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Conserved domains on  [gi|11993475|gb|AAG42756|]
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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 3.74e-162

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: 476.00  E-value: 3.74e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 437 PRGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWCLMCELEQHVMMLRESGGPLSASRIL-SHMRSINCQ 515
Cdd:cd02661   1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFsSNLKQISKH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 516 IGDGSQEDAHEFLRLLVASMPSICLERLGGETKVDPRLQETTLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEIYG 595
Cdd:cd02661  81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 596 WvEFFQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYGKINKCISFPEMLDMIPFMT 675
Cdd:cd02661 161 A-DSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMS 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11993475 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 11993475   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 3.74e-162

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: 476.00  E-value: 3.74e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 437 PRGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWCLMCELEQHVMMLRESGGPLSASRIL-SHMRSINCQ 515
Cdd:cd02661   1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFsSNLKQISKH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 516 IGDGSQEDAHEFLRLLVASMPSICLERLGGETKVDPRLQETTLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEIYG 595
Cdd:cd02661  81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 596 WvEFFQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYGKINKCISFPEMLDMIPFMT 675
Cdd:cd02661 161 A-DSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMS 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11993475 676 RTGDVPPLYMLYAVIVHLDTLNasFSGHYISYVKDLRGNWYRIDDSEIHPVPMTQVMSEGAYMLFYM 742
Cdd:cd02661 240 QPNDGPLKYKLYAVLVHSGFSP--HSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
438-741 5.88e-72

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 240.04  E-value: 5.88e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475   438 RGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWC--LMCELEQ--HVMMLRESGGPLSASRILSHMRSIN 513
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDlfKALQKNSKSSSVSPKMFKKSLGKLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475   514 CQIGDGSQEDAHEFLRLLvasmpsicLERLGGETKVDPRLQETTLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEI 593
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFL--------LDGLHEDLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475   594 YG-----WVEFFQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYG--KINKCISFPE 666
Cdd:pfam00443 153 PGdsaelKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTweKLNTEVEFPL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475   667 MLDMIPFMTRTGDVP----PLYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDSEIHPVPM-TQVMSEGAYMLF 740
Cdd:pfam00443 233 ELDLSRYLAEELKPKtnnlQDYRLVAVVVHSGSLS---SGHYIAYIKAYENNrWYKFDDEKVTEVDEeTAVLSSSAYILF 309


                  .
gi 11993475   741 Y 741
Cdd:pfam00443 310 Y 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 439-743 5.42e-28

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 121.90  E-value: 5.42e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475  439 GLVNCGNSCYANAVLQSLTCTKPL--VAYLLRRSHSRscsGKDWCLMCeLEQHVMMLRESGGPLSASRIlshMRSINCQI 516
Cdd:COG5077  195 GLRNQGATCYMNSLLQSLFFIAKFrkDVYGIPTDHPR---GRDSVALA-LQRLFYNLQTGEEPVDTTEL---TRSFGWDS 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475  517 GDG-SQEDAHEFLRLLVASmpsicLERLGGETKVDPRLQEttlvqhMFGGRLHSKVKCLRCDHESERYENIMDLTLEIYG 595
Cdd:COG5077  268 DDSfMQHDIQEFNRVLQDN-----LEKSMRGTVVENALNG------IFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475  596 wVEFFQDALIQFTRPEDLDGENMYRCSRcAGYVRARKELSIHEAPNILTIVLKRFQ----EGRYGKINKCISFPEMLDMI 671
Cdd:COG5077  337 -MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEydfeRDMMVKINDRYEFPLEIDLL 414

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475  672 PFMTRTGD----VPPLYMLYAVIVHLDTLNasfSGHYISYVK-DLRGNWYRIDDSEIHPVPMTQVMSE------------ 734
Cdd:COG5077  415 PFLDRDADksenSDAVYVLYGVLVHSGDLH---EGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdki 491

                        330
                 ....*....|....*....
gi 11993475  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 11993475   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 1.55e-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: 1.55e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 11993475 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 3.74e-162

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: 476.00  E-value: 3.74e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 437 PRGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWCLMCELEQHVMMLRESGGPLSASRIL-SHMRSINCQ 515
Cdd:cd02661   1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFsSNLKQISKH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 516 IGDGSQEDAHEFLRLLVASMPSICLERLGGETKVDPRLQETTLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEIYG 595
Cdd:cd02661  81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 596 WvEFFQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYGKINKCISFPEMLDMIPFMT 675
Cdd:cd02661 161 A-DSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMS 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11993475 676 RTGDVPPLYMLYAVIVHLDTLNasFSGHYISYVKDLRGNWYRIDDSEIHPVPMTQVMSEGAYMLFYM 742
Cdd:cd02661 240 QPNDGPLKYKLYAVLVHSGFSP--HSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
438-741 5.88e-72

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 240.04  E-value: 5.88e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475   438 RGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWC--LMCELEQ--HVMMLRESGGPLSASRILSHMRSIN 513
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDlfKALQKNSKSSSVSPKMFKKSLGKLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475   514 CQIGDGSQEDAHEFLRLLvasmpsicLERLGGETKVDPRLQETTLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEI 593
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFL--------LDGLHEDLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475   594 YG-----WVEFFQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYG--KINKCISFPE 666
Cdd:pfam00443 153 PGdsaelKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTweKLNTEVEFPL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475   667 MLDMIPFMTRTGDVP----PLYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDSEIHPVPM-TQVMSEGAYMLF 740
Cdd:pfam00443 233 ELDLSRYLAEELKPKtnnlQDYRLVAVVVHSGSLS---SGHYIAYIKAYENNrWYKFDDEKVTEVDEeTAVLSSSAYILF 309


                  .
gi 11993475   741 Y 741
Cdd:pfam00443 310 Y 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 439-742 4.86e-63

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: 213.50  E-value: 4.86e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCtkplvayllrrshsrscsgkdwclmceleqhvmmlresggplsasrilshmrsincqigd 518
Cdd:cd02257   1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 519 gSQEDAHEFLRLLVASMpsiCLERLGGETKVDPRLQETTLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEI---YG 595
Cdd:cd02257  21 -EQQDAHEFLLFLLDKL---HEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkGL 96

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 596 WVEFFQDALIQFTRPEDLDGENMYRCSRCaGYVRARKELSIHEAPNILTIVLKRFQ---EGRYGKINKCISFPEMLDMIP 672
Cdd:cd02257  97 PQVSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSP 175

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 673 FMT------RTGDVPPLYMLYAVIVHLDTlnASFSGHYISYVKD-LRGNWYRIDDSEIHPVPMTQVMSEG-----AYMLF 740
Cdd:cd02257 176 YLSegekdsDSDNGSYKYELVAVVVHSGT--SADSGHYVAYVKDpSDGKWYKFNDDKVTEVSEEEVLEFGslsssAYILF 253


                ..
gi 11993475 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 6.28e-61

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: 210.31  E-value: 6.28e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 438 RGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDW--CLMCELEQ--HVMMLRESGGPLSASRILSHMRSIN 513
Cdd:cd02660   1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPnsCLSCAMDEifQEFYYSGDRSPYGPINLLYLSWKHS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 514 CQIGDGSQEDAHEFLRLLVASMPSICLERLGGETKVDPrlqeTTLVQHM-FGGRLHSKVKCLRCDHESERYENIMDLTLE 592
Cdd:cd02660  81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESH----CNCIIHQtFSGSLQSSVTCQRCGGVSTTVDPFLDLSLD 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 593 IYGWVEFF--------------QDALIQFTRPEDLdGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQ---EGRY 655
Cdd:cd02660 157 IPNKSTPSwalgesgvsgtptlSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEhslNKTS 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 656 GKINKCISFPEMLDMIPFMT----RTGDVPPL-----YMLYAVIVHLDTLNasfSGHYISYVKDLRGNWYRIDDSEIHPV 726
Cdd:cd02660 236 RKIDTYVQFPLELNMTPYTSssigDTQDSNSLdpdytYDLFAVVVHKGTLD---TGHYTAYCRQGDGQWFKFDDAMITRV 312

                       330
                ....*....|....*
gi 11993475 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 3.64e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 191.70  E-value: 3.64e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLR---RSHSRSCSGKdwclMCELEQHVMMLRESGGPLSASRILSHMRSINCQ 515
Cdd:cd02659   4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSippTEDDDDNKSV----PLALQRLFLFLQLSESPVKTTELTDKTRSFGWD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 516 IGD-GSQEDAHEFLRLLVASMpsiclerlggETKVDPRLQETtLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEIY 594
Cdd:cd02659  80 SLNtFEQHDVQEFFRVLFDKL----------EEKLKGTGQEG-LIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVK 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 595 GWVEFfQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF----QEGRYGKINKCISFPEMLDM 670
Cdd:cd02659 149 GKKNL-EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFefdfETMMRIKINDRFEFPLELDM 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 671 IPFMTRTGDVPP-----------LYMLYAVIVHLDTLNasfSGHYISYVKDLR-GNWYRIDDSEIHPVPMTQVMSE---- 734
Cdd:cd02659 228 EPYTEKGLAKKEgdsekkdsesyIYELHGVLVHSGDAH---GGHYYSYIKDRDdGKWYKFNDDVVTPFDPNDAEEEcfgg 304

                       330       340       350
                ....*....|....*....|....*....|
gi 11993475 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 2.80e-52

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 182.49  E-value: 2.80e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLtctkplvayllrrshsrscsgkdwclmceleqhvmmlresggplsasrilSHMrsincqigd 518
Cdd:cd02674   1 GLRNLGNTCYMNSILQCL--------------------------------------------------SAD--------- 21

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 519 gsQEDAHEFLRLLVASMPSIclerlggetkvdprlqettlVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEIYGWVE 598
Cdd:cd02674  22 --QQDAQEFLLFLLDGLHSI--------------------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSG 79

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 599 FF-----QDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF--QEGRYGKINKCISFP-EMLDM 670
Cdd:cd02674  80 DApkvtlEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFsfSRGSTRKLTTPVTFPlNDLDL 159

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 11993475 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 1.98e-51

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: 181.82  E-value: 1.98e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRShsrscsgkdwclmceleqhVMMLREsggplsasrilshMRSINCQIGD 518
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETP-------------------KELFSQ-------------VCRKAPQFKG 48

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 519 GSQEDAHEFLRLLVASMpsiclerlggetkvdprlqeTTLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEIYGWVE 598
Cdd:cd02667  49 YQQQDSHELLRYLLDGL--------------------RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK 108

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 599 ---FFQDALIQFTRPEDLDGENMYRCSRCagyVRARKELSIHEAPNILTIVLKRFQEGRYG---KINKCISFPEMLDMIP 672
Cdd:cd02667 109 secSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPRSAnlrKVSRHVSFPEILDLAP 185

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 673 FMTRTGDVP-----PLYMLYAVIVHLDTLNasfSGHYISYVKD----------------------LRGNWYRIDDSEIHP 725
Cdd:cd02667 186 FCDPKCNSSedkssVLYRLYGVVEHSGTMR---SGHYVAYVKVrppqqrlsdltkskpaadeagpGSGQWYYISDSDVRE 262

                       330
                ....*....|....*.
gi 11993475 726 VPMTQVMSEGAYMLFY 741
Cdd:cd02667 263 VSLEEVLKSEAYLLFY 278
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 439-741 4.94e-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: 141.29  E-value: 4.94e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSL------TCTKPLVayllrrsHSRSCSGKDWclmceleqhvmmlresgGPLSASRILSHMRSI 512
Cdd:cd02663   1 GLENFGNTCYCNSVLQALyfenllTCLKDLF-------ESISEQKKRT-----------------GVISPKKFITRLKRE 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 513 NcQIGDGS-QEDAHEFLRLLVASmpsiCLERLGGETKVDPRLQ----------ETTLVQHMFGGRLHSKVKCLRCDHESE 581
Cdd:cd02663  57 N-ELFDNYmHQDAHEFLNFLLNE----IAEILDAERKAEKANRklnnnnnaepQPTWVHEIFQGILTNETRCLTCETVSS 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 582 RYENIMDLTLEIYGWVEFfQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF----QEGRYGK 657
Cdd:cd02663 132 RDETFLDLSIDVEQNTSI-TSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFkydeQLNRYIK 210

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 658 INKCISFPemLDMIPFMTRTGDVPP--LYMLYAVIVHLDtlNASFSGHYISYVKdLRGNWYRIDDSEIHPVPMTQVM--- 732
Cdd:cd02663 211 LFYRVVFP--LELRLFNTTDDAENPdrLYELVAVVVHIG--GGPNHGHYVSIVK-SHGGWLLFDDETVEKIDENAVEeff 285

                       330
                ....*....|....
gi 11993475 733 -----SEGAYMLFY 741
Cdd:cd02663 286 gdspnQATAYVLFY 299
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 439-741 1.08e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 141.09  E-value: 1.08e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRScsGKDWCLMCELEQHVMML----RESGGP----LSASRILShmr 510
Cdd:cd02664   1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRL--GDSQSVMKKLQLLQAHLmhtqRRAEAPpdyfLEASRPPW--- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 511 sincqIGDGSQEDAHEFLRLLvasmpsicLERLggetkvdprlqeTTLVQHMFGGRLHSKVKCLRCDHESERYENIMDLT 590
Cdd:cd02664  76 -----FTPGSQQDCSEYLRYL--------LDRL------------HTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLD 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 591 LEiygwVEFFQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGR-YGK---------INK 660
Cdd:cd02664 131 LS----FPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQkTHVrekimdnvsINE 206

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 661 CISFP-----------EMLDMIPFMTRTG--DVPPLYMLYAVIVHLDTlnASFSGHYISYV------------------- 708
Cdd:cd02664 207 VLSLPvrveskssespLEKKEEESGDDGElvTRQVHYRLYAVVVHSGY--SSESGHYFTYArdqtdadstgqecpepkda 284

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 11993475 709 --KDLRGNWYRIDDSEIHPVPMTQVM-------SEGAYMLFY 741
Cdd:cd02664 285 eeNDESKNWYLFNDSRVTFSSFESVQnvtsrfpKDTPYILFY 326
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 439-741 6.19e-33

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 130.23  E-value: 6.19e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPLvayllRRShsrscsgkdwCLMCELEQHVMMLR-ESGGPLSASRILSHMRSINCQ-- 515
Cdd:cd02668   1 GLKNLGATCYVNSFLQLWFMNLEF-----RKA----------VYECNSTEDAELKNmPPDKPHEPQTIIDQLQLIFAQlq 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 516 -----------------IGDGSQEDAHEFLRLLVASMPSiCLERLGgetkvDPRLQetTLVQHMFGGRLHSKVKCLRCDH 578
Cdd:cd02668  66 fgnrsvvdpsgfvkalgLDTGQQQDAQEFSKLFLSLLEA-KLSKSK-----NPDLK--NIVQDLFRGEYSYVTQCSKCGR 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 579 ESERYENIMDLTLEIYGwVEFFQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF----QEGR 654
Cdd:cd02668 138 ESSLPSKFYELELQLKG-HKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFvfdrKTGA 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 655 YGKINKCISFPEMLDMIPFMTRTGDVPPLYMLYAVIVHLDtlNASFSGHYISYVKD-LRGNWYRIDDSEIHPVPMTQVM- 732
Cdd:cd02668 217 KKKLNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQG--VSAYSGHYIAHIKDeQTGEWYKFNDEDVEEMPGKPLKl 294

                       330       340
                ....*....|....*....|....*....
gi 11993475 733 --------------------SEGAYMLFY 741
Cdd:cd02668 295 gnsedpakprkseikkgthsSRTAYMLVY 323
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 439-743 5.42e-28

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 121.90  E-value: 5.42e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475  439 GLVNCGNSCYANAVLQSLTCTKPL--VAYLLRRSHSRscsGKDWCLMCeLEQHVMMLRESGGPLSASRIlshMRSINCQI 516
Cdd:COG5077  195 GLRNQGATCYMNSLLQSLFFIAKFrkDVYGIPTDHPR---GRDSVALA-LQRLFYNLQTGEEPVDTTEL---TRSFGWDS 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475  517 GDG-SQEDAHEFLRLLVASmpsicLERLGGETKVDPRLQEttlvqhMFGGRLHSKVKCLRCDHESERYENIMDLTLEIYG 595
Cdd:COG5077  268 DDSfMQHDIQEFNRVLQDN-----LEKSMRGTVVENALNG------IFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475  596 wVEFFQDALIQFTRPEDLDGENMYRCSRcAGYVRARKELSIHEAPNILTIVLKRFQ----EGRYGKINKCISFPEMLDMI 671
Cdd:COG5077  337 -MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEydfeRDMMVKINDRYEFPLEIDLL 414

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475  672 PFMTRTGD----VPPLYMLYAVIVHLDTLNasfSGHYISYVK-DLRGNWYRIDDSEIHPVPMTQVMSE------------ 734
Cdd:COG5077  415 PFLDRDADksenSDAVYVLYGVLVHSGDLH---EGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdki 491

                        330
                 ....*....|....*....
gi 11993475  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 1.19e-26

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: 111.91  E-value: 1.19e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLtCTKPLVAYLLRRSHSRSCSGKDWCLMCEL--EQHVMMLRESggplSASRILSHMRSINCQI 516
Cdd:cd02671  26 GLNNLGNTCYLNSVLQVL-YFCPGFKHGLKHLVSLISSVEQLQSSFLLnpEKYNDELANQ----APRRLLNALREVNPMY 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 517 GDGSQEDAHEFLRLLVASmpsiclerlggetkvdprLQEttLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTL----- 591
Cdd:cd02671 101 EGYLQHDAQEVLQCILGN------------------IQE--LVEKDFQGQLVLRTRCLECETFTERREDFQDISVpvqes 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 592 ---------EIYGWVEF----FQDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQE------ 652
Cdd:cd02671 161 elskseessEISPDPKTemktLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAAngsefd 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 653 --GRYGKINKCISFPemLDMIPFMTRTGDVPPLYMLYAVIVHLD-TLNasfSGHYISYVKdlrgnWYRIDDSEIHpvPMT 729
Cdd:cd02671 241 cyGGLSKVNTPLLTP--LKLSLEEWSTKPKNDVYRLFAVVMHSGaTIS---SGHYTAYVR-----WLLFDDSEVK--VTE 308

                       330       340
                ....*....|....*....|...
gi 11993475 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 2.38e-25

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: 105.53  E-value: 2.38e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRrshsrscsgkdwclmcELEQHvmmlresggplsasrilshmrsincqigd 518
Cdd:cd02662   1 GLVNLGNTCFMNSVLQALASLPSLIEYLEE----------------FLEQQ----------------------------- 35

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 519 gsqeDAHEFLRLLVAsmpsiCLERlggetkvdprlqettLVQHMFGGRLHSKVKCLRCDHESE-RYENIMDLTL----EI 593
Cdd:cd02662  36 ----DAHELFQVLLE-----TLEQ---------------LLKFPFDGLLASRIVCLQCGESSKvRYESFTMLSLpvpnQS 91

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 594 YGWVEFFQDALIQFTRPEDLDGenmYRCSRCAgyvrarkeLSIHEAPNILTIVLKRFQEGRYGKI--NKC-ISFPEMLDm 670
Cdd:cd02662  92 SGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVFDGRGTStkNSCkVSFPERLP- 159

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 671 ipfmtrtgdvPPLYMLYAVIVHLDTLNasfSGHYISY---------------------VKDLRGNWYRIDDSEIHPVPMT 729
Cdd:cd02662 160 ----------KVLYRLRAVVVHYGSHS---SGHYVCYrrkplfskdkepgsfvrmregPSSTSHPWWRISDTTVKEVSES 226

                       330
                ....*....|...
gi 11993475 730 QVMSEG-AYMLFY 741
Cdd:cd02662 227 EVLEQKsAYMLFY 239
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
601-743 8.89e-20

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 94.95  E-value: 8.89e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 601 QDALIQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYG--KINKCISFP-EMLDMIPFMTRT 677
Cdd:COG5560 678 QDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFrdKIDDLVEYPiDDLDLSGVEYMV 757

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11993475 678 GDVPPLYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDSEIHPVPMTQVMSEGAYMLFYMR 743
Cdd:COG5560 758 DDPRLIYDLYAVDNHYGGLS---GGHYTAYARNFANNgWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 439-741 2.90e-19

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: 89.69  E-value: 2.90e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKD--WCLMCELEQ--HVMM----LRESGGPLSASRILSHMR 510
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDpaNDLNCQLIKlaDGLLsgrySKPASLKSENDPYQVGIK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 511 SI---NCqIGDGSQE-------DAHEFLRLLvasmpsicLERLGGETKVDPRLQETTLVQHMFGGRLhskvKCLRCDH-- 578
Cdd:cd02658  81 PSmfkAL-IGKGHPEfstmrqqDALEFLLHL--------IDKLDRESFKNLGLNPNDLFKFMIEDRL----ECLSCKKvk 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 579 ESERYENIMDLTLE------------IYGWVEfFQDALIQFTRPEDLDgenmYRCSRCAGYVRARKELSIHEAPNILTIV 646
Cdd:cd02658 148 YTSELSEILSLPVPkdeatekeegelVYEPVP-LEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVIN 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 647 LKRFQEGRYG---KINKCISFPEMLDmipfmtrtgdvPPLYMLYAVIVHLDTlnASFSGHYISYVK---DLRGNWYRIDD 720
Cdd:cd02658 223 MKRFQLLENWvpkKLDVPIDVPEELG-----------PGKYELIAFISHKGT--SVHSGHYVAHIKkeiDGEGKWVLFND 289

                       330       340
                ....*....|....*....|.
gi 11993475 721 SEIHPVPMTQVMSEGAYMLFY 741
Cdd:cd02658 290 EKVVASQDPPEMKKLGYIYFY 310
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 439-741 1.06e-18

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: 87.77  E-value: 1.06e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLR--RSHSRSCSGKDWcLMCELEQHVMMLRESGGPLSASRILSHMRSINCQI 516
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNynPARRGANQSSDN-LTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 517 ------GDGSQEDAHEFLRLLVaSMPSICLERLGGETKVdprlqettlVQHMFGGRLHSKVKCLRCDHESE---RYENIM 587
Cdd:cd02657  80 aekqnqGGYAQQDAEECWSQLL-SVLSQKLPGAGSKGSF---------IDQLFGIELETKMKCTESPDEEEvstESEYKL 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 588 DLTLEIYGWVEFFQDALIQftRPEDLDGENMYRCSRCAGYVRARKelsIHEAPNILTIVLKRF----QEGRYGKINKCIS 663
Cdd:cd02657 150 QCHISITTEVNYLQDGLKK--GLEEEIEKHSPTLGRDAIYTKTSR---ISRLPKYLTVQFVRFfwkrDIQKKAKILRKVK 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 664 FPEMLDMIPFMTRTGdvppLYMLYAVIVHlDTLNASfSGHYISYVK-DLRGNWYRIDDSEIHPVPMTQV--MSEG----- 735
Cdd:cd02657 225 FPFELDLYELCTPSG----YYELVAVITH-QGRSAD-SGHYVAWVRrKNDGKWIKFDDDKVSEVTEEDIlkLSGGgdwhi 298


                ....*.
gi 11993475 736 AYMLFY 741
Cdd:cd02657 299 AYILLY 304
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
439-743 6.03e-17

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 82.16  E-value: 6.03e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDwclMCELEQHVMMLRESGGPLSASRILSH--MRSINCQi 516
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKELKVLKN---VIRKPEPDLNQEEALKLFTALWSSKEhkVGWIPPM- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 517 gdGSQEDAHEFLRLLvasmpsiclerlggetkvdprLQETTLVQHMFGGRLHSKVKClrcDHESERYENIMDLTLE--IY 594
Cdd:COG5533  77 --GSQEDAHELLGKL---------------------LDELKLDLVNSFTIRIFKTTK---DKKKTSTGDWFDIIIElpDQ 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 595 GWVEF---FQDALIQFTRPEDLD-----GENMYRCSRCagyvRARKELSIHEAPNILTIVLKRF-QEGRYGKINKCISfp 665
Cdd:COG5533 131 TWVNNlktLQEFIDNMEELVDDEtgvkaKENEELEVQA----KQEYEVSFVKLPKILTIQLKRFaNLGGNQKIDTEVD-- 204

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 666 EMLDMIPFMTRTGDVPP--LYMLYAVIVHLDTLNasfSGHYISYVKdLRGNWYRIDDSEIHPVPMTQ---VMSEGAYMLF 740
Cdd:COG5533 205 EKFELPVKHDQILNIVKetYYDLVGFVLHQGSLE---GGHYIAYVK-KGGKWEKANDSDVTPVSEEEainEKAKNAYLYF 280


                ...
gi 11993475 741 YMR 743
Cdd:COG5533 281 YER 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 11993475   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 1.96e-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: 56.00  E-value: 1.96e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 440 LVNCGNSCYANAVLQSLtctkplvayllrrshsrSCSGKdwclmceleqhvmmlresggplsasrilshmrsINCQIGDG 519
Cdd:cd02673   2 LVNTGNSCYFNSTMQAL-----------------SSIGK---------------------------------INTEFDND 31

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 520 SQEDAHEFLRLLVASMPSIcLERLGGETKVDPRLQETTLVQHMFGGRLHSKVKCLRCDHESERYENIMDLTLEI----YG 595
Cdd:cd02673  32 DQQDAHEFLLTLLEAIDDI-MQVNRTNVPPSNIEIKRLNPLEAFKYTIESSYVCIGCSFEENVSDVGNFLDVSMidnkLD 110

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 596 WVEFFQDALIQFTRPEDldgenmyRCSRCAGYVRARKElSIHEAPNILTIVLKRFQE----GRYGKINKCIsfpemldMI 671
Cdd:cd02673 111 IDELLISNFKTWSPIEK-------DCSSCKCESAISSE-RIMTFPECLSINLKRYKLriatSDYLKKNEEI-------MK 175

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11993475 672 PFMTRtgdvPPLYMLYAVIVHL-DTLNAsfsGHYISYVKDLRGN--WYRIDDSEIHPVPMTQVMSE---GAYMLFY 741
Cdd:cd02673 176 KYCGT----DAKYSLVAVICHLgESPYD---GHYIAYTKELYNGssWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
439-593 2.58e-04

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 44.87  E-value: 2.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 439 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCS--------GKDWCLMCELEQHVMMLRESGgpLSASRILSHMR 510
Cdd:COG5560 267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINeenplgmhGSVASAYADLIKQLYDGNLHA--FTPSGFKKTIG 344

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11993475 511 SINCQIGDGSQEDAHEFLRLLVASM---------------PSIC------LERLGGETKVDPRLQETTLVQHMFGGRLHS 569
Cdd:COG5560 345 SFNEEFSGYDQQDSQEFIAFLLDGLhedlnriikkpytskPDLSpgddvvVKKKAKECWWEHLKRNDSIITDLFQGMYKS 424

                       170       180
                ....*....|....*....|....
gi 11993475 570 KVKCLRCDHESERYENIMDLTLEI 593
Cdd:COG5560 425 TLTCPGCGSVSITFDPFMDLTLPL 448
zf-HIT_ZNHIT1_like cd21437
HIT zinc finger found in zinc finger HIT domain-containing protein 1 (ZNHIT1) and similar ...
 128-158 1.55e-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: 1.55e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 11993475 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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