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Conserved domains on  [gi|18394440|ref|NP_564014|]
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ubiquitin-specific protease 15 [Arabidopsis thaliana]

Protein Classification

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

zf-MYND and Peptidase_C19E domain-containing protein

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 ...
 437-742 1.23e-168

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: 492.95  E-value: 1.23e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 437 PRGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWCLMCELEQHVMMLRESGGPLSASRIL-SHMRSINCQ 515
Cdd:cd02661   1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFsSNLKQISKH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 516 IGDGSQEDAHEFLRLLVASMQSICLERLGGETKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYG 595
Cdd:cd02661  81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 596 WvESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYGKINKCISFPEMLDMIPFMT 675
Cdd:cd02661 161 A-DSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMS 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18394440 676 RTGDVPPLYMLYAVIVHLDTLNasFSGHYISYVKDLRGNWYRIDDSEIHPVPMTQVMSEGAYMLFYM 742
Cdd:cd02661 240 QPNDGPLKYKLYAVLVHSGFSP--HSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
zf-MYND pfam01753
MYND finger;
130-167 8.17e-11

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 57.43  E-value: 8.17e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 18394440   130 CARCFGPAKT--RCSRCKSVRYCSGKCQIIHWRVaHKDEC 167
Cdd:pfam01753   1 CAVCGKEALKllRCSRCKSVYYCSKECQKADWPY-HKKEC 39
 
Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 437-742 1.23e-168

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: 492.95  E-value: 1.23e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 437 PRGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWCLMCELEQHVMMLRESGGPLSASRIL-SHMRSINCQ 515
Cdd:cd02661   1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFsSNLKQISKH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 516 IGDGSQEDAHEFLRLLVASMQSICLERLGGETKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYG 595
Cdd:cd02661  81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 596 WvESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYGKINKCISFPEMLDMIPFMT 675
Cdd:cd02661 161 A-DSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMS 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18394440 676 RTGDVPPLYMLYAVIVHLDTLNasFSGHYISYVKDLRGNWYRIDDSEIHPVPMTQVMSEGAYMLFYM 742
Cdd:cd02661 240 QPNDGPLKYKLYAVLVHSGFSP--HSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
438-741 2.63e-74

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 246.20  E-value: 2.63e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440   438 RGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWC--LMCELEQ--HVMMLRESGGPLSASRILSHMRSIN 513
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDlfKALQKNSKSSSVSPKMFKKSLGKLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440   514 CQIGDGSQEDAHEFLRLLVASMQSIClerlggetKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEI 593
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDL--------NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440   594 YG-----WVESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYG--KINKCISFPE 666
Cdd:pfam00443 153 PGdsaelKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTweKLNTEVEFPL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440   667 MLDMIPFMTRTGDVP----PLYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDSEIHPVPM-TQVMSEGAYMLF 740
Cdd:pfam00443 233 ELDLSRYLAEELKPKtnnlQDYRLVAVVVHSGSLS---SGHYIAYIKAYENNrWYKFDDEKVTEVDEeTAVLSSSAYILF 309


                  .
gi 18394440   741 Y 741
Cdd:pfam00443 310 Y 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 439-743 1.18e-29

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 127.29  E-value: 1.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440  439 GLVNCGNSCYANAVLQSLTCTKPL--VAYLLRRSHSRscsGKDWCLMCeLEQHVMMLRESGGPLSASRIlshMRSINCQI 516
Cdd:COG5077  195 GLRNQGATCYMNSLLQSLFFIAKFrkDVYGIPTDHPR---GRDSVALA-LQRLFYNLQTGEEPVDTTEL---TRSFGWDS 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440  517 GDG-SQEDAHEFLRLLVASmqsicLERLGGETKVDPRLQEttlvqhMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYG 595
Cdd:COG5077  268 DDSfMQHDIQEFNRVLQDN-----LEKSMRGTVVENALNG------IFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440  596 wVESLQDALTQFTRPEDLDGENMYRCSRcAGYVRARKELSIHEAPNILTIVLKRFQ----EGRYGKINKCISFPEMLDMI 671
Cdd:COG5077  337 -MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEydfeRDMMVKINDRYEFPLEIDLL 414

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440  672 PFMTRTGD----VPPLYMLYAVIVHLDTLNasfSGHYISYVK-DLRGNWYRIDDSEIHPVPMTQVMSE------------ 734
Cdd:COG5077  415 PFLDRDADksenSDAVYVLYGVLVHSGDLH---EGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdki 491

                        330
                 ....*....|....*....
gi 18394440  735 ----------GAYMLFYMR 743
Cdd:COG5077  492 rdhsgikrfmSAYMLVYLR 510
zf-MYND pfam01753
MYND finger;
130-167 8.17e-11

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 57.43  E-value: 8.17e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 18394440   130 CARCFGPAKT--RCSRCKSVRYCSGKCQIIHWRVaHKDEC 167
Cdd:pfam01753   1 CAVCGKEALKllRCSRCKSVYYCSKECQKADWPY-HKKEC 39
zf-HIT_ZNHIT1_like cd21437
HIT zinc finger found in zinc finger HIT domain-containing protein 1 (ZNHIT1) and similar ...
 128-158 1.54e-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: 37.21  E-value: 1.54e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 18394440 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 ...
 437-742 1.23e-168

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: 492.95  E-value: 1.23e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 437 PRGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWCLMCELEQHVMMLRESGGPLSASRIL-SHMRSINCQ 515
Cdd:cd02661   1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFsSNLKQISKH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 516 IGDGSQEDAHEFLRLLVASMQSICLERLGGETKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYG 595
Cdd:cd02661  81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 596 WvESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYGKINKCISFPEMLDMIPFMT 675
Cdd:cd02661 161 A-DSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMS 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18394440 676 RTGDVPPLYMLYAVIVHLDTLNasFSGHYISYVKDLRGNWYRIDDSEIHPVPMTQVMSEGAYMLFYM 742
Cdd:cd02661 240 QPNDGPLKYKLYAVLVHSGFSP--HSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
438-741 2.63e-74

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 246.20  E-value: 2.63e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440   438 RGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWC--LMCELEQ--HVMMLRESGGPLSASRILSHMRSIN 513
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDlfKALQKNSKSSSVSPKMFKKSLGKLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440   514 CQIGDGSQEDAHEFLRLLVASMQSIClerlggetKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEI 593
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDL--------NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440   594 YG-----WVESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYG--KINKCISFPE 666
Cdd:pfam00443 153 PGdsaelKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTweKLNTEVEFPL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440   667 MLDMIPFMTRTGDVP----PLYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDSEIHPVPM-TQVMSEGAYMLF 740
Cdd:pfam00443 233 ELDLSRYLAEELKPKtnnlQDYRLVAVVVHSGSLS---SGHYIAYIKAYENNrWYKFDDEKVTEVDEeTAVLSSSAYILF 309


                  .
gi 18394440   741 Y 741
Cdd:pfam00443 310 Y 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 439-742 1.15e-66

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: 223.51  E-value: 1.15e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 439 GLVNCGNSCYANAVLQSLTCtkplvayllrrshsrscsgkdwclmceleqhvmmlresggplsasrilshmrsincqigd 518
Cdd:cd02257   1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 519 gSQEDAHEFLRLLVASMQSICLERLGGEtkvDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEI---YG 595
Cdd:cd02257  21 -EQQDAHEFLLFLLDKLHEELKKSSKRT---SDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkGL 96

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 596 WVESLQDALTQFTRPEDLDGENMYRCSRCaGYVRARKELSIHEAPNILTIVLKRFQ---EGRYGKINKCISFPEMLDMIP 672
Cdd:cd02257  97 PQVSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSP 175

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 673 FMT------RTGDVPPLYMLYAVIVHLDTlnASFSGHYISYVKD-LRGNWYRIDDSEIHPVPMTQVMSEG-----AYMLF 740
Cdd:cd02257 176 YLSegekdsDSDNGSYKYELVAVVVHSGT--SADSGHYVAYVKDpSDGKWYKFNDDKVTEVSEEEVLEFGslsssAYILF 253


                ..
gi 18394440 741 YM 742
Cdd:cd02257 254 YE 255
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 438-741 4.68e-63

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: 216.08  E-value: 4.68e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 438 RGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDW--CLMCELEQ--HVMMLRESGGPLSASRILSHMRSIN 513
Cdd:cd02660   1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPnsCLSCAMDEifQEFYYSGDRSPYGPINLLYLSWKHS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 514 CQIGDGSQEDAHEFLRLLVASMQSICLERLGGETKVDPrlqeTTLVQHM-FGGRLRSKVKCLRCDHESERYENIMDLTLE 592
Cdd:cd02660  81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESH----CNCIIHQtFSGSLQSSVTCQRCGGVSTTVDPFLDLSLD 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 593 I-----YGWVES---------LQDALTQFTRPEDLdGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQ---EGRY 655
Cdd:cd02660 157 IpnkstPSWALGesgvsgtptLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEhslNKTS 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 656 GKINKCISFPEMLDMIPFMT----RTGDVPPL-----YMLYAVIVHLDTLNasfSGHYISYVKDLRGNWYRIDDSEIHPV 726
Cdd:cd02660 236 RKIDTYVQFPLELNMTPYTSssigDTQDSNSLdpdytYDLFAVVVHKGTLD---TGHYTAYCRQGDGQWFKFDDAMITRV 312

                       330
                ....*....|....*
gi 18394440 727 PMTQVMSEGAYMLFY 741
Cdd:cd02660 313 SEEEVLKSQAYLLFY 327
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 439-746 4.77e-57

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 199.79  E-value: 4.77e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLR---RSHSRSCSGKdwclMCELEQHVMMLRESGGPLSASRILSHMRSINCQ 515
Cdd:cd02659   4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSippTEDDDDNKSV----PLALQRLFLFLQLSESPVKTTELTDKTRSFGWD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 516 IGD-GSQEDAHEFLRLLVASMqsiclerlggETKVDPRLQETtLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIY 594
Cdd:cd02659  80 SLNtFEQHDVQEFFRVLFDKL----------EEKLKGTGQEG-LIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVK 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 595 GwVESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF----QEGRYGKINKCISFPEMLDM 670
Cdd:cd02659 149 G-KKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFefdfETMMRIKINDRFEFPLELDM 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 671 IPFMTRTGDVPP-----------LYMLYAVIVHLDTLNasfSGHYISYVKDLR-GNWYRIDDSEIHPVPMTQVMSE---- 734
Cdd:cd02659 228 EPYTEKGLAKKEgdsekkdsesyIYELHGVLVHSGDAH---GGHYYSYIKDRDdGKWYKFNDDVVTPFDPNDAEEEcfgg 304

                       330       340       350
                ....*....|....*....|....*....|
gi 18394440 735 ------------------GAYMLFYMRSYP 746
Cdd:cd02659 305 eetqktydsgprafkrttNAYMLFYERKSP 334
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 439-741 6.19e-55

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: 190.19  E-value: 6.19e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 439 GLVNCGNSCYANAVLQSLtctkplvayllrrshsrscsgkdwclmceleqhvmmlresggplsasrilSHMrsincqigd 518
Cdd:cd02674   1 GLRNLGNTCYMNSILQCL--------------------------------------------------SAD--------- 21

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 519 gsQEDAHEFLRLLVASMQSIclerlggetkvdprlqettlVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYGW-- 596
Cdd:cd02674  22 --QQDAQEFLLFLLDGLHSI--------------------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGsg 79

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 597 ---VESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF--QEGRYGKINKCISFP-EMLDM 670
Cdd:cd02674  80 dapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFsfSRGSTRKLTTPVTFPlNDLDL 159

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18394440 671 IPFMTRTGDVPP-LYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDSEIHPVPMTQVMSEGAYMLFY 741
Cdd:cd02674 160 TPYVDTRSFTGPfKYDLYAVVNHYGSLN---GGHYTAYCKNNETNdWYKFDDSRVTKVSESSVVSSSAYILFY 229
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 439-741 1.24e-53

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 188.36  E-value: 1.24e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRShsrscsgkdwclmceleqhVMMLREsggplsasrilshMRSINCQIGD 518
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETP-------------------KELFSQ-------------VCRKAPQFKG 48

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 519 GSQEDAHEFLRLLVASMQsiclerlggetkvdprlqetTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYGWVE 598
Cdd:cd02667  49 YQQQDSHELLRYLLDGLR--------------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK 108

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 599 ---SLQDALTQFTRPEDLDGENMYRCSRCagyVRARKELSIHEAPNILTIVLKRFQEGRYG---KINKCISFPEMLDMIP 672
Cdd:cd02667 109 secSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPRSAnlrKVSRHVSFPEILDLAP 185

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 673 FMTRTGDVP-----PLYMLYAVIVHLDTLNasfSGHYISYVKD----------------------LRGNWYRIDDSEIHP 725
Cdd:cd02667 186 FCDPKCNSSedkssVLYRLYGVVEHSGTMR---SGHYVAYVKVrppqqrlsdltkskpaadeagpGSGQWYYISDSDVRE 262

                       330
                ....*....|....*.
gi 18394440 726 VPMTQVMSEGAYMLFY 741
Cdd:cd02667 263 VSLEEVLKSEAYLLFY 278
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 439-741 1.85e-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: 1.85e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRScsGKDWCLMCELEQHVMML----RESGGP----LSASRILShmr 510
Cdd:cd02664   1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRL--GDSQSVMKKLQLLQAHLmhtqRRAEAPpdyfLEASRPPW--- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 511 sincqIGDGSQEDAHEFLRLLvasmqsicLERLggetkvdprlqeTTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLT 590
Cdd:cd02664  76 -----FTPGSQQDCSEYLRYL--------LDRL------------HTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLD 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 591 LEiygwVESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGR-YGK---------INK 660
Cdd:cd02664 131 LS----FPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQkTHVrekimdnvsINE 206

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 661 CISFP-----------EMLDMIPFMTRTG--DVPPLYMLYAVIVHLDTlnASFSGHYISYV------------------- 708
Cdd:cd02664 207 VLSLPvrveskssespLEKKEEESGDDGElvTRQVHYRLYAVVVHSGY--SSESGHYFTYArdqtdadstgqecpepkda 284

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 18394440 709 --KDLRGNWYRIDDSEIHPVPMTQVM-------SEGAYMLFY 741
Cdd:cd02664 285 eeNDESKNWYLFNDSRVTFSSFESVQnvtsrfpKDTPYILFY 326
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 439-741 5.99e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 147.07  E-value: 5.99e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 439 GLVNCGNSCYANAVLQSL------TCTKPLVayllrrsHSRSCSGKDWclmceleqhvmmlresgGPLSASRILSHMRSI 512
Cdd:cd02663   1 GLENFGNTCYCNSVLQALyfenllTCLKDLF-------ESISEQKKRT-----------------GVISPKKFITRLKRE 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 513 NcQIGDGS-QEDAHEFLRLLVASmqsiCLERLGGETKVDPRLQ----------ETTLVQHMFGGRLRSKVKCLRCDHESE 581
Cdd:cd02663  57 N-ELFDNYmHQDAHEFLNFLLNE----IAEILDAERKAEKANRklnnnnnaepQPTWVHEIFQGILTNETRCLTCETVSS 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 582 RYENIMDLTLEIYGWVeSLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF----QEGRYGK 657
Cdd:cd02663 132 RDETFLDLSIDVEQNT-SITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFkydeQLNRYIK 210

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 658 INKCISFPemLDMIPFMTRTGDVPP--LYMLYAVIVHLDtlNASFSGHYISYVKdLRGNWYRIDDSEIHPVPMTQVM--- 732
Cdd:cd02663 211 LFYRVVFP--LELRLFNTTDDAENPdrLYELVAVVVHIG--GGPNHGHYVSIVK-SHGGWLLFDDETVEKIDENAVEeff 285

                       330
                ....*....|....
gi 18394440 733 -----SEGAYMLFY 741
Cdd:cd02663 286 gdspnQATAYVLFY 299
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 439-741 4.38e-36

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: 139.48  E-value: 4.38e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 439 GLVNCGNSCYANAVLQSLTCTKPLvayllRRShsrscsgkdwCLMCELEQHVMMLR-ESGGPLSASRILSHMRSINCQ-- 515
Cdd:cd02668   1 GLKNLGATCYVNSFLQLWFMNLEF-----RKA----------VYECNSTEDAELKNmPPDKPHEPQTIIDQLQLIFAQlq 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 516 -----------------IGDGSQEDAHEFLRLLVASMQSiCLERLGgetkvDPRLQetTLVQHMFGGRLRSKVKCLRCDH 578
Cdd:cd02668  66 fgnrsvvdpsgfvkalgLDTGQQQDAQEFSKLFLSLLEA-KLSKSK-----NPDLK--NIVQDLFRGEYSYVTQCSKCGR 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 579 ESERYENIMDLTLEIYGwVESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF----QEGR 654
Cdd:cd02668 138 ESSLPSKFYELELQLKG-HKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFvfdrKTGA 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 655 YGKINKCISFPEMLDMIPFMTRTGDVPPLYMLYAVIVHLDtlNASFSGHYISYVKD-LRGNWYRIDDSEIHPVPMTQVM- 732
Cdd:cd02668 217 KKKLNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQG--VSAYSGHYIAHIKDeQTGEWYKFNDEDVEEMPGKPLKl 294

                       330       340
                ....*....|....*....|....*....
gi 18394440 733 --------------------SEGAYMLFY 741
Cdd:cd02668 295 gnsedpakprkseikkgthsSRTAYMLVY 323
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 439-743 1.18e-29

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 127.29  E-value: 1.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440  439 GLVNCGNSCYANAVLQSLTCTKPL--VAYLLRRSHSRscsGKDWCLMCeLEQHVMMLRESGGPLSASRIlshMRSINCQI 516
Cdd:COG5077  195 GLRNQGATCYMNSLLQSLFFIAKFrkDVYGIPTDHPR---GRDSVALA-LQRLFYNLQTGEEPVDTTEL---TRSFGWDS 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440  517 GDG-SQEDAHEFLRLLVASmqsicLERLGGETKVDPRLQEttlvqhMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYG 595
Cdd:COG5077  268 DDSfMQHDIQEFNRVLQDN-----LEKSMRGTVVENALNG------IFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440  596 wVESLQDALTQFTRPEDLDGENMYRCSRcAGYVRARKELSIHEAPNILTIVLKRFQ----EGRYGKINKCISFPEMLDMI 671
Cdd:COG5077  337 -MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEydfeRDMMVKINDRYEFPLEIDLL 414

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440  672 PFMTRTGD----VPPLYMLYAVIVHLDTLNasfSGHYISYVK-DLRGNWYRIDDSEIHPVPMTQVMSE------------ 734
Cdd:COG5077  415 PFLDRDADksenSDAVYVLYGVLVHSGDLH---EGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdki 491

                        330
                 ....*....|....*....
gi 18394440  735 ----------GAYMLFYMR 743
Cdd:COG5077  492 rdhsgikrfmSAYMLVYLR 510
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 439-741 2.95e-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: 119.61  E-value: 2.95e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 439 GLVNCGNSCYANAVLQSLtCTKPLVAYLLRRSHSRSCSGKDWCLMCEL--EQHVMMLRESggplSASRILSHMRSINCQI 516
Cdd:cd02671  26 GLNNLGNTCYLNSVLQVL-YFCPGFKHGLKHLVSLISSVEQLQSSFLLnpEKYNDELANQ----APRRLLNALREVNPMY 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 517 GDGSQEDAHEFLRLLVASMQSiclerlggetkvdprlqettLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTL----- 591
Cdd:cd02671 101 EGYLQHDAQEVLQCILGNIQE--------------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVpvqes 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 592 EIYGWVES-------------LQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQE------ 652
Cdd:cd02671 161 ELSKSEESseispdpktemktLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAAngsefd 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 653 --GRYGKINKCISFPemLDMIPFMTRTGDVPPLYMLYAVIVHLD-TLNasfSGHYISYVKdlrgnWYRIDDSEIHpvPMT 729
Cdd:cd02671 241 cyGGLSKVNTPLLTP--LKLSLEEWSTKPKNDVYRLFAVVMHSGaTIS---SGHYTAYVR-----WLLFDDSEVK--VTE 308

                       330       340
                ....*....|....*....|...
gi 18394440 730 QVMSEGA-----------YMLFY 741
Cdd:cd02671 309 EKDFLEAlspntsststpYLLFY 331
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 439-741 3.09e-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: 111.30  E-value: 3.09e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRrshsrscsgkdwclmcELEQHvmmlresggplsasrilshmrsincqigd 518
Cdd:cd02662   1 GLVNLGNTCFMNSVLQALASLPSLIEYLEE----------------FLEQQ----------------------------- 35

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 519 gsqeDAHEFLRLLVASMQSIClerlggetkvdprlqettlvQHMFGGRLRSKVKCLRCDHESE-RYENIMDLTL----EI 593
Cdd:cd02662  36 ----DAHELFQVLLETLEQLL--------------------KFPFDGLLASRIVCLQCGESSKvRYESFTMLSLpvpnQS 91

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 594 YGWVESLQDALTQFTRPEDLDGenmYRCSRCAgyvrarkeLSIHEAPNILTIVLKRFQEGRYGKI--NKC-ISFPEMLDm 670
Cdd:cd02662  92 SGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVFDGRGTStkNSCkVSFPERLP- 159

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 671 ipfmtrtgdvPPLYMLYAVIVHLDTLNasfSGHYISY---------------------VKDLRGNWYRIDDSEIHPVPMT 729
Cdd:cd02662 160 ----------KVLYRLRAVVVHYGSHS---SGHYVCYrrkplfskdkepgsfvrmregPSSTSHPWWRISDTTVKEVSES 226

                       330
                ....*....|...
gi 18394440 730 QVMSEG-AYMLFY 741
Cdd:cd02662 227 EVLEQKsAYMLFY 239
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
576-743 9.11e-21

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 98.42  E-value: 9.11e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 576 CDHESERYENIMDLTLEiygWVES----------LQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTI 645
Cdd:COG5560 646 CEWEEKRYLSLFSYDPL---WTIReigaaertitLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILII 722

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 646 VLKRFQEGRYG--KINKCISFP-EMLDMIPFMTRTGDVPPLYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDS 721
Cdd:COG5560 723 HLKRFSSVRSFrdKIDDLVEYPiDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLS---GGHYTAYARNFANNgWYLFDDS 799

                       170       180
                ....*....|....*....|..
gi 18394440 722 EIHPVPMTQVMSEGAYMLFYMR 743
Cdd:COG5560 800 RITEVDPEDSVTSSAYVLFYRR 821
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 439-741 5.65e-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: 91.62  E-value: 5.65e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLR--RSHSRSCSGKDWcLMCELEQHVMMLRESGGPLSASRILSHMRSINCQI 516
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNynPARRGANQSSDN-LTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 517 ------GDGSQEDAHEFLRLLVASMQSiCLERLGGETKVdprlqettlVQHMFGGRLRSKVKCLRCDHESE---RYENIM 587
Cdd:cd02657  80 aekqnqGGYAQQDAEECWSQLLSVLSQ-KLPGAGSKGSF---------IDQLFGIELETKMKCTESPDEEEvstESEYKL 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 588 DLTLEIYGWVESLQDALTQftRPEDLDGENMYRCSRCAGYVRARKelsIHEAPNILTIVLKRF----QEGRYGKINKCIS 663
Cdd:cd02657 150 QCHISITTEVNYLQDGLKK--GLEEEIEKHSPTLGRDAIYTKTSR---ISRLPKYLTVQFVRFfwkrDIQKKAKILRKVK 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 664 FPEMLDMIPFMTRTGdvppLYMLYAVIVHlDTLNASfSGHYISYVK-DLRGNWYRIDDSEIHPVPMTQV--MSEG----- 735
Cdd:cd02657 225 FPFELDLYELCTPSG----YYELVAVITH-QGRSAD-SGHYVAWVRrKNDGKWIKFDDDKVSEVTEEDIlkLSGGgdwhi 298


                ....*.
gi 18394440 736 AYMLFY 741
Cdd:cd02657 299 AYILLY 304
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 439-741 8.15e-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: 91.23  E-value: 8.15e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKD--WCLMCELEQ--HVMM----LRESGGPLSASRILSHMR 510
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDpaNDLNCQLIKlaDGLLsgrySKPASLKSENDPYQVGIK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 511 SI---NCqIGDGSQE-------DAHEFLRLLvasmqsicLERLGGETKVDPRLQETTLVQHMfggrLRSKVKCLRCDH-- 578
Cdd:cd02658  81 PSmfkAL-IGKGHPEfstmrqqDALEFLLHL--------IDKLDRESFKNLGLNPNDLFKFM----IEDRLECLSCKKvk 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 579 ESERYENIMDLTLE------------IYGWVEsLQDALTQFTRPEDLDgenmYRCSRCAGYVRARKELSIHEAPNILTIV 646
Cdd:cd02658 148 YTSELSEILSLPVPkdeatekeegelVYEPVP-LEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVIN 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 647 LKRFQEGRYG---KINKCISFPEMLDmipfmtrtgdvPPLYMLYAVIVHLDTlnASFSGHYISYVK---DLRGNWYRIDD 720
Cdd:cd02658 223 MKRFQLLENWvpkKLDVPIDVPEELG-----------PGKYELIAFISHKGT--SVHSGHYVAHIKkeiDGEGKWVLFND 289

                       330       340
                ....*....|....*....|.
gi 18394440 721 SEIHPVPMTQVMSEGAYMLFY 741
Cdd:cd02658 290 EKVVASQDPPEMKKLGYIYFY 310
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
439-720 5.57e-18

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 85.79  E-value: 5.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440   439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLrrSHSRSCSGKDWCLMCELeQHV--MMLRESGGPLSAS---RILSHMRSIN 513
Cdd:pfam13423   2 GLETHIPNSYTNSLLQLLRFIPPLRNLAL--SHLATECLKEHCLLCEL-GFLfdMLEKAKGKNCQASnflRALSSIPEAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440   514 cQIG---DGSQEDAHEFLRLLVASMQSICLERLGGETKV--DPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMD 588
Cdd:pfam13423  79 -ALGlldEDRETNSAISLSSLIQSFNRFLLDQLSSEENStpPNPSPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440   589 LTLeIYGWVESLQDALTQFTRPED-----LDGENMYR--CSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYGKINKC 661
Cdd:pfam13423 158 LDL-IYPRKPSSNNKKPPNQTFSSilkssLERETTTKawCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQLWKTP 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18394440   662 ISFPEMLDMIPFMTRTGDVPP-LYMLYAVIVHLDtlNASFSGHYISYVK--------DLRGNWYRIDD 720
Cdd:pfam13423 237 GWLPPEIGLTLSDDLQGDNEIvKYELRGVVVHIG--DSGTSGHLVSFVKvadseledPTESQWYLFND 302
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
439-743 8.53e-18

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 84.85  E-value: 8.53e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDwclMCELEQHVMMLRESGGPLSASRILSH--MRSINCQi 516
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKELKVLKN---VIRKPEPDLNQEEALKLFTALWSSKEhkVGWIPPM- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 517 gdGSQEDAHEFLRLLvasMQSICLERLG-GETKVDPRLQettlvqhmfggrlrskvkclrcDHESERYENIMDLTLE--I 593
Cdd:COG5533  77 --GSQEDAHELLGKL---LDELKLDLVNsFTIRIFKTTK----------------------DKKKTSTGDWFDIIIElpD 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 594 YGWVE---SLQDALTQFTRPEDLD-----GENMYRCSRCagyvRARKELSIHEAPNILTIVLKRF-QEGRYGKINKCISf 664
Cdd:COG5533 130 QTWVNnlkTLQEFIDNMEELVDDEtgvkaKENEELEVQA----KQEYEVSFVKLPKILTIQLKRFaNLGGNQKIDTEVD- 204

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 665 pEMLDMIPFMTRTGDVPP--LYMLYAVIVHLDTLNasfSGHYISYVKdLRGNWYRIDDSEIHPVPMTQ---VMSEGAYML 739
Cdd:COG5533 205 -EKFELPVKHDQILNIVKetYYDLVGFVLHQGSLE---GGHYIAYVK-KGGKWEKANDSDVTPVSEEEainEKAKNAYLY 279


                ....
gi 18394440 740 FYMR 743
Cdd:COG5533 280 FYER 283
zf-MYND pfam01753
MYND finger;
130-167 8.17e-11

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 57.43  E-value: 8.17e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 18394440   130 CARCFGPAKT--RCSRCKSVRYCSGKCQIIHWRVaHKDEC 167
Cdd:pfam01753   1 CAVCGKEALKllRCSRCKSVYYCSKECQKADWPY-HKKEC 39
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 440-741 7.68e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 60.24  E-value: 7.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 440 LVNCGNSCYANAVLQSLtctkplvayllrrshsrSCSGKdwclmceleqhvmmlresggplsasrilshmrsINCQIGDG 519
Cdd:cd02673   2 LVNTGNSCYFNSTMQAL-----------------SSIGK---------------------------------INTEFDND 31

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 520 SQEDAHEFLRLLVASMQSIcLERLGGETKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEI----YG 595
Cdd:cd02673  32 DQQDAHEFLLTLLEAIDDI-MQVNRTNVPPSNIEIKRLNPLEAFKYTIESSYVCIGCSFEENVSDVGNFLDVSMidnkLD 110

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394440 596 WVESLQDALTQFTRPEDldgenmyRCSRCAGYVRARKElSIHEAPNILTIVLKRFQE----GRYGKINKCIsfpemldMI 671
Cdd:cd02673 111 IDELLISNFKTWSPIEK-------DCSSCKCESAISSE-RIMTFPECLSINLKRYKLriatSDYLKKNEEI-------MK 175

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18394440 672 PFMTRtgdvPPLYMLYAVIVHL-DTLNAsfsGHYISYVKDLRGN--WYRIDDSEIHPVPMTQVMSE---GAYMLFY 741
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 1.54e-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: 37.21  E-value: 1.54e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 18394440 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.
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