRHRDeRDWNRDRRFGSDSYRPSGyHNRNGYSNHSHRGMEEAHGRATHTVNGSKGR 944
Cdd:TIGR01622    2 YRDRERERLRDSSSAGDRDRRRDKGRERS-RDRSRDRERSRSRRRDRH-RDRDYYRGRERRSRSRRPNRRYRPREKRRRR 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 28502773    945 PSSphsvSPLPRHHKRKRSPSVDARESSDE 974
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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