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Conserved domains on  [gi|1190947513|ref|XP_020867098|]
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ubiquitin carboxyl-terminal hydrolase 15 isoform X1 [Arabidopsis lyrata subsp. lyrata]

Protein Classification

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

zf-MYND and Peptidase_C19E domain-containing protein

Graphical summary

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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 ...
 445-750 2.43e-167

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


:

Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 489.48  E-value: 2.43e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 445 PRGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWCLMCELEQHVMMLRESGGPLSASRIL-SHMRSINCQ 523
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFsSNLKQISKH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 524 IGDGSQEDAHEFLRLLVASMQSICLERLGGETKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYG 603
Cdd:cd02661    81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 604 WvESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYGKINKCISFPEMLDMIPFMT 683
Cdd:cd02661   161 A-DSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1190947513 684 RTGDVPPLYMLYAVIVHLDTLNasFSGHYISYVKDLRGNWYRIDDSEIHRVPMTQVMSEGAYMLFYM 750
Cdd:cd02661   240 QPNDGPLKYKLYAVLVHSGFSP--HSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
zf-MYND pfam01753
MYND finger;
130-167 1.54e-10

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 56.66  E-value: 1.54e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1190947513 130 CARCFGPAKT--RCSRCKSVRYCSGKCQIIHWrIAHKDEC 167
Cdd:pfam01753   1 CAVCGKEALKllRCSRCKSVYYCSKECQKADW-PYHKKEC 39
 
Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 445-750 2.43e-167

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 489.48  E-value: 2.43e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 445 PRGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWCLMCELEQHVMMLRESGGPLSASRIL-SHMRSINCQ 523
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFsSNLKQISKH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 524 IGDGSQEDAHEFLRLLVASMQSICLERLGGETKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYG 603
Cdd:cd02661    81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 604 WvESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYGKINKCISFPEMLDMIPFMT 683
Cdd:cd02661   161 A-DSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1190947513 684 RTGDVPPLYMLYAVIVHLDTLNasFSGHYISYVKDLRGNWYRIDDSEIHRVPMTQVMSEGAYMLFYM 750
Cdd:cd02661   240 QPNDGPLKYKLYAVLVHSGFSP--HSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
446-749 1.57e-73

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 244.27  E-value: 1.57e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 446 RGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWC--LMCELEQ--HVMMLRESGGPLSASRILSHMRSIN 521
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDlfKALQKNSKSSSVSPKMFKKSLGKLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 522 CQIGDGSQEDAHEFLRLLVASMQSIClerlggetKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEI 601
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDL--------NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 602 YG-----WVESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYG--KINKCISFPE 674
Cdd:pfam00443 153 PGdsaelKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTweKLNTEVEFPL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 675 MLDMIPFMTRTGDVP----PLYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDSEIHRVPM-TQVMSEGAYMLF 748
Cdd:pfam00443 233 ELDLSRYLAEELKPKtnnlQDYRLVAVVVHSGSLS---SGHYIAYIKAYENNrWYKFDDEKVTEVDEeTAVLSSSAYILF 309


                  .
gi 1190947513 749 Y 749
Cdd:pfam00443 310 Y 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 447-751 1.64e-30

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 129.99  E-value: 1.64e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513  447 GLVNCGNSCYANAVLQSLTCTKPL--VAYLLRRSHSRscsGKDWCLMCeLEQHVMMLRESGGPLSASRIlshMRSINCQI 524
Cdd:COG5077    195 GLRNQGATCYMNSLLQSLFFIAKFrkDVYGIPTDHPR---GRDSVALA-LQRLFYNLQTGEEPVDTTEL---TRSFGWDS 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513  525 GDG-SQEDAHEFLRLLVASmqsicLERLGGETKVDPRLQEttlvqhMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYG 603
Cdd:COG5077    268 DDSfMQHDIQEFNRVLQDN-----LEKSMRGTVVENALNG------IFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513  604 wVESLQDALTQFTRPEDLDGENMYRCSRcAGYVRARKELSIHEAPNILTIVLKRFQ----EGRYGKINKCISFPEMLDMI 679
Cdd:COG5077    337 -MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEydfeRDMMVKINDRYEFPLEIDLL 414

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513  680 PFMTRTGD----VPPLYMLYAVIVHLDTLNasfSGHYISYVK-DLRGNWYRIDDSEIHRVPMTQVMSE------------ 742
Cdd:COG5077    415 PFLDRDADksenSDAVYVLYGVLVHSGDLH---EGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdki 491

                          330
                   ....*....|....*....
gi 1190947513  743 ----------GAYMLFYMR 751
Cdd:COG5077    492 rdhsgikrfmSAYMLVYLR 510
zf-MYND pfam01753
MYND finger;
130-167 1.54e-10

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 56.66  E-value: 1.54e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1190947513 130 CARCFGPAKT--RCSRCKSVRYCSGKCQIIHWrIAHKDEC 167
Cdd:pfam01753   1 CAVCGKEALKllRCSRCKSVYYCSKECQKADW-PYHKKEC 39
zf-HIT_ZNHIT1_like cd21437
HIT zinc finger found in zinc finger HIT domain-containing protein 1 (ZNHIT1) and similar ...
 128-158 1.96e-03

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


Pssm-ID: 467791  Cd Length: 43  Bit Score: 36.83  E-value: 1.96e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1190947513 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 ...
 445-750 2.43e-167

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 489.48  E-value: 2.43e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 445 PRGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWCLMCELEQHVMMLRESGGPLSASRIL-SHMRSINCQ 523
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFsSNLKQISKH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 524 IGDGSQEDAHEFLRLLVASMQSICLERLGGETKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYG 603
Cdd:cd02661    81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 604 WvESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYGKINKCISFPEMLDMIPFMT 683
Cdd:cd02661   161 A-DSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1190947513 684 RTGDVPPLYMLYAVIVHLDTLNasFSGHYISYVKDLRGNWYRIDDSEIHRVPMTQVMSEGAYMLFYM 750
Cdd:cd02661   240 QPNDGPLKYKLYAVLVHSGFSP--HSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
446-749 1.57e-73

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 244.27  E-value: 1.57e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 446 RGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDWC--LMCELEQ--HVMMLRESGGPLSASRILSHMRSIN 521
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDlfKALQKNSKSSSVSPKMFKKSLGKLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 522 CQIGDGSQEDAHEFLRLLVASMQSIClerlggetKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEI 601
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDL--------NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 602 YG-----WVESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYG--KINKCISFPE 674
Cdd:pfam00443 153 PGdsaelKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTweKLNTEVEFPL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 675 MLDMIPFMTRTGDVP----PLYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDSEIHRVPM-TQVMSEGAYMLF 748
Cdd:pfam00443 233 ELDLSRYLAEELKPKtnnlQDYRLVAVVVHSGSLS---SGHYIAYIKAYENNrWYKFDDEKVTEVDEeTAVLSSSAYILF 309


                  .
gi 1190947513 749 Y 749
Cdd:pfam00443 310 Y 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 447-750 1.86e-65

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


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 220.43  E-value: 1.86e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 447 GLVNCGNSCYANAVLQSLTCtkplvayllrrshsrscsgkdwclmceleqhvmmlresggplsasrilshmrsincqigd 526
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 527 gSQEDAHEFLRLLVASMQSICLERLGGEtkvDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEI---YG 603
Cdd:cd02257    21 -EQQDAHEFLLFLLDKLHEELKKSSKRT---SDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkGL 96

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 604 WVESLQDALTQFTRPEDLDGENMYRCSRCaGYVRARKELSIHEAPNILTIVLKRFQ---EGRYGKINKCISFPEMLDMIP 680
Cdd:cd02257    97 PQVSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSP 175

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 681 FMT------RTGDVPPLYMLYAVIVHLDTlnASFSGHYISYVKD-LRGNWYRIDDSEIHRVPMTQVMSEG-----AYMLF 748
Cdd:cd02257   176 YLSegekdsDSDNGSYKYELVAVVVHSGT--SADSGHYVAYVKDpSDGKWYKFNDDKVTEVSEEEVLEFGslsssAYILF 253


                  ..
gi 1190947513 749 YM 750
Cdd:cd02257   254 YE 255
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 446-749 1.67e-62

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 214.93  E-value: 1.67e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 446 RGLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDW--CLMCELEQ--HVMMLRESGGPLSASRILSHMRSIN 521
Cdd:cd02660     1 RGLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPnsCLSCAMDEifQEFYYSGDRSPYGPINLLYLSWKHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 522 CQIGDGSQEDAHEFLRLLVASMQSICLERLGGETKVDPrlqeTTLVQHM-FGGRLRSKVKCLRCDHESERYENIMDLTLE 600
Cdd:cd02660    81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESH----CNCIIHQtFSGSLQSSVTCQRCGGVSTTVDPFLDLSLD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 601 I-----YGWVES---------LQDALTQFTRPEDLdGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQ---EGRY 663
Cdd:cd02660   157 IpnkstPSWALGesgvsgtptLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEhslNKTS 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 664 GKINKCISFPEMLDMIPFMT----RTGDVPPL-----YMLYAVIVHLDTLNasfSGHYISYVKDLRGNWYRIDDSEIHRV 734
Cdd:cd02660   236 RKIDTYVQFPLELNMTPYTSssigDTQDSNSLdpdytYDLFAVVVHKGTLD---TGHYTAYCRQGDGQWFKFDDAMITRV 312

                         330
                  ....*....|....*
gi 1190947513 735 PMTQVMSEGAYMLFY 749
Cdd:cd02660   313 SEEEVLKSQAYLLFY 327
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 447-754 2.55e-56

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 197.86  E-value: 2.55e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 447 GLVNCGNSCYANAVLQSLTCTKPLVAYLLR---RSHSRSCSGKdwclMCELEQHVMMLRESGGPLSASRILSHMRSINCQ 523
Cdd:cd02659     4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSippTEDDDDNKSV----PLALQRLFLFLQLSESPVKTTELTDKTRSFGWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 524 IGD-GSQEDAHEFLRLLVASMqsiclerlggETKVDPRLQETtLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIY 602
Cdd:cd02659    80 SLNtFEQHDVQEFFRVLFDKL----------EEKLKGTGQEG-LIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVK 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 603 GwVESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF----QEGRYGKINKCISFPEMLDM 678
Cdd:cd02659   149 G-KKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFefdfETMMRIKINDRFEFPLELDM 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 679 IPFMTRTGDVPP-----------LYMLYAVIVHLDTLNasfSGHYISYVKDLR-GNWYRIDDSEIHRVPMTQVMSE---- 742
Cdd:cd02659   228 EPYTEKGLAKKEgdsekkdsesyIYELHGVLVHSGDAH---GGHYYSYIKDRDdGKWYKFNDDVVTPFDPNDAEEEcfgg 304

                         330       340       350
                  ....*....|....*....|....*....|
gi 1190947513 743 ------------------GAYMLFYMRSYP 754
Cdd:cd02659   305 eetqktydsgprafkrttNAYMLFYERKSP 334
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 447-749 1.73e-54

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 189.04  E-value: 1.73e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 447 GLVNCGNSCYANAVLQSLtctkplvayllrrshsrscsgkdwclmceleqhvmmlresggplsasrilSHMrsincqigd 526
Cdd:cd02674     1 GLRNLGNTCYMNSILQCL--------------------------------------------------SAD--------- 21

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 527 gsQEDAHEFLRLLVASMQSIclerlggetkvdprlqettlVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYGW-- 604
Cdd:cd02674    22 --QQDAQEFLLFLLDGLHSI--------------------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGsg 79

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 605 ---VESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF--QEGRYGKINKCISFP-EMLDM 678
Cdd:cd02674    80 dapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFsfSRGSTRKLTTPVTFPlNDLDL 159

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1190947513 679 IPFMTRTGDVPP-LYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDSEIHRVPMTQVMSEGAYMLFY 749
Cdd:cd02674   160 TPYVDTRSFTGPfKYDLYAVVNHYGSLN---GGHYTAYCKNNETNdWYKFDDSRVTKVSESSVVSSSAYILFY 229
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 447-749 2.56e-52

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 184.51  E-value: 2.56e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 447 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRShsrscsgkdwclmceleqhVMMLREsggplsasrilshMRSINCQIGD 526
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETP-------------------KELFSQ-------------VCRKAPQFKG 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 527 GSQEDAHEFLRLLVASMQsiclerlggetkvdprlqetTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYGWVE 606
Cdd:cd02667    49 YQQQDSHELLRYLLDGLR--------------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 607 ---SLQDALTQFTRPEDLDGENMYRCSRCagyVRARKELSIHEAPNILTIVLKRFQEGRYG---KINKCISFPEMLDMIP 680
Cdd:cd02667   109 secSIESCLKQFTEVEILEGNNKFACENC---TKAKKQYLISKLPPVLVIHLKRFQQPRSAnlrKVSRHVSFPEILDLAP 185

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 681 FMTRTGDVP-----PLYMLYAVIVHLDTLNasfSGHYISYVKD----------------------LRGNWYRIDDSEIHR 733
Cdd:cd02667   186 FCDPKCNSSedkssVLYRLYGVVEHSGTMR---SGHYVAYVKVrppqqrlsdltkskpaadeagpGSGQWYYISDSDVRE 262

                         330
                  ....*....|....*.
gi 1190947513 734 VPMTQVMSEGAYMLFY 749
Cdd:cd02667   263 VSLEEVLKSEAYLLFY 278
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 447-749 2.09e-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: 2.09e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 447 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRScsGKDWCLMCELEQHVMML----RESGGP----LSASRILShmr 518
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRL--GDSQSVMKKLQLLQAHLmhtqRRAEAPpdyfLEASRPPW--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 519 sincqIGDGSQEDAHEFLRLLvasmqsicLERLggetkvdprlqeTTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLT 598
Cdd:cd02664    76 -----FTPGSQQDCSEYLRYL--------LDRL------------HTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLD 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 599 LEiygwVESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQEGR-YGK---------INK 668
Cdd:cd02664   131 LS----FPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQkTHVrekimdnvsINE 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 669 CISFP-----------EMLDMIPFMTRTG--DVPPLYMLYAVIVHLDTlnASFSGHYISYV------------------- 716
Cdd:cd02664   207 VLSLPvrveskssespLEKKEEESGDDGElvTRQVHYRLYAVVVHSGY--SSESGHYFTYArdqtdadstgqecpepkda 284

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1190947513 717 --KDLRGNWYRIDDSeihRVPMTQVMS----------EGAYMLFY 749
Cdd:cd02664   285 eeNDESKNWYLFNDS---RVTFSSFESvqnvtsrfpkDTPYILFY 326
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 447-749 1.01e-37

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 143.60  E-value: 1.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 447 GLVNCGNSCYANAVLQSL------TCTKPLVayllrrsHSRSCSGKDWclmceleqhvmmlresgGPLSASRILSHMRSI 520
Cdd:cd02663     1 GLENFGNTCYCNSVLQALyfenllTCLKDLF-------ESISEQKKRT-----------------GVISPKKFITRLKRE 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 521 NcQIGDGS-QEDAHEFLRLLVASmqsiCLERLGGETKVDPRLQ----------ETTLVQHMFGGRLRSKVKCLRCDHESE 589
Cdd:cd02663    57 N-ELFDNYmHQDAHEFLNFLLNE----IAEILDAERKAEKANRklnnnnnaepQPTWVHEIFQGILTNETRCLTCETVSS 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 590 RYENIMDLTLEIYGWVeSLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF----QEGRYGK 665
Cdd:cd02663   132 RDETFLDLSIDVEQNT-SITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFkydeQLNRYIK 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 666 INKCISFPemLDMIPFMTRTGDVPP--LYMLYAVIVHLDtlNASFSGHYISYVKdLRGNWYRIDDSEIHRVPMTQVM--- 740
Cdd:cd02663   211 LFYRVVFP--LELRLFNTTDDAENPdrLYELVAVVVHIG--GGPNHGHYVSIVK-SHGGWLLFDDETVEKIDENAVEeff 285

                         330
                  ....*....|....
gi 1190947513 741 -----SEGAYMLFY 749
Cdd:cd02663   286 gdspnQATAYVLFY 299
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 447-749 4.38e-35

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 136.40  E-value: 4.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 447 GLVNCGNSCYANAVLQSLTCTKPLvayllRRShsrscsgkdwCLMCELEQHVMMLR-ESGGPLSASRILSHMRSINCQ-- 523
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEF-----RKA----------VYECNSTEDAELKNmPPDKPHEPQTIIDQLQLIFAQlq 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 524 -----------------IGDGSQEDAHEFLRLLVASMQSiCLERLGgetkvDPRLQetTLVQHMFGGRLRSKVKCLRCDH 586
Cdd:cd02668    66 fgnrsvvdpsgfvkalgLDTGQQQDAQEFSKLFLSLLEA-KLSKSK-----NPDLK--NIVQDLFRGEYSYVTQCSKCGR 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 587 ESERYENIMDLTLEIYGwVESLQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRF----QEGR 662
Cdd:cd02668   138 ESSLPSKFYELELQLKG-HKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFvfdrKTGA 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 663 YGKINKCISFPEMLDMIPFMTRTGDVPPLYMLYAVIVHLDtlNASFSGHYISYVKD-LRGNWYRIDDSEIHRVPMTQVM- 740
Cdd:cd02668   217 KKKLNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQG--VSAYSGHYIAHIKDeQTGEWYKFNDEDVEEMPGKPLKl 294

                         330       340
                  ....*....|....*....|....*....
gi 1190947513 741 --------------------SEGAYMLFY 749
Cdd:cd02668   295 gnsedpakprkseikkgthsSRTAYMLVY 323
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 447-751 1.64e-30

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 129.99  E-value: 1.64e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513  447 GLVNCGNSCYANAVLQSLTCTKPL--VAYLLRRSHSRscsGKDWCLMCeLEQHVMMLRESGGPLSASRIlshMRSINCQI 524
Cdd:COG5077    195 GLRNQGATCYMNSLLQSLFFIAKFrkDVYGIPTDHPR---GRDSVALA-LQRLFYNLQTGEEPVDTTEL---TRSFGWDS 267

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513  525 GDG-SQEDAHEFLRLLVASmqsicLERLGGETKVDPRLQEttlvqhMFGGRLRSKVKCLRCDHESERYENIMDLTLEIYG 603
Cdd:COG5077    268 DDSfMQHDIQEFNRVLQDN-----LEKSMRGTVVENALNG------IFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513  604 wVESLQDALTQFTRPEDLDGENMYRCSRcAGYVRARKELSIHEAPNILTIVLKRFQ----EGRYGKINKCISFPEMLDMI 679
Cdd:COG5077    337 -MKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFEydfeRDMMVKINDRYEFPLEIDLL 414

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513  680 PFMTRTGD----VPPLYMLYAVIVHLDTLNasfSGHYISYVK-DLRGNWYRIDDSEIHRVPMTQVMSE------------ 742
Cdd:COG5077    415 PFLDRDADksenSDAVYVLYGVLVHSGDLH---EGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdki 491

                          330
                   ....*....|....*....
gi 1190947513  743 ----------GAYMLFYMR 751
Cdd:COG5077    492 rdhsgikrfmSAYMLVYLR 510
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 447-749 5.29e-29

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 118.84  E-value: 5.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 447 GLVNCGNSCYANAVLQSLtCTKPLVAYLLRRSHSRSCSGKDWCLMCEL--EQHVMMLRESggplSASRILSHMRSINCQI 524
Cdd:cd02671    26 GLNNLGNTCYLNSVLQVL-YFCPGFKHGLKHLVSLISSVEQLQSSFLLnpEKYNDELANQ----APRRLLNALREVNPMY 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 525 GDGSQEDAHEFLRLLVASMQSiclerlggetkvdprlqettLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTL----- 599
Cdd:cd02671   101 EGYLQHDAQEVLQCILGNIQE--------------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVpvqes 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 600 EIYGWVES-------------LQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTIVLKRFQE------ 660
Cdd:cd02671   161 ELSKSEESseispdpktemktLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAAngsefd 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 661 --GRYGKINKCISFPemLDMIPFMTRTGDVPPLYMLYAVIVHLD-TLNasfSGHYISYVKdlrgnWYRIDDSEIhRVpMT 737
Cdd:cd02671   241 cyGGLSKVNTPLLTP--LKLSLEEWSTKPKNDVYRLFAVVMHSGaTIS---SGHYTAYVR-----WLLFDDSEV-KV-TE 308

                         330       340
                  ....*....|....*....|...
gi 1190947513 738 QVMSEGA-----------YMLFY 749
Cdd:cd02671   309 EKDFLEAlspntsststpYLLFY 331
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 447-749 1.53e-27

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 112.07  E-value: 1.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 447 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRrshsrscsgkdwclmcELEQHvmmlresggplsasrilshmrsincqigd 526
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLIEYLEE----------------FLEQQ----------------------------- 35

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 527 gsqeDAHEFLRLLVASMQSIClerlggetkvdprlqettlvQHMFGGRLRSKVKCLRCDHESE-RYENIMDLTL----EI 601
Cdd:cd02662    36 ----DAHELFQVLLETLEQLL--------------------KFPFDGLLASRIVCLQCGESSKvRYESFTMLSLpvpnQS 91

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 602 YGWVESLQDALTQFTRPEDLDGenmYRCSRCAgyvrarkeLSIHEAPNILTIVLKRFQEGRYGKI--NKC-ISFPEMLDm 678
Cdd:cd02662    92 SGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVFDGRGTStkNSCkVSFPERLP- 159

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 679 ipfmtrtgdvPPLYMLYAVIVHLDTLNasfSGHYISY---------------------VKDLRGNWYRIDDSEIHRVPMT 737
Cdd:cd02662   160 ----------KVLYRLRAVVVHYGSHS---SGHYVCYrrkplfskdkepgsfvrmregPSSTSHPWWRISDTTVKEVSES 226

                         330
                  ....*....|...
gi 1190947513 738 QVMSEG-AYMLFY 749
Cdd:cd02662   227 EVLEQKsAYMLFY 239
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
584-751 1.44e-20

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 97.65  E-value: 1.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 584 CDHESERYENIMDLTLEiygWVES----------LQDALTQFTRPEDLDGENMYRCSRCAGYVRARKELSIHEAPNILTI 653
Cdd:COG5560   646 CEWEEKRYLSLFSYDPL---WTIReigaaertitLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILII 722

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 654 VLKRFQEGRYG--KINKCISFP-EMLDMIPFMTRTGDVPPLYMLYAVIVHLDTLNasfSGHYISYVKDLRGN-WYRIDDS 729
Cdd:COG5560   723 HLKRFSSVRSFrdKIDDLVEYPiDDLDLSGVEYMVDDPRLIYDLYAVDNHYGGLS---GGHYTAYARNFANNgWYLFDDS 799

                         170       180
                  ....*....|....*....|..
gi 1190947513 730 EIHRVPMTQVMSEGAYMLFYMR 751
Cdd:COG5560   800 RITEVDPEDSVTSSAYVLFYRR 821
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 447-749 2.02e-20

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


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 93.16  E-value: 2.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 447 GLVNCGNSCYANAVLQSLTCTKPLVAYLLR--RSHSRSCSGKDWcLMCELEQHVMMLRESGGPLSASRILSHMRSINCQI 524
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNynPARRGANQSSDN-LTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 525 ------GDGSQEDAHEFLRLLVASMQSiCLERLGGETKVdprlqettlVQHMFGGRLRSKVKCLRCDHESE---RYENIM 595
Cdd:cd02657    80 aekqnqGGYAQQDAEECWSQLLSVLSQ-KLPGAGSKGSF---------IDQLFGIELETKMKCTESPDEEEvstESEYKL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 596 DLTLEIYGWVESLQDALTQftRPEDLDGENMYRCSRCAGYVRARKelsIHEAPNILTIVLKRF----QEGRYGKINKCIS 671
Cdd:cd02657   150 QCHISITTEVNYLQDGLKK--GLEEEIEKHSPTLGRDAIYTKTSR---ISRLPKYLTVQFVRFfwkrDIQKKAKILRKVK 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 672 FPEMLDMIPFMTRTGdvppLYMLYAVIVHlDTLNASfSGHYISYVK-DLRGNWYRIDDSEIHRVPMTQV--MSEG----- 743
Cdd:cd02657   225 FPFELDLYELCTPSG----YYELVAVITH-QGRSAD-SGHYVAWVRrKNDGKWIKFDDDKVSEVTEEDIlkLSGGgdwhi 298


                  ....*.
gi 1190947513 744 AYMLFY 749
Cdd:cd02657   299 AYILLY 304
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 447-749 4.92e-20

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 92.00  E-value: 4.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 447 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKD--WCLMCELEQ--HVMM----LRESGGPLSASRILSHMR 518
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDpaNDLNCQLIKlaDGLLsgrySKPASLKSENDPYQVGIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 519 SI---NCqIGDGSQE-------DAHEFLRLLvasmqsicLERLGGETKVDPRLQETTLVQHMfggrLRSKVKCLRCDH-- 586
Cdd:cd02658    81 PSmfkAL-IGKGHPEfstmrqqDALEFLLHL--------IDKLDRESFKNLGLNPNDLFKFM----IEDRLECLSCKKvk 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 587 ESERYENIMDLTLE------------IYGWVEsLQDALTQFTRPEDLDgenmYRCSRCAGYVRARKELSIHEAPNILTIV 654
Cdd:cd02658   148 YTSELSEILSLPVPkdeatekeegelVYEPVP-LEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVIN 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 655 LKRFQEGRYG---KINKCISFPEMLDmipfmtrtgdvPPLYMLYAVIVHLDTlnASFSGHYISYVK---DLRGNWYRIDD 728
Cdd:cd02658   223 MKRFQLLENWvpkKLDVPIDVPEELG-----------PGKYELIAFISHKGT--SVHSGHYVAHIKkeiDGEGKWVLFND 289

                         330       340
                  ....*....|....*....|.
gi 1190947513 729 SEIHRVPMTQVMSEGAYMLFY 749
Cdd:cd02658   290 EKVVASQDPPEMKKLGYIYFY 310
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
447-728 1.23e-17

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 84.63  E-value: 1.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 447 GLVNCGNSCYANAVLQSLTCTKPLVAYLLrrSHSRSCSGKDWCLMCELeQHV--MMLRESGGPLSAS---RILSHMRSIN 521
Cdd:pfam13423   2 GLETHIPNSYTNSLLQLLRFIPPLRNLAL--SHLATECLKEHCLLCEL-GFLfdMLEKAKGKNCQASnflRALSSIPEAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 522 cQIG---DGSQEDAHEFLRLLVASMQSICLERLGGETKV--DPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMD 596
Cdd:pfam13423  79 -ALGlldEDRETNSAISLSSLIQSFNRFLLDQLSSEENStpPNPSPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 597 LTLeIYGWVESLQDALTQFTRPED-----LDGENMYR--CSRCAGYVRARKELSIHEAPNILTIVLKRFQEGRYGKINKC 669
Cdd:pfam13423 158 LDL-IYPRKPSSNNKKPPNQTFSSilkssLERETTTKawCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQLWKTP 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1190947513 670 ISFPEMLDMIPFMTRTGDVPP-LYMLYAVIVHLDtlNASFSGHYISYVK--------DLRGNWYRIDD 728
Cdd:pfam13423 237 GWLPPEIGLTLSDDLQGDNEIvKYELRGVVVHIG--DSGTSGHLVSFVKvadseledPTESQWYLFND 302
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
447-751 1.15e-16

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 81.39  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 447 GLVNCGNSCYANAVLQSLTCTKPLVAYLLRRSHSRSCSGKDwclMCELEQHVMMLRESGGPLSASRILSH--MRSINCQi 524
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILALYLPKLDELLDDLSKELKVLKN---VIRKPEPDLNQEEALKLFTALWSSKEhkVGWIPPM- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 525 gdGSQEDAHEFLRLLvasMQSICLERLG-GETKVDPRLQettlvqhmfggrlrskvkclrcDHESERYENIMDLTLE--I 601
Cdd:COG5533    77 --GSQEDAHELLGKL---LDELKLDLVNsFTIRIFKTTK----------------------DKKKTSTGDWFDIIIElpD 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 602 YGWVE---SLQDALTQFTRPEDLD-----GENMYRCSRCagyvRARKELSIHEAPNILTIVLKRF-QEGRYGKINKCISf 672
Cdd:COG5533   130 QTWVNnlkTLQEFIDNMEELVDDEtgvkaKENEELEVQA----KQEYEVSFVKLPKILTIQLKRFaNLGGNQKIDTEVD- 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 673 pEMLDMIPFMTRTGDVPP--LYMLYAVIVHLDTLNasfSGHYISYVKdLRGNWYRIDDSEIHRVPMTQ---VMSEGAYML 747
Cdd:COG5533   205 -EKFELPVKHDQILNIVKetYYDLVGFVLHQGSLE---GGHYIAYVK-KGGKWEKANDSDVTPVSEEEainEKAKNAYLY 279


                  ....
gi 1190947513 748 FYMR 751
Cdd:COG5533   280 FYER 283
zf-MYND pfam01753
MYND finger;
130-167 1.54e-10

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 56.66  E-value: 1.54e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1190947513 130 CARCFGPAKT--RCSRCKSVRYCSGKCQIIHWrIAHKDEC 167
Cdd:pfam01753   1 CAVCGKEALKllRCSRCKSVYYCSKECQKADW-PYHKKEC 39
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 448-749 1.77e-08

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


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 56.38  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 448 LVNCGNSCYANAVLQSLtctkplvayllrrshsrSCSGKdwclmceleqhvmmlresggplsasrilshmrsINCQIGDG 527
Cdd:cd02673     2 LVNTGNSCYFNSTMQAL-----------------SSIGK---------------------------------INTEFDND 31

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 528 SQEDAHEFLRLLVASMQSIcLERLGGETKVDPRLQETTLVQHMFGGRLRSKVKCLRCDHESERYENIMDLTLEI----YG 603
Cdd:cd02673    32 DQQDAHEFLLTLLEAIDDI-MQVNRTNVPPSNIEIKRLNPLEAFKYTIESSYVCIGCSFEENVSDVGNFLDVSMidnkLD 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190947513 604 WVESLQDALTQFTRPEDldgenmyRCSRCAGYVRARKElSIHEAPNILTIVLKRFQE----GRYGKINKCIsfpemldMI 679
Cdd:cd02673   111 IDELLISNFKTWSPIEK-------DCSSCKCESAISSE-RIMTFPECLSINLKRYKLriatSDYLKKNEEI-------MK 175

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1190947513 680 PFMTRtgdvPPLYMLYAVIVHL-DTLNAsfsGHYISYVKDLRGN--WYRIDDSEIHRVPMTQVMSE---GAYMLFY 749
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 1.96e-03

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


Pssm-ID: 467791  Cd Length: 43  Bit Score: 36.83  E-value: 1.96e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1190947513 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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