NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|297338777|gb|EFH69194|]
View 

ubiquitin-specific protease 15 [Arabidopsis lyrata subsp. lyrata]

Protein Classification

zf-MYND and Peptidase_C19E domain-containing protein( domain architecture ID 10484418)

zf-MYND and Peptidase_C19E domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 441-746 2.01e-167

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: 489.86  E-value: 2.01e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 441 PRGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWCLMCELEQHVMMLRESGGPLSASRIL-SHMRSINCQ 519
Cdd:cd02661    1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFsSNLKQISKH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 520 IGDGSQEDAHEFLRLLVASMQSICLERLGGETKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYG 599
Cdd:cd02661   81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 600 WvESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYGKINKCISFPEMLDMIPFMT 679
Cdd:cd02661  161 A-DSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297338777 680 RTGDVPPLYMLYAVIVHLDTLNasFSGHYISYVKDLRGNWYRIDDSEIHRVPMTQVMSEGAYMLFYM 746
Cdd:cd02661  240 QPNDGPLKYKLYAVLVHSGFSP--HSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
zf-MYND pfam01753
MYND finger;
130-167 1.64e-10

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 56.66  E-value: 1.64e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 297338777  130 CARCFGPAKT--RCSRCKSVRYCSGKCQIIHWrIAHKDEC 167
Cdd:pfam01753   1 CAVCGKEALKllRCSRCKSVYYCSKECQKADW-PYHKKEC 39
 
Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 441-746 2.01e-167

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: 489.86  E-value: 2.01e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 441 PRGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWCLMCELEQHVMMLRESGGPLSASRIL-SHMRSINCQ 519
Cdd:cd02661    1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFsSNLKQISKH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 520 IGDGSQEDAHEFLRLLVASMQSICLERLGGETKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYG 599
Cdd:cd02661   81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 600 WvESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYGKINKCISFPEMLDMIPFMT 679
Cdd:cd02661  161 A-DSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297338777 680 RTGDVPPLYMLYAVIVHLDTLNasFSGHYISYVKDLRGNWYRIDDSEIHRVPMTQVMSEGAYMLFYM 746
Cdd:cd02661  240 QPNDGPLKYKLYAVLVHSGFSP--HSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
442-745 1.45e-73

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 244.27  E-value: 1.45e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  442 RGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWC--LMCELEQ--HVMMLRESGGPLSASRILSHMRSIN 517
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDlfKALQKNSKSSSVSPKMFKKSLGKLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  518 CQIGDGSQEDAHEFLRLLVASMQSIClerlggetKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEI 597
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDL--------NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  598 YG-----WVESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYG--KINKCISFPE 670
Cdd:pfam00443 153 PGdsaelKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTweKLNTEVEFPL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  671 MLDMIPFMTRTGDVP----PLYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDSEIHRVPM-TQVMSEGAYMLF 744
Cdd:pfam00443 233 ELDLSRYLAEELKPKtnnlQDYRLVAVVVHSGSLS---SGHYIAYIKAYENNrWYKFDDEKVTEVDEeTAVLSSSAYILF 309


                  .
gi 297338777  745 Y 745
Cdd:pfam00443 310 Y 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 443-747 1.61e-30

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 129.99  E-value: 1.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  443 GLVNCGNSCYANAVLQSLTCTKPL--VAYLLRRSHSRscsGKDWCLMCeLEQHVMMLRESGGPLSASRIlshMRSINCQI 520
Cdd:COG5077   195 GLRNQGATCYMNSLLQSLFFIAKFrkDVYGIPTDHPR---GRDSVALA-LQRLFYNLQTGEEPVDTTEL---TRSFGWDS 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  521 GDG-SQEDAHEFLRLLVASmqsicLERLGGETKVDPRLQEttlvqhMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYG 599
Cdd:COG5077   268 DDSfMQHDIQEFNRVLQDN-----LEKSMRGTVVENALNG------IFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  600 wVESLQDALTQFTRPEDLDGENMYRCSRcAGYVRARKELSIHEAPNILTIVLKRFQ----EGRYGKINKCISFPEMLDMI 675
Cdd:COG5077   337 -MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEydfeRDMMVKINDRYEFPLEIDLL 414

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  676 PFMTRTGD----VPPLYMLYAVIVHLDTLNasfSGHYISYVK-DLRGNWYRIDDSEIHRVPMTQVMSE------------ 738
Cdd:COG5077   415 PFLDRDADksenSDAVYVLYGVLVHSGDLH---EGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdki 491

                         330
                  ....*....|....*....
gi 297338777  739 ----------GAYMLFYMR 747
Cdd:COG5077   492 rdhsgikrfmSAYMLVYLR 510
zf-MYND pfam01753
MYND finger;
130-167 1.64e-10

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 56.66  E-value: 1.64e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 297338777  130 CARCFGPAKT--RCSRCKSVRYCSGKCQIIHWrIAHKDEC 167
Cdd:pfam01753   1 CAVCGKEALKllRCSRCKSVYYCSKECQKADW-PYHKKEC 39
zf-HIT_ZNHIT1_like cd21437
HIT zinc finger found in zinc finger HIT domain-containing protein 1 (ZNHIT1) and similar ...
 128-158 2.01e-03

HIT zinc finger found in zinc finger HIT domain-containing protein 1 (ZNHIT1) and similar proteins; The family includes ZNHIT1 and its yeast counterpart, the vacuolar protein sorting-associated protein 71 (Vps71p). ZNHIT1, also known as cyclin-G1-binding protein 1 (CGBP1), zinc finger protein subfamily 4A member 1 (ZNFN4A1), or p18 Hamlet, may have a role in inducing apoptosis through p53 signaling. It binds to Rev-erb beta and releases its inhibitory effect on the transcription of apolipoprotein C3 (APOC3) without affecting its DNA-binding activity. The yeast counterpart Vps71p, also referred to as SWR complex protein 6 (Swc6p), plays a role in the exchange of histone H2A for the H2A variant HZT1, a euchromatin-specific factor, leading to chromatin remodeling and transcriptional changes of targeted genes. It is indirectly involved in vacuolar protein sorting. Members of this family contain a zf-HIT domain characterized by a "treble-clef" fold through interleaved CCCC and CCHC zinc finger motifs, both of which bind a zinc ion.


Pssm-ID: 467791  Cd Length: 43  Bit Score: 36.83  E-value: 2.01e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 297338777 128 HVCARCFGPAKTRCSRCkSVRYCSGKCQIIH 158
Cdd:cd21437    8 KFCSVCGYWGKYTCVRC-GARYCSLKCLETH 37
 
Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 441-746 2.01e-167

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: 489.86  E-value: 2.01e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 441 PRGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWCLMCELEQHVMMLRESGGPLSASRIL-SHMRSINCQ 519
Cdd:cd02661    1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFsSNLKQISKH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 520 IGDGSQEDAHEFLRLLVASMQSICLERLGGETKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYG 599
Cdd:cd02661   81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 600 WvESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYGKINKCISFPEMLDMIPFMT 679
Cdd:cd02661  161 A-DSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMS 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297338777 680 RTGDVPPLYMLYAVIVHLDTLNasFSGHYISYVKDLRGNWYRIDDSEIHRVPMTQVMSEGAYMLFYM 746
Cdd:cd02661  240 QPNDGPLKYKLYAVLVHSGFSP--HSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
442-745 1.45e-73

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 244.27  E-value: 1.45e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  442 RGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWC--LMCELEQ--HVMMLRESGGPLSASRILSHMRSIN 517
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDlfKALQKNSKSSSVSPKMFKKSLGKLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  518 CQIGDGSQEDAHEFLRLLVASMQSIClerlggetKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEI 597
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDL--------NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  598 YG-----WVESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYG--KINKCISFPE 670
Cdd:pfam00443 153 PGdsaelKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTweKLNTEVEFPL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  671 MLDMIPFMTRTGDVP----PLYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDSEIHRVPM-TQVMSEGAYMLF 744
Cdd:pfam00443 233 ELDLSRYLAEELKPKtnnlQDYRLVAVVVHSGSLS---SGHYIAYIKAYENNrWYKFDDEKVTEVDEeTAVLSSSAYILF 309


                  .
gi 297338777  745 Y 745
Cdd:pfam00443 310 Y 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 443-746 1.67e-65

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: 220.43  E-value: 1.67e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 443 GLVNCGNSCYANAVLQSLTCtkplvayllrrshsrscsgkdwclmceleqhvmmlresggplsasrilshmrsincqigd 522
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 523 gSQEDAHEFLRLLVASMQSICLERLGGEtkvDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEI---YG 599
Cdd:cd02257   21 -EQQDAHEFLLFLLDKLHEELKKSSKRT---SDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkGL 96

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 600 WVESLQDALTQFTRPEDLDGENMYRCSRCaGYVRARKELSIHEAPNILTIVLKRFQ---EGRYGKINKCISFPEMLDMIP 676
Cdd:cd02257   97 PQVSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSP 175

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 677 FMT------RTGDVPPLYMLYAVIVHLDTlnASFSGHYISYVKD-LRGNWYRIDDSEIHRVPMTQVMSEG-----AYMLF 744
Cdd:cd02257  176 YLSegekdsDSDNGSYKYELVAVVVHSGT--SADSGHYVAYVKDpSDGKWYKFNDDKVTEVSEEEVLEFGslsssAYILF 253


                 ..
gi 297338777 745 YM 746
Cdd:cd02257  254 YE 255
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 442-745 1.50e-62

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: 214.93  E-value: 1.50e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 442 RGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDW--CLMCELEQ--HVMMLRESGGPLSASRILSHMRSIN 517
Cdd:cd02660    1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPnsCLSCAMDEifQEFYYSGDRSPYGPINLLYLSWKHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 518 CQIGDGSQEDAHEFLRLLVASMQSICLERLGGETKVDPrlqeTTLVQHM-FGGRLRSKVKCLRCDHESERYENIMDLTLE 596
Cdd:cd02660   81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESH----CNCIIHQtFSGSLQSSVTCQRCGGVSTTVDPFLDLSLD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 597 I-----YGWVES---------LQDALTQFTRPEDLdGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQ---EGRY 659
Cdd:cd02660  157 IpnkstPSWALGesgvsgtptLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEhslNKTS 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 660 GKINKCISFPEMLDMIPFMT----RTGDVPPL-----YMLYAVIVHLDTLNasfSGHYISYVKDLRGNWYRIDDSEIHRV 730
Cdd:cd02660  236 RKIDTYVQFPLELNMTPYTSssigDTQDSNSLdpdytYDLFAVVVHKGTLD---TGHYTAYCRQGDGQWFKFDDAMITRV 312

                        330
                 ....*....|....*
gi 297338777 731 PMTQVMSEGAYMLFY 745
Cdd:cd02660  313 SEEEVLKSQAYLLFY 327
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 443-750 2.67e-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: 197.48  E-value: 2.67e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 443 GLVNCGNSCYANAVLQSLTCTKPLVAYLLR---RSHSRSCSGKdwclMCELEQHVMMLRESGGPLSASRILSHMRSINCQ 519
Cdd:cd02659    4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSippTEDDDDNKSV----PLALQRLFLFLQLSESPVKTTELTDKTRSFGWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 520 IGD-GSQEDAHEFLRLLVASMqsiclerlggETKVDPRLQETtLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIY 598
Cdd:cd02659   80 SLNtFEQHDVQEFFRVLFDKL----------EEKLKGTGQEG-LIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVK 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 599 GwVESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF----QEGRYGKINKCISFPEMLDM 674
Cdd:cd02659  149 G-KKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFefdfETMMRIKINDRFEFPLELDM 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 675 IPFMTRTGDVPP-----------LYMLYAVIVHLDTLNasfSGHYISYVKDLR-GNWYRIDDSEIHRVPMTQVMSE---- 738
Cdd:cd02659  228 EPYTEKGLAKKEgdsekkdsesyIYELHGVLVHSGDAH---GGHYYSYIKDRDdGKWYKFNDDVVTPFDPNDAEEEcfgg 304

                        330       340       350
                 ....*....|....*....|....*....|
gi 297338777 739 ------------------GAYMLFYMRSYP 750
Cdd:cd02659  305 eetqktydsgprafkrttNAYMLFYERKSP 334
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 443-745 1.75e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 188.65  E-value: 1.75e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 443 GLVNCGNSCYANAVLQSLtctkplvayllrrshsrscsgkdwclmceleqhvmmlresggplsasrilSHMrsincqigd 522
Cdd:cd02674    1 GLRNLGNTCYMNSILQCL--------------------------------------------------SAD--------- 21

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 523 gsQEDAHEFLRLLVASMQSIclerlggetkvdprlqettlVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYGW-- 600
Cdd:cd02674   22 --QQDAQEFLLFLLDGLHSI--------------------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGsg 79

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 601 ---VESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF--QEGRYGKINKCISFP-EMLDM 674
Cdd:cd02674   80 dapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFsfSRGSTRKLTTPVTFPlNDLDL 159

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297338777 675 IPFMTRTGDVPP-LYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDSEIHRVPMTQVMSEGAYMLFY 745
Cdd:cd02674  160 TPYVDTRSFTGPfKYDLYAVVNHYGSLN---GGHYTAYCKNNETNdWYKFDDSRVTKVSESSVVSSSAYILFY 229
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 443-745 2.20e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 184.90  E-value: 2.20e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 443 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRShsrscsgkdwclmceleqhVMMLREsggplsasrilshMRSINCQIGD 522
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETP-------------------KELFSQ-------------VCRKAPQFKG 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 523 GSQEDAHEFLRLLVASMQsiclerlggetkvdprlqetTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYGWVE 602
Cdd:cd02667   49 YQQQDSHELLRYLLDGLR--------------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK 108

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 603 ---SLQDALTQFTRPEDLDGENMYRCSRCagyVRARKELSIHEAPNILTIVLKRFQEGRYG---KINKCISFPEMLDMIP 676
Cdd:cd02667  109 secSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPRSAnlrKVSRHVSFPEILDLAP 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 677 FMTRTGDVP-----PLYMLYAVIVHLDTLNasfSGHYISYVKD----------------------LRGNWYRIDDSEIHR 729
Cdd:cd02667  186 FCDPKCNSSedkssVLYRLYGVVEHSGTMR---SGHYVAYVKVrppqqrlsdltkskpaadeagpGSGQWYYISDSDVRE 262

                        330
                 ....*....|....*.
gi 297338777 730 VPMTQVMSEGAYMLFY 745
Cdd:cd02667  263 VSLEEVLKSEAYLLFY 278
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 443-745 1.96e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 149.18  E-value: 1.96e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 443 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRScsGKDWCLMCELEQHVMML----RESGGP----LSASRILShmr 514
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRL--GDSQSVMKKLQLLQAHLmhtqRRAEAPpdyfLEASRPPW--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 515 sincqIGDGSQEDAHEFLRLLvasmqsicLERLggetkvdprlqeTTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLT 594
Cdd:cd02664   76 -----FTPGSQQDCSEYLRYL--------LDRL------------HTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLD 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 595 LEiygwVESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGR-YGK---------INK 664
Cdd:cd02664  131 LS----FPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQkTHVrekimdnvsINE 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 665 CISFP-----------EMLDMIPFMTRTG--DVPPLYMLYAVIVHLDTlnASFSGHYISYV------------------- 712
Cdd:cd02664  207 VLSLPvrveskssespLEKKEEESGDDGElvTRQVHYRLYAVVVHSGY--SSESGHYFTYArdqtdadstgqecpepkda 284

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 297338777 713 --KDLRGNWYRIDDSeihRVPMTQVMS----------EGAYMLFY 745
Cdd:cd02664  285 eeNDESKNWYLFNDS---RVTFSSFESvqnvtsrfpkDTPYILFY 326
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 443-745 1.03e-37

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: 143.22  E-value: 1.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 443 GLVNCGNSCYANAVLQSL------TCTKPLVayllrrsHSRSCSGKDWclmceleqhvmmlresgGPLSASRILSHMRSI 516
Cdd:cd02663    1 GLENFGNTCYCNSVLQALyfenllTCLKDLF-------ESISEQKKRT-----------------GVISPKKFITRLKRE 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 517 NcQIGDGS-QEDAHEFLRLLVASmqsiCLERLGGETKVDPRLQ----------ETTLVQHMFGGRLRSKVKCLRCDHESE 585
Cdd:cd02663   57 N-ELFDNYmHQDAHEFLNFLLNE----IAEILDAERKAEKANRklnnnnnaepQPTWVHEIFQGILTNETRCLTCETVSS 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 586 RYENIMDLTLEIYGWVeSLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF----QEGRYGK 661
Cdd:cd02663  132 RDETFLDLSIDVEQNT-SITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFkydeQLNRYIK 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 662 INKCISFPemLDMIPFMTRTGDVPP--LYMLYAVIVHLDtlNASFSGHYISYVKdLRGNWYRIDDSEIHRVPMTQVM--- 736
Cdd:cd02663  211 LFYRVVFP--LELRLFNTTDDAENPdrLYELVAVVVHIG--GGPNHGHYVSIVK-SHGGWLLFDDETVEKIDENAVEeff 285

                        330
                 ....*....|....
gi 297338777 737 -----SEGAYMLFY 745
Cdd:cd02663  286 gdspnQATAYVLFY 299
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 443-745 4.31e-35

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: 136.40  E-value: 4.31e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 443 GLVNCGNSCYANAVLQSLTCTKPLvayllRRShsrscsgkdwCLMCELEQHVMMLR-ESGGPLSASRILSHMRSINCQ-- 519
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEF-----RKA----------VYECNSTEDAELKNmPPDKPHEPQTIIDQLQLIFAQlq 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 520 -----------------IGDGSQEDAHEFLRLLVASMQSiCLERLGgetkvDPRLQetTLVQHMFGGRLRSKVKCLRCDH 582
Cdd:cd02668   66 fgnrsvvdpsgfvkalgLDTGQQQDAQEFSKLFLSLLEA-KLSKSK-----NPDLK--NIVQDLFRGEYSYVTQCSKCGR 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 583 ESERYENIMDLTLEIYGwVESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF----QEGR 658
Cdd:cd02668  138 ESSLPSKFYELELQLKG-HKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFvfdrKTGA 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 659 YGKINKCISFPEMLDMIPFMTRTGDVPPLYMLYAVIVHLDtlNASFSGHYISYVKD-LRGNWYRIDDSEIHRVPMTQVM- 736
Cdd:cd02668  217 KKKLNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQG--VSAYSGHYIAHIKDeQTGEWYKFNDEDVEEMPGKPLKl 294

                        330       340
                 ....*....|....*....|....*....
gi 297338777 737 --------------------SEGAYMLFY 745
Cdd:cd02668  295 gnsedpakprkseikkgthsSRTAYMLVY 323
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 443-747 1.61e-30

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 129.99  E-value: 1.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  443 GLVNCGNSCYANAVLQSLTCTKPL--VAYLLRRSHSRscsGKDWCLMCeLEQHVMMLRESGGPLSASRIlshMRSINCQI 520
Cdd:COG5077   195 GLRNQGATCYMNSLLQSLFFIAKFrkDVYGIPTDHPR---GRDSVALA-LQRLFYNLQTGEEPVDTTEL---TRSFGWDS 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  521 GDG-SQEDAHEFLRLLVASmqsicLERLGGETKVDPRLQEttlvqhMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYG 599
Cdd:COG5077   268 DDSfMQHDIQEFNRVLQDN-----LEKSMRGTVVENALNG------IFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  600 wVESLQDALTQFTRPEDLDGENMYRCSRcAGYVRARKELSIHEAPNILTIVLKRFQ----EGRYGKINKCISFPEMLDMI 675
Cdd:COG5077   337 -MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEydfeRDMMVKINDRYEFPLEIDLL 414

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  676 PFMTRTGD----VPPLYMLYAVIVHLDTLNasfSGHYISYVK-DLRGNWYRIDDSEIHRVPMTQVMSE------------ 738
Cdd:COG5077   415 PFLDRDADksenSDAVYVLYGVLVHSGDLH---EGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdki 491

                         330
                  ....*....|....*....
gi 297338777  739 ----------GAYMLFYMR 747
Cdd:COG5077   492 rdhsgikrfmSAYMLVYLR 510
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 443-745 5.01e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 118.84  E-value: 5.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 443 GLVNCGNSCYANAVLQSLtCTKPLVAYLLRRSHSRSCSGKDWCLMCEL--EQHVMMLRESggplSASRILSHMRSINCQI 520
Cdd:cd02671   26 GLNNLGNTCYLNSVLQVL-YFCPGFKHGLKHLVSLISSVEQLQSSFLLnpEKYNDELANQ----APRRLLNALREVNPMY 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 521 GDGSQEDAHEFLRLLVASMQSiclerlggetkvdprlqettLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTL----- 595
Cdd:cd02671  101 EGYLQHDAQEVLQCILGNIQE--------------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVpvqes 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 596 EIYGWVES-------------LQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQE------ 656
Cdd:cd02671  161 ELSKSEESseispdpktemktLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAAngsefd 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 657 --GRYGKINKCISFPemLDMIPFMTRTGDVPPLYMLYAVIVHLD-TLNasfSGHYISYVKdlrgnWYRIDDSEIhRVpMT 733
Cdd:cd02671  241 cyGGLSKVNTPLLTP--LKLSLEEWSTKPKNDVYRLFAVVMHSGaTIS---SGHYTAYVR-----WLLFDDSEV-KV-TE 308

                        330       340
                 ....*....|....*....|...
gi 297338777 734 QVMSEGA-----------YMLFY 745
Cdd:cd02671  309 EKDFLEAlspntsststpYLLFY 331
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 443-745 1.37e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 112.07  E-value: 1.37e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 443 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRrshsrscsgkdwclmcELEQHvmmlresggplsasrilshmrsincqigd 522
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEYLEE----------------FLEQQ----------------------------- 35

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 523 gsqeDAHEFLRLLVASMQSIClerlggetkvdprlqettlvQHMFGGRLRSKVKCLRCDHESE-RYENIMDLTL----EI 597
Cdd:cd02662   36 ----DAHELFQVLLETLEQLL--------------------KFPFDGLLASRIVCLQCGESSKvRYESFTMLSLpvpnQS 91

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 598 YGWVESLQDALTQFTRPEDLDGenmYRCSRCAgyvrarkeLSIHEAPNILTIVLKRFQEGRYGKI--NKC-ISFPEMLDm 674
Cdd:cd02662   92 SGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVFDGRGTStkNSCkVSFPERLP- 159

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 675 ipfmtrtgdvPPLYMLYAVIVHLDTLNasfSGHYISY---------------------VKDLRGNWYRIDDSEIHRVPMT 733
Cdd:cd02662  160 ----------KVLYRLRAVVVHYGSHS---SGHYVCYrrkplfskdkepgsfvrmregPSSTSHPWWRISDTTVKEVSES 226

                        330
                 ....*....|...
gi 297338777 734 QVMSEG-AYMLFY 745
Cdd:cd02662  227 EVLEQKsAYMLFY 239
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
580-747 1.38e-20

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 97.65  E-value: 1.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 580 CDHESERYENIMDLTLEiygWVES----------LQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTI 649
Cdd:COG5560  646 CEWEEKRYLSLFSYDPL---WTIReigaaertitLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILII 722

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 650 VLKRFQEGRYG--KINKCISFP-EMLDMIPFMTRTGDVPPLYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDS 725
Cdd:COG5560  723 HLKRFSSVRSFrdKIDDLVEYPiDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLS---GGHYTAYARNFANNgWYLFDDS 799

                        170       180
                 ....*....|....*....|..
gi 297338777 726 EIHRVPMTQVMSEGAYMLFYMR 747
Cdd:COG5560  800 RITEVDPEDSVTSSAYVLFYRR 821
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 443-745 1.93e-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 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: 93.16  E-value: 1.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 443 GLVNCGNSCYANAVLQSLTCTKPLVAYLLR--RSHSRSCSGKDWcLMCELEQHVMMLRESGGPLSASRILSHMRSINCQI 520
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNynPARRGANQSSDN-LTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 521 ------GDGSQEDAHEFLRLLVASMQSiCLERLGGETKVdprlqettlVQHMFGGRLRSKVKCLRCDHESE---RYENIM 591
Cdd:cd02657   80 aekqnqGGYAQQDAEECWSQLLSVLSQ-KLPGAGSKGSF---------IDQLFGIELETKMKCTESPDEEEvstESEYKL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 592 DLTLEIYGWVESLQDALTQftRPEDLDGENMYRCSRCAGYVRARKelsIHEAPNILTIVLKRF----QEGRYGKINKCIS 667
Cdd:cd02657  150 QCHISITTEVNYLQDGLKK--GLEEEIEKHSPTLGRDAIYTKTSR---ISRLPKYLTVQFVRFfwkrDIQKKAKILRKVK 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 668 FPEMLDMIPFMTRTGdvppLYMLYAVIVHlDTLNASfSGHYISYVK-DLRGNWYRIDDSEIHRVPMTQV--MSEG----- 739
Cdd:cd02657  225 FPFELDLYELCTPSG----YYELVAVITH-QGRSAD-SGHYVAWVRrKNDGKWIKFDDDKVSEVTEEDIlkLSGGgdwhi 298


                 ....*.
gi 297338777 740 AYMLFY 745
Cdd:cd02657  299 AYILLY 304
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 443-745 4.93e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 92.00  E-value: 4.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 443 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKD--WCLMCELEQ--HVMM----LRESGGPLSASRILSHMR 514
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDpaNDLNCQLIKlaDGLLsgrySKPASLKSENDPYQVGIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 515 SI---NCqIGDGSQE-------DAHEFLRLLvasmqsicLERLGGETKVDPRLQETTLVQHMfggrLRSKVKCLRCDH-- 582
Cdd:cd02658   81 PSmfkAL-IGKGHPEfstmrqqDALEFLLHL--------IDKLDRESFKNLGLNPNDLFKFM----IEDRLECLSCKKvk 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 583 ESERYENIMDLTLE------------IYGWVEsLQDALTQFTRPEDLDgenmYRCSRCAGYVRARKELSIHEAPNILTIV 650
Cdd:cd02658  148 YTSELSEILSLPVPkdeatekeegelVYEPVP-LEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVIN 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 651 LKRFQEGRYG---KINKCISFPEMLDmipfmtrtgdvPPLYMLYAVIVHLDTlnASFSGHYISYVK---DLRGNWYRIDD 724
Cdd:cd02658  223 MKRFQLLENWvpkKLDVPIDVPEELG-----------PGKYELIAFISHKGT--SVHSGHYVAHIKkeiDGEGKWVLFND 289

                        330       340
                 ....*....|....*....|.
gi 297338777 725 SEIHRVPMTQVMSEGAYMLFY 745
Cdd:cd02658  290 EKVVASQDPPEMKKLGYIYFY 310
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
443-724 1.11e-17

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 85.01  E-value: 1.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  443 GLVNCGNSCYANAVLQSLTCTKPLVAYLLrrSHSRSCSGKDWCLMCELeQHV--MMLRESGGPLSAS---RILSHMRSIN 517
Cdd:pfam13423   2 GLETHIPNSYTNSLLQLLRFIPPLRNLAL--SHLATECLKEHCLLCEL-GFLfdMLEKAKGKNCQASnflRALSSIPEAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  518 cQIG---DGSQEDAHEFLRLLVASMQSICLERLGGETKV--DPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMD 592
Cdd:pfam13423  79 -ALGlldEDRETNSAISLSSLIQSFNRFLLDQLSSEENStpPNPSPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777  593 LTLeIYGWVESLQDALTQFTRPED-----LDGENMYR--CSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYGKINKC 665
Cdd:pfam13423 158 LDL-IYPRKPSSNNKKPPNQTFSSilkssLERETTTKawCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQLWKTP 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297338777  666 ISFPEMLDMIPFMTRTGDVPP-LYMLYAVIVHLDtlNASFSGHYISYVK--------DLRGNWYRIDD 724
Cdd:pfam13423 237 GWLPPEIGLTLSDDLQGDNEIvKYELRGVVVHIG--DSGTSGHLVSFVKvadseledPTESQWYLFND 302
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
443-747 1.14e-16

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 81.39  E-value: 1.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 443 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDwclMCELEQHVMMLRESGGPLSASRILSH--MRSINCQi 520
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKELKVLKN---VIRKPEPDLNQEEALKLFTALWSSKEhkVGWIPPM- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 521 gdGSQEDAHEFLRLLvasMQSICLERLG-GETKVDPRLQettlvqhmfggrlrskvkclrcDHESERYENIMDLTLE--I 597
Cdd:COG5533   77 --GSQEDAHELLGKL---LDELKLDLVNsFTIRIFKTTK----------------------DKKKTSTGDWFDIIIElpD 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 598 YGWVE---SLQDALTQFTRPEDLD-----GENMYRCSRCagyvRARKELSIHEAPNILTIVLKRF-QEGRYGKINKCISf 668
Cdd:COG5533  130 QTWVNnlkTLQEFIDNMEELVDDEtgvkaKENEELEVQA----KQEYEVSFVKLPKILTIQLKRFaNLGGNQKIDTEVD- 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 669 pEMLDMIPFMTRTGDVPP--LYMLYAVIVHLDTLNasfSGHYISYVKdLRGNWYRIDDSEIHRVPMTQ---VMSEGAYML 743
Cdd:COG5533  205 -EKFELPVKHDQILNIVKetYYDLVGFVLHQGSLE---GGHYIAYVK-KGGKWEKANDSDVTPVSEEEainEKAKNAYLY 279


                 ....
gi 297338777 744 FYMR 747
Cdd:COG5533  280 FYER 283
zf-MYND pfam01753
MYND finger;
130-167 1.64e-10

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 56.66  E-value: 1.64e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 297338777  130 CARCFGPAKT--RCSRCKSVRYCSGKCQIIHWrIAHKDEC 167
Cdd:pfam01753   1 CAVCGKEALKllRCSRCKSVYYCSKECQKADW-PYHKKEC 39
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 444-745 1.53e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 56.38  E-value: 1.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 444 LVNCGNSCYANAVLQSLtctkplvayllrrshsrSCSGKdwclmceleqhvmmlresggplsasrilshmrsINCQIGDG 523
Cdd:cd02673    2 LVNTGNSCYFNSTMQAL-----------------SSIGK---------------------------------INTEFDND 31

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 524 SQEDAHEFLRLLVASMQSIcLERLGGETKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEI----YG 599
Cdd:cd02673   32 DQQDAHEFLLTLLEAIDDI-MQVNRTNVPPSNIEIKRLNPLEAFKYTIESSYVCIGCSFEENVSDVGNFLDVSMidnkLD 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297338777 600 WVESLQDALTQFTRPEDldgenmyRCSRCAGYVRARKElSIHEAPNILTIVLKRFQE----GRYGKINKCIsfpemldMI 675
Cdd:cd02673  111 IDELLISNFKTWSPIEK-------DCSSCKCESAISSE-RIMTFPECLSINLKRYKLriatSDYLKKNEEI-------MK 175

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297338777 676 PFMTRtgdvPPLYMLYAVIVHL-DTLNAsfsGHYISYVKDLRGN--WYRIDDSEIHRVPMTQVMSE---GAYMLFY 745
Cdd:cd02673  176 KYCGT----DAKYSLVAVICHLgESPYD---GHYIAYTKELYNGssWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
zf-HIT_ZNHIT1_like cd21437
HIT zinc finger found in zinc finger HIT domain-containing protein 1 (ZNHIT1) and similar ...
 128-158 2.01e-03

HIT zinc finger found in zinc finger HIT domain-containing protein 1 (ZNHIT1) and similar proteins; The family includes ZNHIT1 and its yeast counterpart, the vacuolar protein sorting-associated protein 71 (Vps71p). ZNHIT1, also known as cyclin-G1-binding protein 1 (CGBP1), zinc finger protein subfamily 4A member 1 (ZNFN4A1), or p18 Hamlet, may have a role in inducing apoptosis through p53 signaling. It binds to Rev-erb beta and releases its inhibitory effect on the transcription of apolipoprotein C3 (APOC3) without affecting its DNA-binding activity. The yeast counterpart Vps71p, also referred to as SWR complex protein 6 (Swc6p), plays a role in the exchange of histone H2A for the H2A variant HZT1, a euchromatin-specific factor, leading to chromatin remodeling and transcriptional changes of targeted genes. It is indirectly involved in vacuolar protein sorting. Members of this family contain a zf-HIT domain characterized by a "treble-clef" fold through interleaved CCCC and CCHC zinc finger motifs, both of which bind a zinc ion.


Pssm-ID: 467791  Cd Length: 43  Bit Score: 36.83  E-value: 2.01e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 297338777 128 HVCARCFGPAKTRCSRCkSVRYCSGKCQIIH 158
Cdd:cd21437    8 KFCSVCGYWGKYTCVRC-GARYCSLKCLETH 37
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH