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Conserved domains on  [gi|1207190300|ref|XP_021328186|]
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ubiquitin carboxyl-terminal hydrolase 42 isoform X2 [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 ...
33-332 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: 540.71  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   33 GAGLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFCMMCTMQNHIIQVFANSGNVIKPISVLNELKRIGKH 112
Cdd:cd02661      1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  113 FRFGSQEDAHEFLRYTVDAMQKSCLPGNK----LDRQTQATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKT 188
Cdd:cd02661     81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKklkaVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  189 AQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFNGGKITKDVRYAEHLDLRPFMSQ 268
Cdd:cd02661    161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190300  269 SHGEPQIYALYAVLVHSGFSCHAGHYYCYIKASNGQWYQMNDSSVSLSDIRTVLNQQAYLLFYI 332
Cdd:cd02661    241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
U2AF_lg super family cl36941
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
764-860 8.63e-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: 8.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  764 EDRNRGSDRPHFSSTPKDRERYRHyRDHSdRSRSRYGHSYQDSRRSTSRER-YYRDRDLERHWDRFSHHRREHHYFQRRH 842
Cdd:TIGR01642    5 PDREREKSRGRDRDRSSERPRRRS-RDRS-RFRDRHRRSRERSYREDSRPRdRRRYDSRSPRSLRYSSVRRSRDRPRRRS 82
                           90
                   ....*....|....*...
gi 1207190300  843 RDERDWNRDRRFGSDSYR 860
Cdd:TIGR01642   83 RSVRSIEQHRRRLRDRSP 100
SF-CC1 super family cl36939
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
816-925 6.76e-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: 6.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  816 YRDRDLERHWDRFSHHRREHHYFQRRHRDeRDWNRDRRFGSDSYRPSGyHNRNGYSNHSHRGMEEAHGRATHTVNGSKGR 895
Cdd:TIGR01622    2 YRDRERERLRDSSSAGDRDRRRDKGRERS-RDRSRDRERSRSRRRDRH-RDRDYYRGRERRSRSRRPNRRYRPREKRRRR 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 1207190300  896 PSSphsvSPLPRHHKRKRSPSVDARESSDE 925
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 ...
33-332 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: 540.71  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   33 GAGLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFCMMCTMQNHIIQVFANSGNVIKPISVLNELKRIGKH 112
Cdd:cd02661      1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  113 FRFGSQEDAHEFLRYTVDAMQKSCLPGNK----LDRQTQATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKT 188
Cdd:cd02661     81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKklkaVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  189 AQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFNGGKITKDVRYAEHLDLRPFMSQ 268
Cdd:cd02661    161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190300  269 SHGEPQIYALYAVLVHSGFSCHAGHYYCYIKASNGQWYQMNDSSVSLSDIRTVLNQQAYLLFYI 332
Cdd:cd02661    241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
34-331 8.16e-78

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 258.14  E-value: 8.16e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   34 AGLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFC--MMCTMQNHIIQVFANS-GNVIKPISVLNELKRIG 110
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNSkSSSVSPKMFKKSLGKLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  111 KHFRFGSQEDAHEFLRYTVDAMQkSCLPGNKLDRQTQAttfVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKTAQ 190
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLH-EDLNGNHSTENESL---ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  191 TLSK------AFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTnFNGG---KITKDVRYAEHLD 261
Cdd:pfam00443  157 AELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFS-YNRStweKLNTEVEFPLELD 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190300  262 LRPFMSQ----SHGEPQIYALYAVLVHSGfSCHAGHYYCYIKA-SNGQWYQMNDSSVSLSDIRT-VLNQQAYLLFY 331
Cdd:pfam00443  236 LSRYLAEelkpKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
35-333 1.23e-31

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 134.23  E-value: 1.23e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   35 GLHNLGNTCFLNSTLQCLTYTAPLAN--YMLTREHSKtchePGFCMMCTMQnhiiQVFANSGNVIKPISVLNELKRIG-- 110
Cdd:COG5077    195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPR----GRDSVALALQ----RLFYNLQTGEEPVDTTELTRSFGwd 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  111 --KHFrfgSQEDAHEFLRYTVDAMQKSClpgnkldRQTQATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKT 188
Cdd:COG5077    267 sdDSF---MQHDIQEFNRVLQDNLEKSM-------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  189 AQTLSKAFEQFVKPEQLDGDNAYKCSKcKKMVTASKRFTVHRSSNVLTISLKRFT-NFNGG---KITKDVRYAEHLDLRP 264
Cdd:COG5077    337 MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEyDFERDmmvKINDRYEFPLEIDLLP 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  265 FMS----QSHGEPQIYALYAVLVHSGfSCHAGHYYCYIKAS-NGQWYQMNDSSVSLSDIRTVLNQ--------------- 324
Cdd:COG5077    416 FLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdh 494
                          330
                   ....*....|....*.
gi 1207190300  325 -------QAYLLFYIR 333
Cdd:COG5077    495 sgikrfmSAYMLVYLR 510
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
764-860 8.63e-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: 8.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  764 EDRNRGSDRPHFSSTPKDRERYRHyRDHSdRSRSRYGHSYQDSRRSTSRER-YYRDRDLERHWDRFSHHRREHHYFQRRH 842
Cdd:TIGR01642    5 PDREREKSRGRDRDRSSERPRRRS-RDRS-RFRDRHRRSRERSYREDSRPRdRRRYDSRSPRSLRYSSVRRSRDRPRRRS 82
                           90
                   ....*....|....*...
gi 1207190300  843 RDERDWNRDRRFGSDSYR 860
Cdd:TIGR01642   83 RSVRSIEQHRRRLRDRSP 100
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
764-853 4.76e-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: 4.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  764 EDRNRGSDRPHFSSTPKDRERYRHYRdhSDRSRSRYGHSyqdSRRSTSRERYYRDRDLERHWDRFSHHRRehhyfQRRHR 843
Cdd:pfam12871   20 EDEEASDESERASLSRKRRSRSRRRS--STRDRSRSRSR---SRSRDRRSRGTRDRRRDRDRDRYRSLRS-----RSRDR 89
                           90
                   ....*....|
gi 1207190300  844 DeRDWNRDRR 853
Cdd:pfam12871   90 S-RDRDRDRR 98
PRK12678 PRK12678
transcription termination factor Rho; Provisional
756-861 2.02e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.20  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  756 SGDGWRSGEDRNRGSDRPHfsstpKDRERYRHYRDHSDRSRSRYGHSYQDSRRSTSRERYYRDRDLERHWDRfshHRREh 835
Cdd:PRK12678   193 REERGRDGDDRDRRDRREQ-----GDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRG---GRRG- 263
                           90       100
                   ....*....|....*....|....*.
gi 1207190300  836 hyfqRRHRDERDWNRDRRFGSDSYRP 861
Cdd:PRK12678   264 ----RRFRDRDRRGRRGGDGGNEREP 285
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
816-925 6.76e-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: 6.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  816 YRDRDLERHWDRFSHHRREHHYFQRRHRDeRDWNRDRRFGSDSYRPSGyHNRNGYSNHSHRGMEEAHGRATHTVNGSKGR 895
Cdd:TIGR01622    2 YRDRERERLRDSSSAGDRDRRRDKGRERS-RDRSRDRERSRSRRRDRH-RDRDYYRGRERRSRSRRPNRRYRPREKRRRR 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 1207190300  896 PSSphsvSPLPRHHKRKRSPSVDARESSDE 925
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 ...
33-332 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: 540.71  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   33 GAGLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFCMMCTMQNHIIQVFANSGNVIKPISVLNELKRIGKH 112
Cdd:cd02661      1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  113 FRFGSQEDAHEFLRYTVDAMQKSCLPGNK----LDRQTQATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKT 188
Cdd:cd02661     81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKklkaVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  189 AQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFNGGKITKDVRYAEHLDLRPFMSQ 268
Cdd:cd02661    161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207190300  269 SHGEPQIYALYAVLVHSGFSCHAGHYYCYIKASNGQWYQMNDSSVSLSDIRTVLNQQAYLLFYI 332
Cdd:cd02661    241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
34-331 8.16e-78

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 258.14  E-value: 8.16e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   34 AGLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFC--MMCTMQNHIIQVFANS-GNVIKPISVLNELKRIG 110
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNSkSSSVSPKMFKKSLGKLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  111 KHFRFGSQEDAHEFLRYTVDAMQkSCLPGNKLDRQTQAttfVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKTAQ 190
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLH-EDLNGNHSTENESL---ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  191 TLSK------AFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTnFNGG---KITKDVRYAEHLD 261
Cdd:pfam00443  157 AELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFS-YNRStweKLNTEVEFPLELD 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190300  262 LRPFMSQ----SHGEPQIYALYAVLVHSGfSCHAGHYYCYIKA-SNGQWYQMNDSSVSLSDIRT-VLNQQAYLLFY 331
Cdd:pfam00443  236 LSRYLAEelkpKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
35-332 7.29e-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: 239.58  E-value: 7.29e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   35 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCH--EPGFCMMCTMQNhIIQVFANSGNVIK--PISVLNELKRIG 110
Cdd:cd02660      2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLscSPNSCLSCAMDE-IFQEFYYSGDRSPygPINLLYLSWKHS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  111 KHFRFGSQEDAHEFLRYTVDAMQKSCLPGNKLDRQT-QATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIK-- 187
Cdd:cd02660     81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDEsHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPnk 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  188 -------------TAQTLSKAFEQFVKPEQLdGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFNGG---KIT 251
Cdd:cd02660    161 stpswalgesgvsGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKID 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  252 KDVRYAEHLDLRPFMSQSHGEPQ---------IYALYAVLVHSGfSCHAGHYYCYIKASNGQWYQMNDSSVSLSDIRTVL 322
Cdd:cd02660    240 TYVQFPLELNMTPYTSSSIGDTQdsnsldpdyTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVL 318
                          330
                   ....*....|
gi 1207190300  323 NQQAYLLFYI 332
Cdd:cd02660    319 KSQAYLLFYH 328
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
35-332 2.50e-67

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: 226.98  E-value: 2.50e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   35 GLHNLGNTCFLNSTLQCLtytaplanymltrehsktchepgfcmmctmqnhiiqvfansgnvikpisvlnelkrigkhfr 114
Cdd:cd02257      1 GLNNLGNTCYLNSVLQAL-------------------------------------------------------------- 18
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  115 FGSQEDAHEFLRYTVDAMQKSCLPGNKLDR-QTQATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEI----KTA 189
Cdd:cd02257     19 FSEQQDAHEFLLFLLDKLHEELKKSSKRTSdSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  190 QTLSKAFEQFVKPEQLDGDNAYKCSKCKKmVTASKRFTVHRSSNVLTISLKRFT---NFNGGKITKDVRYAEHLDLRPFM 266
Cdd:cd02257     99 VSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYL 177
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190300  267 SQ------SHGEPQIYALYAVLVHSGFSCHAGHYYCYIK-ASNGQWYQMNDSSVSLSDIRTVL-----NQQAYLLFYI 332
Cdd:cd02257    178 SEgekdsdSDNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
35-334 1.36e-56

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: 199.41  E-value: 1.36e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   35 GLHNLGNTCFLNSTLQCLTYTAPLANYML----TREHSKTCHEPgfcmmCTMQnhiiQVFANSGNVIKPISVLNELkriG 110
Cdd:cd02659      4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYsippTEDDDDNKSVP-----LALQ----RLFLFLQLSESPVKTTELT---D 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  111 KHFRFGS-------QEDAHEFLRYTVDAMQKsCLPGNKLDRqtqattFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDIS 183
Cdd:cd02659     72 KTRSFGWdslntfeQHDVQEFFRVLFDKLEE-KLKGTGQEG------LIKNLFGGKLVNYIICKECPHESEREEYFLDLQ 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  184 LEIKTAQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFT-NFNGG---KITKDVRYAEH 259
Cdd:cd02659    145 VAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfDFETMmriKINDRFEFPLE 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  260 LDLRPFMSQS-----------HGEPQIYALYAVLVHSGfSCHAGHYYCYIK-ASNGQWYQMNDSSVSLSDIRTVLNQQ-- 325
Cdd:cd02659    225 LDMEPYTEKGlakkegdsekkDSESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECfg 303
                          330       340
                   ....*....|....*....|....*....
gi 1207190300  326 --------------------AYLLFYIRS 334
Cdd:cd02659    304 geetqktydsgprafkrttnAYMLFYERK 332
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
35-331 8.23e-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: 8.23e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   35 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTRehsktchepgfcmmctmqnhiiqvfansgnvikPISVLNELKRIGKHFR 114
Cdd:cd02667      1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET---------------------------------PKELFSQVCRKAPQFK 47
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  115 FGSQEDAHEFLRYTVDAMQksclpgnkldrqtqatTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISL----EIKTAQ 190
Cdd:cd02667     48 GYQQQDSHELLRYLLDGLR----------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSEC 111
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  191 TLSKAFEQFVKPEQLDGDNAYKCSKCKKmvtASKRFTVHRSSNVLTISLKRFT---NFNGGKITKDVRYAEHLDLRPFMS 267
Cdd:cd02667    112 SIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQqprSANLRKVSRHVSFPEILDLAPFCD 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  268 QSHGEPQ-----IYALYAVLVHSGfSCHAGHYYCYIKASN----------------------GQWYQMNDSSVSLSDIRT 320
Cdd:cd02667    189 PKCNSSEdkssvLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVSLEE 267
                          330
                   ....*....|.
gi 1207190300  321 VLNQQAYLLFY 331
Cdd:cd02667    268 VLKSEAYLLFY 278
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
35-332 1.44e-52

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: 184.03  E-value: 1.44e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   35 GLHNLGNTCFLNSTLQCLtytaplanymltrehsktchepgfcmmctmqnhiiqvfansgnvikpisvlnelkrigkhfr 114
Cdd:cd02674      1 GLRNLGNTCYMNSILQCL-------------------------------------------------------------- 18
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  115 FGSQEDAHEFLRYTVDamqksclpgnKLDRqtqattFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEI------KT 188
Cdd:cd02674     19 SADQQDAQEFLLFLLD----------GLHS------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdAP 82
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  189 AQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFNGG--KITKDVRYA-EHLDLRPF 265
Cdd:cd02674     83 KVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGStrKLTTPVTFPlNDLDLTPY 162
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190300  266 -MSQSHGEPQIYALYAVLVHSGfSCHAGHYYCYIK-ASNGQWYQMNDSSVSLSDIRTVLNQQAYLLFYI 332
Cdd:cd02674    163 vDTRSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
35-331 4.27e-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: 159.40  E-value: 4.27e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   35 GLHNLGNTCFLNSTLQCLTYTAPLanymltrehskTCHEPGFCmmctmqnHIIQVFANSGnVIKPISVLNELKRIGKHFR 114
Cdd:cd02663      1 GLENFGNTCYCNSVLQALYFENLL-----------TCLKDLFE-------SISEQKKRTG-VISPKKFITRLKRENELFD 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  115 FGSQEDAHEFLRY-------TVDAMQKSCLPGNKLDRQTQA---TTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISL 184
Cdd:cd02663     62 NYMHQDAHEFLNFllneiaeILDAERKAEKANRKLNNNNNAepqPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSI 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  185 EIKTAQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFT-NFNGGKITK-DVRYAEHLDL 262
Cdd:cd02663    142 DVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKyDEQLNRYIKlFYRVVFPLEL 221
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207190300  263 RPFMSQSHGEP--QIYALYAVLVHSGFSCHAGHYYCYIKaSNGQWYQMNDSSVSLSDIRTVLN--------QQAYLLFY 331
Cdd:cd02663    222 RLFNTTDDAENpdRLYELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDETVEKIDENAVEEffgdspnqATAYVLFY 299
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
35-340 1.46e-38

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: 146.80  E-value: 1.46e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   35 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTrehsktchepgfcmmCTMQNHIIQVFANSGNVIKPISVLNELKRIGKHFR 114
Cdd:cd02668      1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE---------------CNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQ 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  115 FGS-------------------QEDAHEFLRYTVDAMQksclpgNKLDRQT--QATTFVHQIFGGYLRSRVKCLNCKAVS 173
Cdd:cd02668     66 FGNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLE------AKLSKSKnpDLKNIVQDLFRGEYSYVTQCSKCGRES 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  174 DTFDPYLDISLEIKTAQTLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFT----NFNGGK 249
Cdd:cd02668    140 SLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVfdrkTGAKKK 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  250 ITKDVRYAEHLDLRPFMSQSHGEPQIYALYAVLVHSGFSCHAGHYYCYIK-ASNGQWYQMNDSSVSLSDIRTVLNQQAYL 328
Cdd:cd02668    220 LNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDVEEMPGKPLKLGNSED 299
                          330
                   ....*....|..
gi 1207190300  329 LFYIRSPDVKNG 340
Cdd:cd02668    300 PAKPRKSEIKKG 311
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
35-331 5.25e-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: 130.69  E-value: 5.25e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   35 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTchEPGFCMMCTMQNHIIQVFANSGNVIKPISVLNELKRiGKHFR 114
Cdd:cd02664      1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRL--GDSQSVMKKLQLLQAHLMHTQRRAEAPPDYFLEASR-PPWFT 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  115 FGSQEDAHEFLRYTVDamqksclpgnKLDrqtqatTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKTAQTLsk 194
Cdd:cd02664     78 PGSQQDCSEYLRYLLD----------RLH------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDL-- 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  195 aFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRF-----TNFNgGKITKDV--------------- 254
Cdd:cd02664    140 -LNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFsydqkTHVR-EKIMDNVsinevlslpvrvesk 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  255 ----RYAEHLDLRPFMSQSHGEPQIYALYAVLVHSGFSCHAGHYYCYI---------------------KASNGQWYQMN 309
Cdd:cd02664    218 ssesPLEKKEEESGDDGELVTRQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNWYLFN 297
                          330       340
                   ....*....|....*....|....*....
gi 1207190300  310 DSSVSLSDIRTVLN-------QQAYLLFY 331
Cdd:cd02664    298 DSRVTFSSFESVQNvtsrfpkDTPYILFY 326
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
35-333 1.23e-31

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 134.23  E-value: 1.23e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   35 GLHNLGNTCFLNSTLQCLTYTAPLAN--YMLTREHSKtchePGFCMMCTMQnhiiQVFANSGNVIKPISVLNELKRIG-- 110
Cdd:COG5077    195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPR----GRDSVALALQ----RLFYNLQTGEEPVDTTELTRSFGwd 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  111 --KHFrfgSQEDAHEFLRYTVDAMQKSClpgnkldRQTQATTFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKT 188
Cdd:COG5077    267 sdDSF---MQHDIQEFNRVLQDNLEKSM-------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  189 AQTLSKAFEQFVKPEQLDGDNAYKCSKcKKMVTASKRFTVHRSSNVLTISLKRFT-NFNGG---KITKDVRYAEHLDLRP 264
Cdd:COG5077    337 MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEyDFERDmmvKINDRYEFPLEIDLLP 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  265 FMS----QSHGEPQIYALYAVLVHSGfSCHAGHYYCYIKAS-NGQWYQMNDSSVSLSDIRTVLNQ--------------- 324
Cdd:COG5077    416 FLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdh 494
                          330
                   ....*....|....*.
gi 1207190300  325 -------QAYLLFYIR 333
Cdd:COG5077    495 sgikrfmSAYMLVYLR 510
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
35-333 3.87e-30

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 121.06  E-value: 3.87e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   35 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTRehsktchePGFCMMCTMQ----NHIIQVFANSGNVIKPISVLNELKrIG 110
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILALYLPKLDELLDD--------LSKELKVLKNvirkPEPDLNQEEALKLFTALWSSKEHK-VG 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  111 KHFRFGSQEDAHEFLRYTVDAMqksclpgnKLDRQTQATTFVHQIFGGYLRSrvkclnckAVSDTFDpyLDISLEIKTAQ 190
Cdd:COG5533     72 WIPPMGSQEDAHELLGKLLDEL--------KLDLVNSFTIRIFKTTKDKKKT--------STGDWFD--IIIELPDQTWV 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  191 TLSKAFEQFVKP--EQLD-------GDNAYKCSKCKKMVTASKRftvhRSSNVLTISLKRFTNFNGG-KITKDVRYAEHL 260
Cdd:COG5533    134 NNLKTLQEFIDNmeELVDdetgvkaKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANLGGNqKIDTEVDEKFEL 209
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190300  261 DLRPFMSQSHGEPQIYALYAVLVHSGfSCHAGHYYCYIKaSNGQWYQMNDSSVSLSDIRTVLN---QQAYLLFYIR 333
Cdd:COG5533    210 PVKHDQILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
35-331 8.78e-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: 8.78e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   35 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCH--EPGFCMMCTM--------------QNHIIQVFANSGNVIK 98
Cdd:cd02658      1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDvvDPANDLNCQLikladgllsgryskPASLKSENDPYQVGIK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   99 PISvlneLKR-IGK-HFRFGS--QEDAHEFLRYTVDAMQKSCLPGNKLDRQTqattfvhqIFGGYLRSRVKCLNCKAVSD 174
Cdd:cd02658     81 PSM----FKAlIGKgHPEFSTmrQQDALEFLLHLIDKLDRESFKNLGLNPND--------LFKFMIEDRLECLSCKKVKY 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  175 TFDPYLDISL--------------EIKTAQTLSKAFEQFVKPEQLDgdnaYKCSKCKKMVTASKRFTVHRSSNVLTISLK 240
Cdd:cd02658    149 TSELSEILSLpvpkdeatekeegeLVYEPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMK 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  241 RFT---NFNGGKITKDVRYAEHLDlrpfmsqshgePQIYALYAVLVHSGFSCHAGHYYCYIK---ASNGQWYQMNDSSVS 314
Cdd:cd02658    225 RFQlleNWVPKKLDVPIDVPEELG-----------PGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVV 293
                          330
                   ....*....|....*..
gi 1207190300  315 LSDIRTVLNQQAYLLFY 331
Cdd:cd02658    294 ASQDPPEMKKLGYIYFY 310
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
34-331 1.75e-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: 1.75e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   34 AGLHNLGNTCFLNSTLQCLTYtAP--LAN--YMLTREHSKTCHEPGFcmmctMQNHiiQVFANSGNVIKPISVLNELKRI 109
Cdd:cd02671     25 VGLNNLGNTCYLNSVLQVLYF-CPgfKHGlkHLVSLISSVEQLQSSF-----LLNP--EKYNDELANQAPRRLLNALREV 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  110 GKHFRFGSQEDAHEFLRYTVDAMQKsclpgnkldrqtqattFVHQIFGGYLRSRVKCLNCKAVSDTFDPYLDISLEIKTA 189
Cdd:cd02671     97 NPMYEGYLQHDAQEVLQCILGNIQE----------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQES 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  190 Q-------------------TLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFN---- 246
Cdd:cd02671    161 ElskseesseispdpktemkTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGsefd 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  247 -GGKITKDVRYAehldLRPFMSQSHG-----EPQIYALYAVLVHSGFSCHAGHYYCYIKasngqWYQMNDSSVSLSDIRT 320
Cdd:cd02671    241 cYGGLSKVNTPL----LTPLKLSLEEwstkpKNDVYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKD 311
                          330       340
                   ....*....|....*....|
gi 1207190300  321 VLN---------QQAYLLFY 331
Cdd:cd02671    312 FLEalspntsstSTPYLLFY 331
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
35-314 5.51e-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: 100.87  E-value: 5.51e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   35 GLHNLGNTCFLNSTLQCLtYTAP-----LANYMLTREHSKTCHEPGFCMMctmqNHIIQVFANSGNVIKPISVLNELKRI 109
Cdd:cd02657      1 GLTNLGNTCYLNSTLQCL-RSVPelrdaLKNYNPARRGANQSSDNLTNAL----RDLFDTMDKKQEPVPPIEFLQLLRMA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  110 GKHF----RFG--SQEDAHEFLRYTVDAMQkSCLPGNKLDRQtqattFVHQIFGGYLRSRVKCL-NCKAVSDTFDP---- 178
Cdd:cd02657     76 FPQFaekqNQGgyAQQDAEECWSQLLSVLS-QKLPGAGSKGS-----FIDQLFGIELETKMKCTeSPDEEEVSTESeykl 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  179 --YLDISLEIKTAQT-LSKAF-EQFVKPEQLDGDNAykcskckkmvTASKRFTVHRSSNVLTISLKRF-----TNFNgGK 249
Cdd:cd02657    150 qcHISITTEVNYLQDgLKKGLeEEIEKHSPTLGRDA----------IYTKTSRISRLPKYLTVQFVRFfwkrdIQKK-AK 218
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207190300  250 ITKDVRYAEHLDLRPFMSQShgepQIYALYAVLVHSGFSCHAGHYYCYIKASN-GQWYQMNDSSVS 314
Cdd:cd02657    219 ILRKVKFPFELDLYELCTPS----GYYELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDDKVS 280
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
35-331 7.85e-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: 89.73  E-value: 7.85e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   35 GLHNLGNTCFLNSTLQCLtytAPLanymltrehsktchePGFcmmctmqnhiiqvfansgnvikpISVLNELKrigkhfr 114
Cdd:cd02662      1 GLVNLGNTCFMNSVLQAL---ASL---------------PSL-----------------------IEYLEEFL------- 32
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  115 fgSQEDAHEFLRYTVDAMQKSCLpgnkldrqtqattfvhQIFGGYLRSRVKCLNCKAVS-DTFDPYLDISL-----EIKT 188
Cdd:cd02662     33 --EQQDAHELFQVLLETLEQLLK----------------FPFDGLLASRIVCLQCGESSkVRYESFTMLSLpvpnqSSGS 94
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  189 AQTLSKAFEQFVKPEQLDGdnaYKCSKCKKMVTASKRftvhrssnVLTISLKRFTnFNG-GKITKD---VRYAEHLDlrp 264
Cdd:cd02662     95 GTTLEHCLDDFLSTEIIDD---YKCDRCQTVIVRLPQ--------ILCIHLSRSV-FDGrGTSTKNsckVSFPERLP--- 159
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  265 fmsqshgePQIYALYAVLVHSGfSCHAGHYYCY--------------------IKASN-GQWYQMNDSSVSLSDIRTVLN 323
Cdd:cd02662    160 --------KVLYRLRAVVVHYG-SHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTsHPWWRISDTTVKEVSESEVLE 230

                   ....*....
gi 1207190300  324 Q-QAYLLFY 331
Cdd:cd02662    231 QkSAYMLFY 239
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
191-333 1.84e-18

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 91.10  E-value: 1.84e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  191 TLSKAFEQFVKPEQLDGDNAYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFTNFNGG--KITKDVRYA-EHLDLRPFMS 267
Cdd:COG5560    676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFrdKIDDLVEYPiDDLDLSGVEY 755
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190300  268 QSHGEPQIYALYAVLVHSGFScHAGHYYCYIK-ASNGQWYQMNDSSVSLSDIRTVLNQQAYLLFYIR 333
Cdd:COG5560    756 MVDDPRLIYDLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
35-194 2.81e-14

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 77.62  E-value: 2.81e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   35 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFCMM-----CTMQNHIIQVFANSGNVIKPISVLNELKRI 109
Cdd:COG5560    267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMhgsvaSAYADLIKQLYDGNLHAFTPSGFKKTIGSF 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  110 GKHFRFGSQEDAHEFLRYTVDAMQK--------------SCLPGNKLDRQTQAT-----------TFVHQIFGGYLRSRV 164
Cdd:COG5560    347 NEEFSGYDQQDSQEFIAFLLDGLHEdlnriikkpytskpDLSPGDDVVVKKKAKecwwehlkrndSIITDLFQGMYKSTL 426
                          170       180       190
                   ....*....|....*....|....*....|
gi 1207190300  165 KCLNCKAVSDTFDPYLDISLEIKTAQTLSK 194
Cdd:COG5560    427 TCPGCGSVSITFDPFMDLTLPLPVSMVWKH 456
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
34-313 7.37e-12

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 67.68  E-value: 7.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   34 AGLHNLGNTCFLNSTLQCLTYTAPLANYMLtrEHSKTCHEPGFCMMC-------TMQNhiiqvfANSGNV-----IKPIS 101
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLAL--SHLATECLKEHCLLCelgflfdMLEK------AKGKNCqasnfLRALS 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  102 VLNELKRIGKHFRFGSQEDAHE-------FLRYTVDAMQKSCLPGNKldRQTQATTFVHQIFGGYLRSRVKCLNCKAVSD 174
Cdd:pfam13423   73 SIPEASALGLLDEDRETNSAISlssliqsFNRFLLDQLSSEENSTPP--NPSPAESPLEQLFGIDAETTIRCSNCGHESV 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  175 TFDPYLDISL------EIKTAQTLSKAFEQFVKpEQLDGDNAYK--CSKCKKMVTASKRFTVHRSSNVLTISLKrFTNFN 246
Cdd:pfam13423  151 RESSTHVLDLiyprkpSSNNKKPPNQTFSSILK-SSLERETTTKawCEKCKRYQPLESRRTVRNLPPVLSLNAA-LTNEE 228
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207190300  247 GGKITKDVRY-AEHLDLRPFM-SQSHGEPQIYALYAVLVHSGFSCHAGHYYCYIKASN--------GQWYQMNDSSV 313
Cdd:pfam13423  229 WRQLWKTPGWlPPEIGLTLSDdLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKVADseledpteSQWYLFNDFLV 305
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
36-331 8.71e-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: 63.32  E-value: 8.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   36 LHNLGNTCFLNSTLQCLTYTaplanymltrehsktchepgfcmmctmqNHIIQVFANSgnvikpisvlnelkrigkhfrf 115
Cdd:cd02673      2 LVNTGNSCYFNSTMQALSSI----------------------------GKINTEFDND---------------------- 31
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  116 gSQEDAHEFLRYTVDAMQKscLPGNKLDRQTQATTFVHQI-----FGGYLRSRVKCLNCK--AVSDTFDPYLDISLEIKT 188
Cdd:cd02673     32 -DQQDAHEFLLTLLEAIDD--IMQVNRTNVPPSNIEIKRLnpleaFKYTIESSYVCIGCSfeENVSDVGNFLDVSMIDNK 108
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  189 A---QTLSKAFEQFVKPEQldgdnayKCSKCK-KMVTASKRFTvhRSSNVLTISLKRFtnfnggkitkDVRYAEHLDL-- 262
Cdd:cd02673    109 LdidELLISNFKTWSPIEK-------DCSSCKcESAISSERIM--TFPECLSINLKRY----------KLRIATSDYLkk 169
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207190300  263 -RPFMSQSHGEPQIYALYAVLVHSGFSCHAGHYYCYIKAS--NGQWYQMNDSS---VSLSDIRTVLNQQAYLLFY 331
Cdd:cd02673    170 nEEIMKKYCGTDAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEirpVSKNDVSTNARSSGYLIFY 244
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
35-314 1.81e-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: 1.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   35 GLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTCHEPGFcmmctmqnHIIQVFA-------NSGN---VIKPISVLN 104
Cdd:cd02669    121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKS--------ELVKRLSelirkiwNPRNfkgHVSPHELLQ 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  105 EL-KRIGKHFRFGSQEDAHEFLRYTVDAMqKSCLPGNKLDRQTQattfVHQIFGGYLR--------------SRVKCLNC 169
Cdd:cd02669    193 AVsKVSKKKFSITEQSDPVEFLSWLLNTL-HKDLGGSKKPNSSI----IHDCFQGKVQietqkikphaeeegSKDKFFKD 267
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  170 KAVSDTFD-PYLDISLEIKTA-----QTLSKAFEQFVKPEQLDGdnaYKCSKCKKMVTASKRFTVHRSSNVLTISLKRFT 243
Cdd:cd02669    268 SRVKKTSVsPFLLLTLDLPPPplfkdGNEENIIPQVPLKQLLKK---YDGKTETELKDSLKRYLISRLPKYLIFHIKRFS 344
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207190300  244 --NFNGGKITKDVRY-AEHLDLRPFMSQ---SHGEPQIYALYAVLVHSGFSCHAGHYYCYI-KASNGQWYQMNDSSVS 314
Cdd:cd02669    345 knNFFKEKNPTIVNFpIKNLDLSDYVHFdkpSLNLSTKYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQDLNVK 422
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
34-332 3.11e-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: 56.73  E-value: 3.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300   34 AGLHNLGNTCFLNSTLQCLTYTAPLANYMLTREHSKTchepgfcmmcTMQNHIIQVFANSGNVIKPISVL------NELK 107
Cdd:cd02666      2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKA----------ELASDYPTERRIGGREVSRSELQrsnqfvYELR 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  108 RIGKH-------------------FRfgsQEDAHE------FLRYTVDAMQKSCLPGNKLDRQTQATTFVHQIF-GGYLR 161
Cdd:cd02666     72 SLFNDlihsntrsvtpskelaylaLR---QQDVTEcidnvlFQLEVALEPISNAFAGPDTEDDKEQSDLIKRLFsGKTKQ 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  162 SRVKCLNCKAVSDTFDPYLDISLEIKT------------AQTLSKAFEQFVKPEQL-----DGDNAYKCSKCK-KMVTAS 223
Cdd:cd02666    149 QLVPESMGNQPSVRTKTERFLSLLVDVgkkgreivvllePKDLYDALDRYFDYDSLtklpqRSQVQAQLAQPLqRELISM 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  224 KRFTVHRSSN-VLTISLKRFTNFNGGKITKDVRYAEHLDLRPfmSQSHGEPQI-YALYAVLVHSGfSCHAGHYYCYIK-A 300
Cdd:cd02666    229 DRYELPSSIDdIDELIREAIQSESSLVRQAQNELAELKHEIE--KQFDDLKSYgYRLHAVFIHRG-EASSGHYWVYIKdF 305
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1207190300  301 SNGQWYQMNDSSVSLSDIRTVLNQ------QAYLLFYI 332
Cdd:cd02666    306 EENVWRKYNDETVTVVPASEVFLFtlgntaTPYFLVYV 343
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
764-860 8.63e-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: 8.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  764 EDRNRGSDRPHFSSTPKDRERYRHyRDHSdRSRSRYGHSYQDSRRSTSRER-YYRDRDLERHWDRFSHHRREHHYFQRRH 842
Cdd:TIGR01642    5 PDREREKSRGRDRDRSSERPRRRS-RDRS-RFRDRHRRSRERSYREDSRPRdRRRYDSRSPRSLRYSSVRRSRDRPRRRS 82
                           90
                   ....*....|....*...
gi 1207190300  843 RDERDWNRDRRFGSDSYR 860
Cdd:TIGR01642   83 RSVRSIEQHRRRLRDRSP 100
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
765-857 2.52e-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: 2.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  765 DRNRGSDRPhfSSTPKDRERYRHYRDHSDRSRSRyghsyqDSRRSTSRER-YYRDRDLERHWDRFSHHRREHHYFQRRHR 843
Cdd:TIGR01622    4 DRERERLRD--SSSAGDRDRRRDKGRERSRDRSR------DRERSRSRRRdRHRDRDYYRGRERRSRSRRPNRRYRPREK 75
                           90
                   ....*....|....
gi 1207190300  844 DERDWNRDRRFGSD 857
Cdd:TIGR01622   76 RRRRGDSYRRRRDD 89
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
234-332 3.11e-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: 49.48  E-value: 3.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  234 VLTISLKRFtNFNGGKITKdvryaEHLDLR-PFMSQSHGepqiYALYAVLVHSGfSCHAGHYYCYI-KASNGQWYQMNDS 311
Cdd:cd02665    131 VLTFELSRF-EFNQGRPEK-----IHDKLEfPQIIQQVP----YELHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYNDI 199
                           90       100
                   ....*....|....*....|....*....
gi 1207190300  312 SVSLSDIRTV--------LNQQAYLLFYI 332
Cdd:cd02665    200 SVTESSWEEVerdsfgggRNPSAYCLMYI 228
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
780-869 6.96e-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: 6.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  780 KDRERYRHYRDHSDRSRSRyghsyqdsRRSTSREryyRDRDLERHWDRFSHHRREhhyfqrRHRDeRDWNRDRRFGSDSY 859
Cdd:TIGR01622    3 RDRERERLRDSSSAGDRDR--------RRDKGRE---RSRDRSRDRERSRSRRRD------RHRD-RDYYRGRERRSRSR 64
                           90
                   ....*....|
gi 1207190300  860 RPSGYHNRNG 869
Cdd:TIGR01622   65 RPNRRYRPRE 74
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
803-923 1.20e-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: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  803 YQDSRRSTSRERYyRDRDLERHWDRfshhRREHHYFQRRHRderdWNRDRRFGSDSyRPsgyHNRNGYSNHSHRGMEEAH 882
Cdd:TIGR01642    4 EPDREREKSRGRD-RDRSSERPRRR----SRDRSRFRDRHR----RSRERSYREDS-RP---RDRRRYDSRSPRSLRYSS 70
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1207190300  883 GRATHTVNGSKGRPSSPHSVSplpRHHKRKRSPSVDARESS 923
Cdd:TIGR01642   71 VRRSRDRPRRRSRSVRSIEQH---RRRLRDRSPSNQWRKDD 108
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
780-877 3.39e-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: 3.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  780 KDRERYRHYRDHSDRSRSRYGHSYQDSRRSTSRERYYRDRDLERHWDRFSHHRREHHYFQRRHRDERDWNRDRrfgSDSY 859
Cdd:TIGR01642    1 RDEEPDREREKSRGRDRDRSSERPRRRSRDRSRFRDRHRRSRERSYREDSRPRDRRRYDSRSPRSLRYSSVRR---SRDR 77
                           90
                   ....*....|....*...
gi 1207190300  860 RPSGYHNRNGYSNHSHRG 877
Cdd:TIGR01642   78 PRRRSRSVRSIEQHRRRL 95
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
780-873 4.16e-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: 4.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  780 KDRERYRHYRDHSDRSRSRYGHSYQDSRRSTSRERYyRDRDLERHWDRFSHHRREhhyfqRRHRDERDWNRDRRFGSDSY 859
Cdd:TIGR01622    5 RERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERS-RSRRRDRHRDRDYYRGRE-----RRSRSRRPNRRYRPREKRRR 78
                           90
                   ....*....|....
gi 1207190300  860 RPSGYHNRNGYSNH 873
Cdd:TIGR01622   79 RGDSYRRRRDDRRS 92
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
743-853 2.15e-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: 2.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  743 SKEAKPSHSDKFGSGDGWRSGEDRNRGSDRPHFSSTPKDRERYRH-----YRDHSDRSRSRYGHSYQDSRRSTSR--ERY 815
Cdd:TIGR01622    4 DRERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRRRDRHrdrdyYRGRERRSRSRRPNRRYRPREKRRRrgDSY 83
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1207190300  816 YRDRDLERhwdrfshHRREHHYFQRRHRDE-RDWNRDRR 853
Cdd:TIGR01622   84 RRRRDDRR-------SRREKPRARDGTPEPlTEDERDRR 115
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
764-853 4.76e-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: 4.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  764 EDRNRGSDRPHFSSTPKDRERYRHYRdhSDRSRSRYGHSyqdSRRSTSRERYYRDRDLERHWDRFSHHRRehhyfQRRHR 843
Cdd:pfam12871   20 EDEEASDESERASLSRKRRSRSRRRS--STRDRSRSRSR---SRSRDRRSRGTRDRRRDRDRDRYRSLRS-----RSRDR 89
                           90
                   ....*....|
gi 1207190300  844 DeRDWNRDRR 853
Cdd:pfam12871   90 S-RDRDRDRR 98
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
739-824 1.11e-03

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: 39.37  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  739 SEGESKEAKPSHSDKFGSGDGWRSGEDRNRGSDRPHFSSTPKDRERYRHYRDHSDRSRSRYgHSYQDSRRSTSRERyYRD 818
Cdd:pfam12871   15 EEDEEEDEEASDESERASLSRKRRSRSRRRSSTRDRSRSRSRSRSRDRRSRGTRDRRRDRD-RDRYRSLRSRSRDR-SRD 92

                   ....*.
gi 1207190300  819 RDLERH 824
Cdd:pfam12871   93 RDRDRR 98
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
743-864 1.74e-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: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  743 SKEAKPSHSDKFGSGDGWRSGEDRNRGSDRPHFSSTPKDRERYRHYRDHSDRSRSRYGHSYQDSRRSTSRERyYRDRDLe 822
Cdd:TIGR01642    8 EREKSRGRDRDRSSERPRRRSRDRSRFRDRHRRSRERSYREDSRPRDRRRYDSRSPRSLRYSSVRRSRDRPR-RRSRSV- 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1207190300  823 rhwDRFSHHRREHHYFQRRHRDERDWNrdRRFGSDsYRPSGY 864
Cdd:TIGR01642   86 ---RSIEQHRRRLRDRSPSNQWRKDDK--KRSLWD-IKPPGY 121
PRK12678 PRK12678
transcription termination factor Rho; Provisional
756-861 2.02e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.20  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  756 SGDGWRSGEDRNRGSDRPHfsstpKDRERYRHYRDHSDRSRSRYGHSYQDSRRSTSRERYYRDRDLERHWDRfshHRREh 835
Cdd:PRK12678   193 REERGRDGDDRDRRDRREQ-----GDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRG---GRRG- 263
                           90       100
                   ....*....|....*....|....*.
gi 1207190300  836 hyfqRRHRDERDWNRDRRFGSDSYRP 861
Cdd:PRK12678   264 ----RRFRDRDRRGRRGGDGGNEREP 285
PRK12678 PRK12678
transcription termination factor Rho; Provisional
739-857 3.34e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.43  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  739 SEGESKEAKPSHSDKFGSGDGWRSGEDRNRGSDRphfsstpKDRERYRHYRDHSDRSRSRYGHSYQDSRRSTSRERYYRD 818
Cdd:PRK12678   167 EERDERRRRGDREDRQAEAERGERGRREERGRDG-------DDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDAR 239
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1207190300  819 RDLERHWDRFSHHRREHHYFQRRHRDERDWNRDRRFGSD 857
Cdd:PRK12678   240 GDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGD 278
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
816-925 6.76e-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: 6.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207190300  816 YRDRDLERHWDRFSHHRREHHYFQRRHRDeRDWNRDRRFGSDSYRPSGyHNRNGYSNHSHRGMEEAHGRATHTVNGSKGR 895
Cdd:TIGR01622    2 YRDRERERLRDSSSAGDRDRRRDKGRERS-RDRSRDRERSRSRRRDRH-RDRDYYRGRERRSRSRRPNRRYRPREKRRRR 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 1207190300  896 PSSphsvSPLPRHHKRKRSPSVDARESSDE 925
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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