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Conserved domains on  [gi|6322264|ref|NP_012338|]
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putative ubiquitin-specific protease UBP12 [Saccharomyces cerevisiae S288C]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 11475638)

ubiquitin carboxyl-terminal hydrolase is a C19 family peptidase that deubiquitinates polyubiquitinated target proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
99-1111 0e+00

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


:

Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 1068.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264    99 LEQQRDVVArliEENKETQKEGDKVCIVPKVWYDKFFDPDVTDPEDIGPINTRMICR-DFENFVLEDYNRCPYLSIAEPV 177
Cdd:COG5560   26 LMMQEELID---EKPAESSKQCEYAVIFAYAWYEGMFDRASCDGGSPGPIVQGPIVDfEPESLKKSLREGIDYSIISGAV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   178 FNFLSEIYGMTSGSYPVVTNLVINQTTGEleTEYNKWFFRLHYLTEkQDGRKRRHGQDdsIMYLSMSALNLVRDLVEKSM 257
Cdd:COG5560  103 WQLLVRWYGLAGLITPRITVLLPSESAPE--VESYPVVFKLHWLFS-INGSLINLGHD--PVPHSASSHGTLRDLSERVM 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   258 NLFFEKADhldvnavDFKIWFVSEGSDIATDSNVSTFLNSSYEITPLQFLELPIKKLLIPDMFENRLDKITSNPSDLVIE 337
Cdd:COG5560  178 NAFVDPSD-------DFRLWDVVPEIMGLRLGLDSFFRRYRVLASDGRVLHPLTRLELFEDRSVLLLSKITRNPDWLVDS 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   338 ikpiegnHHWPSNYFAYNKLepasGTTGLVNLGNTCYMNSALQCLVHIPQLRDYFLYDGYEDEINEENPLGYHGYVARAF 417
Cdd:COG5560  251 -------IVDDHNRSINKEA----GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAY 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   418 SDLVQKLFqnrmsiMQRNAAFPPSMFKSTIGHFNSMFSGYMQQDSQEFLAFLLDSLHEDLNRIIKKEYTEKPSLSPGDDV 497
Cdd:COG5560  320 ADLIKQLY------DGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDV 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   498 ndwnVVKKLADDTWEMHLKRNCSVITDLFVGMYKSTLYCPECQNVSITFDPYNDVTLPLPVDTVWDKTIKIFPMNSPPLL 577
Cdd:COG5560  394 ----VVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRRQP 469
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   578 LEVELSKSSTYMDLKNYVGKMSGLDPNTlfgcEIFSNQIYVNYESTESNAQFLTLQELIKPADDVIFYElpvTNDNEVIV 657
Cdd:COG5560  470 LKIELDASSTIRGLKKLVDAEYGKLGCF----EIKVMCIYYGGNYNMLEPADKVLLQDIPQTDFVYLYE---TNDNGIEV 542
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   658 PVLNTRIEKGYKNAMLFGVPFFiTLKedeLNNPGAIRMKLQNrfvhlsggyipfpepvgnrtdfadafpllvekypdvEF 737
Cdd:COG5560  543 PVVHLRIEKGYKSKRLFGDPFL-QLN---VLIKASIYDKLVK------------------------------------EF 582
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   738 EQYkdiLQYTSIKVTDKDKSFFSIKIlsvekeqqfaSNNRTGPNFWtpisqlnLDKATDIDDKLEDvvkdiynysslvdc 817
Cdd:COG5560  583 EEL---LVLVEMKKTDVDLVSEQVRL----------LREESSPSSW-------LKLETEIDTKREE-------------- 628
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   818 aegvlmQVDDEgdtegsEAKNFskpfqsgddeenketvtnnenvnntndrdedmeltddveedastepeltdkPEALdki 897
Cdd:COG5560  629 ------QVEEE------GQMNF---------------------------------------------------NDAV--- 642
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   898 kdsltstpfailsmndIIVCEWSELGSNEAFSddkiynweNPATLPNKELENAklersnakERTITLDDCLQLFSKPEIL 977
Cdd:COG5560  643 ----------------VISCEWEEKRYLSLFS--------YDPLWTIREIGAA--------ERTITLQDCLNEFSKPEQL 690
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   978 GLTDSWYCPTCKEHRQATKQIQLWNTPDILLIHLKRFESQRSFSDKIDATVNFPITDLDLSRYVVYKDDPRgLIYDLYAV 1057
Cdd:COG5560  691 GLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPR-LIYDLYAV 769
                        970       980       990      1000      1010
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6322264  1058 DNHYGGLGGGHYTAYVKNFADNKWYYFDDSRVTETAPENSIAGSAYLLFYIRRH 1111
Cdd:COG5560  770 DNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
99-1111 0e+00

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 1068.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264    99 LEQQRDVVArliEENKETQKEGDKVCIVPKVWYDKFFDPDVTDPEDIGPINTRMICR-DFENFVLEDYNRCPYLSIAEPV 177
Cdd:COG5560   26 LMMQEELID---EKPAESSKQCEYAVIFAYAWYEGMFDRASCDGGSPGPIVQGPIVDfEPESLKKSLREGIDYSIISGAV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   178 FNFLSEIYGMTSGSYPVVTNLVINQTTGEleTEYNKWFFRLHYLTEkQDGRKRRHGQDdsIMYLSMSALNLVRDLVEKSM 257
Cdd:COG5560  103 WQLLVRWYGLAGLITPRITVLLPSESAPE--VESYPVVFKLHWLFS-INGSLINLGHD--PVPHSASSHGTLRDLSERVM 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   258 NLFFEKADhldvnavDFKIWFVSEGSDIATDSNVSTFLNSSYEITPLQFLELPIKKLLIPDMFENRLDKITSNPSDLVIE 337
Cdd:COG5560  178 NAFVDPSD-------DFRLWDVVPEIMGLRLGLDSFFRRYRVLASDGRVLHPLTRLELFEDRSVLLLSKITRNPDWLVDS 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   338 ikpiegnHHWPSNYFAYNKLepasGTTGLVNLGNTCYMNSALQCLVHIPQLRDYFLYDGYEDEINEENPLGYHGYVARAF 417
Cdd:COG5560  251 -------IVDDHNRSINKEA----GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAY 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   418 SDLVQKLFqnrmsiMQRNAAFPPSMFKSTIGHFNSMFSGYMQQDSQEFLAFLLDSLHEDLNRIIKKEYTEKPSLSPGDDV 497
Cdd:COG5560  320 ADLIKQLY------DGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDV 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   498 ndwnVVKKLADDTWEMHLKRNCSVITDLFVGMYKSTLYCPECQNVSITFDPYNDVTLPLPVDTVWDKTIKIFPMNSPPLL 577
Cdd:COG5560  394 ----VVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRRQP 469
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   578 LEVELSKSSTYMDLKNYVGKMSGLDPNTlfgcEIFSNQIYVNYESTESNAQFLTLQELIKPADDVIFYElpvTNDNEVIV 657
Cdd:COG5560  470 LKIELDASSTIRGLKKLVDAEYGKLGCF----EIKVMCIYYGGNYNMLEPADKVLLQDIPQTDFVYLYE---TNDNGIEV 542
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   658 PVLNTRIEKGYKNAMLFGVPFFiTLKedeLNNPGAIRMKLQNrfvhlsggyipfpepvgnrtdfadafpllvekypdvEF 737
Cdd:COG5560  543 PVVHLRIEKGYKSKRLFGDPFL-QLN---VLIKASIYDKLVK------------------------------------EF 582
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   738 EQYkdiLQYTSIKVTDKDKSFFSIKIlsvekeqqfaSNNRTGPNFWtpisqlnLDKATDIDDKLEDvvkdiynysslvdc 817
Cdd:COG5560  583 EEL---LVLVEMKKTDVDLVSEQVRL----------LREESSPSSW-------LKLETEIDTKREE-------------- 628
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   818 aegvlmQVDDEgdtegsEAKNFskpfqsgddeenketvtnnenvnntndrdedmeltddveedastepeltdkPEALdki 897
Cdd:COG5560  629 ------QVEEE------GQMNF---------------------------------------------------NDAV--- 642
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   898 kdsltstpfailsmndIIVCEWSELGSNEAFSddkiynweNPATLPNKELENAklersnakERTITLDDCLQLFSKPEIL 977
Cdd:COG5560  643 ----------------VISCEWEEKRYLSLFS--------YDPLWTIREIGAA--------ERTITLQDCLNEFSKPEQL 690
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   978 GLTDSWYCPTCKEHRQATKQIQLWNTPDILLIHLKRFESQRSFSDKIDATVNFPITDLDLSRYVVYKDDPRgLIYDLYAV 1057
Cdd:COG5560  691 GLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPR-LIYDLYAV 769
                        970       980       990      1000      1010
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6322264  1058 DNHYGGLGGGHYTAYVKNFADNKWYYFDDSRVTETAPENSIAGSAYLLFYIRRH 1111
Cdd:COG5560  770 DNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
364-580 1.71e-52

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 186.88  E-value: 1.71e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264     364 TGLVNLGNTCYMNSALQCLVHIPQLRDYFLYDGYEDEINEENPlgyHGYVARAFSDLVQKLFQNrmsimQRNAAFPPSMF 443
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK---DINLLCALRDLFKALQKN-----SKSSSVSPKMF 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264     444 KSTIGHFNSMFSGYMQQDSQEFLAFLLDSLHEDLNRiikkeytekpslspgddvndwnvvkkladdtweMHLKRNCSVIT 523
Cdd:pfam00443   73 KKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG---------------------------------NHSTENESLIT 119
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6322264     524 DLFVGMYKSTLYCPECQNVSITFDPYNDVTLPLPVDTVWDKTIKIFPMNSPPLLLEV 580
Cdd:pfam00443  120 DLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQICFLQFSKLEE 176
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
962-1108 3.83e-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: 182.87  E-value: 3.83e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   962 ITLDDCLQLFSKPEILGLTDSWYCPTCKEHRQATKQIQLWNTPDILLIHLKRFESQRSFSDKIDATVNFPITDLDLSRYV 1041
Cdd:cd02674   84 VTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYV 163
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322264  1042 VYKDDPRGLIYDLYAVDNHYGGLGGGHYTAYVKNFADNKWYYFDDSRVTETAPENSIAGSAYLLFYI 1108
Cdd:cd02674  164 DTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
DUSP smart00695
Domain in ubiquitin-specific proteases;
116-202 1.35e-18

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 81.64  E-value: 1.35e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264      116 TQKEGDKVCIVPKVWYDKFFDPDV-TDPEDIGPI-NTRMICRDF-ENFVLEDYNRCPYLSIAEPVFNFLSEIYGMTSGsy 192
Cdd:smart00695    1 PLEEGLTWYLISTRWYRQWADFVEgKDGKDPGPIdNSGILCSHGgPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78
                            90
                    ....*....|
gi 6322264      193 PVVTNLVINQ 202
Cdd:smart00695   79 PIPRKVVCQG 88
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
99-1111 0e+00

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 1068.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264    99 LEQQRDVVArliEENKETQKEGDKVCIVPKVWYDKFFDPDVTDPEDIGPINTRMICR-DFENFVLEDYNRCPYLSIAEPV 177
Cdd:COG5560   26 LMMQEELID---EKPAESSKQCEYAVIFAYAWYEGMFDRASCDGGSPGPIVQGPIVDfEPESLKKSLREGIDYSIISGAV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   178 FNFLSEIYGMTSGSYPVVTNLVINQTTGEleTEYNKWFFRLHYLTEkQDGRKRRHGQDdsIMYLSMSALNLVRDLVEKSM 257
Cdd:COG5560  103 WQLLVRWYGLAGLITPRITVLLPSESAPE--VESYPVVFKLHWLFS-INGSLINLGHD--PVPHSASSHGTLRDLSERVM 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   258 NLFFEKADhldvnavDFKIWFVSEGSDIATDSNVSTFLNSSYEITPLQFLELPIKKLLIPDMFENRLDKITSNPSDLVIE 337
Cdd:COG5560  178 NAFVDPSD-------DFRLWDVVPEIMGLRLGLDSFFRRYRVLASDGRVLHPLTRLELFEDRSVLLLSKITRNPDWLVDS 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   338 ikpiegnHHWPSNYFAYNKLepasGTTGLVNLGNTCYMNSALQCLVHIPQLRDYFLYDGYEDEINEENPLGYHGYVARAF 417
Cdd:COG5560  251 -------IVDDHNRSINKEA----GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAY 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   418 SDLVQKLFqnrmsiMQRNAAFPPSMFKSTIGHFNSMFSGYMQQDSQEFLAFLLDSLHEDLNRIIKKEYTEKPSLSPGDDV 497
Cdd:COG5560  320 ADLIKQLY------DGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDV 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   498 ndwnVVKKLADDTWEMHLKRNCSVITDLFVGMYKSTLYCPECQNVSITFDPYNDVTLPLPVDTVWDKTIKIFPMNSPPLL 577
Cdd:COG5560  394 ----VVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGRRQP 469
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   578 LEVELSKSSTYMDLKNYVGKMSGLDPNTlfgcEIFSNQIYVNYESTESNAQFLTLQELIKPADDVIFYElpvTNDNEVIV 657
Cdd:COG5560  470 LKIELDASSTIRGLKKLVDAEYGKLGCF----EIKVMCIYYGGNYNMLEPADKVLLQDIPQTDFVYLYE---TNDNGIEV 542
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   658 PVLNTRIEKGYKNAMLFGVPFFiTLKedeLNNPGAIRMKLQNrfvhlsggyipfpepvgnrtdfadafpllvekypdvEF 737
Cdd:COG5560  543 PVVHLRIEKGYKSKRLFGDPFL-QLN---VLIKASIYDKLVK------------------------------------EF 582
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   738 EQYkdiLQYTSIKVTDKDKSFFSIKIlsvekeqqfaSNNRTGPNFWtpisqlnLDKATDIDDKLEDvvkdiynysslvdc 817
Cdd:COG5560  583 EEL---LVLVEMKKTDVDLVSEQVRL----------LREESSPSSW-------LKLETEIDTKREE-------------- 628
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   818 aegvlmQVDDEgdtegsEAKNFskpfqsgddeenketvtnnenvnntndrdedmeltddveedastepeltdkPEALdki 897
Cdd:COG5560  629 ------QVEEE------GQMNF---------------------------------------------------NDAV--- 642
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   898 kdsltstpfailsmndIIVCEWSELGSNEAFSddkiynweNPATLPNKELENAklersnakERTITLDDCLQLFSKPEIL 977
Cdd:COG5560  643 ----------------VISCEWEEKRYLSLFS--------YDPLWTIREIGAA--------ERTITLQDCLNEFSKPEQL 690
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   978 GLTDSWYCPTCKEHRQATKQIQLWNTPDILLIHLKRFESQRSFSDKIDATVNFPITDLDLSRYVVYKDDPRgLIYDLYAV 1057
Cdd:COG5560  691 GLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPR-LIYDLYAV 769
                        970       980       990      1000      1010
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6322264  1058 DNHYGGLGGGHYTAYVKNFADNKWYYFDDSRVTETAPENSIAGSAYLLFYIRRH 1111
Cdd:COG5560  770 DNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
364-580 1.71e-52

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 186.88  E-value: 1.71e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264     364 TGLVNLGNTCYMNSALQCLVHIPQLRDYFLYDGYEDEINEENPlgyHGYVARAFSDLVQKLFQNrmsimQRNAAFPPSMF 443
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK---DINLLCALRDLFKALQKN-----SKSSSVSPKMF 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264     444 KSTIGHFNSMFSGYMQQDSQEFLAFLLDSLHEDLNRiikkeytekpslspgddvndwnvvkkladdtweMHLKRNCSVIT 523
Cdd:pfam00443   73 KKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNG---------------------------------NHSTENESLIT 119
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6322264     524 DLFVGMYKSTLYCPECQNVSITFDPYNDVTLPLPVDTVWDKTIKIFPMNSPPLLLEV 580
Cdd:pfam00443  120 DLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKTASLQICFLQFSKLEE 176
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
962-1108 3.83e-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: 182.87  E-value: 3.83e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   962 ITLDDCLQLFSKPEILGLTDSWYCPTCKEHRQATKQIQLWNTPDILLIHLKRFESQRSFSDKIDATVNFPITDLDLSRYV 1041
Cdd:cd02674   84 VTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPVTFPLNDLDLTPYV 163
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322264  1042 VYKDDPRGLIYDLYAVDNHYGGLGGGHYTAYVKNFADNKWYYFDDSRVTETAPENSIAGSAYLLFYI 1108
Cdd:cd02674  164 DTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
952-1107 3.04e-43

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 160.30  E-value: 3.04e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264     952 LERSNAKERTITLDDCLQLFSKPEILGLTDSWYCPTCKEHRQATKQIQLWNTPDILLIHLKRFESQRSFSDKIDATVNFP 1031
Cdd:pfam00443  152 IPGDSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFP 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264    1032 ItDLDLSRYV---VYKDDPRGLIYDLYAVDNHYGGLGGGHYTAYVKNFADNKWYYFDDSRVTETAPENSI-AGSAYLLFY 1107
Cdd:pfam00443  232 L-ELDLSRYLaeeLKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVlSSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
961-1108 6.84e-32

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: 125.67  E-value: 6.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   961 TITLDDCLQLFSKPEILGLTDSWYCPTCKeHRQATKQIQLWNTPDILLIHLKRFESQRSFS-DKIDATVNFPITdLDLSR 1039
Cdd:cd02257   98 QVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFSFNEDGTkEKLNTKVSFPLE-LDLSP 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264  1040 YVVYK-----DDPRGLIYDLYAVDNHYGGLGGG-HYTAYVKNFADNKWYYFDDSRVTETAPE-----NSIAGSAYLLFYI 1108
Cdd:cd02257  176 YLSEGekdsdSDNGSYKYELVAVVVHSGTSADSgHYVAYVKDPSDGKWYKFNDDKVTEVSEEevlefGSLSSSAYILFYE 255
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
941-1108 9.77e-30

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: 121.33  E-value: 9.77e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   941 TLPNKELENAKLERSNAKErTITLDDCLQLFSKPEILGltDSWY-CPTCKEHRQATKQIQLWNTPDILLIHLKRFE-SQR 1018
Cdd:cd02660  156 DIPNKSTPSWALGESGVSG-TPTLSDCLDRFTRPEKLG--DFAYkCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEhSLN 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264  1019 SFSDKIDATVNFPiTDLDLSRYV-----VYKD---DPRGLIYDLYAVDNHYGGLGGGHYTAYVKNfADNKWYYFDDSRVT 1090
Cdd:cd02660  233 KTSRKIDTYVQFP-LELNMTPYTsssigDTQDsnsLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQ-GDGQWFKFDDAMIT 310
                        170
                 ....*....|....*...
gi 6322264  1091 ETAPENSIAGSAYLLFYI 1108
Cdd:cd02660  311 RVSEEEVLKSQAYLLFYH 328
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
963-1108 1.89e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 120.07  E-value: 1.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   963 TLDDCLQLFSKPEILGLTDSWYCPTCKEHRQATKQIQLWNTPDILLIHLKRFESQRsfSDKIDATVNFPITdLDLSRYVV 1042
Cdd:cd02661  163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GGKINKQISFPET-LDLSPYMS 239
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322264  1043 YKDDPrGLIYDLYAVDNHYGGLGGG-HYTAYVKNfADNKWYYFDDSRVTETAPENSIAGSAYLLFYI 1108
Cdd:cd02661  240 QPNDG-PLKYKLYAVLVHSGFSPHSgHYYCYVKS-SNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
365-561 9.43e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 109.77  E-value: 9.43e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   365 GLVNLGNTCYMNSALQCLVHIPQLRDYFLYDGYEDEINEENPlgyHGYVARAFSDLVQKLFQNrmsimQRNAAFPPSMFK 444
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSP---NSCLSCAMDEIFQEFYYS-----GDRSPYGPINLL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   445 STIGHFNSMFSGYMQQDSQEFLAFLLDSLHEDLNRIIKKEYTEKPslspgddvndwnvvkkladdtwemhlkrnCSVITD 524
Cdd:cd02660   74 YLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESH-----------------------------CNCIIH 124
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 6322264   525 -LFVGMYKSTLYCPECQNVSITFDPYNDVTLPLPVDTV 561
Cdd:cd02660  125 qTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKST 162
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
364-563 1.14e-23

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 103.12  E-value: 1.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   364 TGLVNLGNTCYMNSALQCLVHIPQLRDYFLYDGYEDEINEENPLgyhgyVARAFSDLVQKLFQNRMSIMqrnaafPPSMF 443
Cdd:cd02661    2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFC-----MMCALEAHVERALASSGPGS------APRIF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   444 KSTIGHFNSMFSGYMQQDSQEFLAFLLDSLHEDLNRIIKKEYTEKPSLspgddvndwnvvkkladdtwemhlkRNCSVIT 523
Cdd:cd02661   71 SSNLKQISKHFRIGRQEDAHEFLRYLLDAMQKACLDRFKKLKAVDPSS-------------------------QETTLVQ 125
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 6322264   524 DLFVGMYKSTLYCPECQNVSITFDPYNDVTLPLP-VDTVWD 563
Cdd:cd02661  126 QIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKgADSLED 166
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
365-557 3.62e-21

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: 93.89  E-value: 3.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   365 GLVNLGNTCYMNSALQCLVHipqlrdyflydgyedeineenplgyhgyvarafsdlvqklfqnrmsimqrnaafppsmfk 444
Cdd:cd02674    1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   445 stighfnsmfsgyMQQDSQEFLAFLLDSLHedlnriikkeytekpslspgddvndwnvvkkladdtwemhlkrncSVITD 524
Cdd:cd02674   21 -------------DQQDAQEFLLFLLDGLH---------------------------------------------SIIVD 42
                        170       180       190
                 ....*....|....*....|....*....|...
gi 6322264   525 LFVGMYKSTLYCPECQNVSITFDPYNDVTLPLP 557
Cdd:cd02674   43 LFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIP 75
DUSP smart00695
Domain in ubiquitin-specific proteases;
116-202 1.35e-18

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 81.64  E-value: 1.35e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264      116 TQKEGDKVCIVPKVWYDKFFDPDV-TDPEDIGPI-NTRMICRDF-ENFVLEDYNRCPYLSIAEPVFNFLSEIYGMTSGsy 192
Cdd:smart00695    1 PLEEGLTWYLISTRWYRQWADFVEgKDGKDPGPIdNSGILCSHGgPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78
                            90
                    ....*....|
gi 6322264      193 PVVTNLVINQ 202
Cdd:smart00695   79 PIPRKVVCQG 88
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
963-1121 7.53e-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 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: 86.32  E-value: 7.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   963 TLDDCLQLFSKPEILGLTDSWYCPTCKEHRQATKQIQLWNTPDILLIHLKR--FESQRSFSDKIDATVNFPiTDLDLSRY 1040
Cdd:cd02668  157 TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRfvFDRKTGAKKKLNASISFP-EILDMGEY 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264  1041 VVYKdDPRGLIYDLYAVDNHY-GGLGGGHYTAYVKNFADNKWYYFDDSRVTETAPENSIAGSAYLLFYIRRHKDGNGLGS 1119
Cdd:cd02668  236 LAES-DEGSYVYELSGVLIHQgVSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKLGNSEDPAKPRKSEIKKGTHS 314

                 ..
gi 6322264  1120 SK 1121
Cdd:cd02668  315 SR 316
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
914-1107 1.23e-17

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: 84.75  E-value: 1.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   914 IIVCEWSELGSNEAFSDDKIynwenpaTLPNKELENaklersnaKERTItlDDCLQLFSKPEILGLTDSWYCPTCKEhrq 993
Cdd:cd02667   80 TIMCESCGTVSLVYEPFLDL-------SLPRSDEIK--------SECSI--ESCLKQFTEVEILEGNNKFACENCTK--- 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   994 ATKQIQLWNTPDILLIHLKRFESQRSFSD-KIDATVNFPiTDLDLSRYVVYKDD-PRG---LIYDLYAVDNHYGGLGGGH 1068
Cdd:cd02667  140 AKKQYLISKLPPVLVIHLKRFQQPRSANLrKVSRHVSFP-EILDLAPFCDPKCNsSEDkssVLYRLYGVVEHSGTMRSGH 218
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264  1069 YTAYVK---------------NFADN------KWYYFDDSRVTETAPENSIAGSAYLLFY 1107
Cdd:cd02667  219 YVAYVKvrppqqrlsdltkskPAADEagpgsgQWYYISDSDVREVSLEEVLKSEAYLLFY 278
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
365-487 3.38e-17

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: 83.91  E-value: 3.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   365 GLVNLGNTCYMNSALQCLVHIP--QLRDYFLYDGYEDEINE-ENPLGYHgyvaraFSDLVQKLFQNR----MSIMQRNAA 437
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPsfQWRYDDLENKFPSDVVDpANDLNCQ------LIKLADGLLSGRyskpASLKSENDP 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6322264   438 FP----PSMFKSTIGHFNSMFSGYMQQDSQEFLAFLLDSLHEDLNRIIKKEYTE 487
Cdd:cd02658   75 YQvgikPSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGLNPND 128
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
365-566 4.95e-17

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: 82.15  E-value: 4.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   365 GLVNLGNTCYMNSALQCLVHipqlrdyflydgyedeineenplgyhgyvarafsdlvqklfqnrmsimqrnaafppsmfk 444
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   445 stighfnsmfsgyMQQDSQEFLAFLLDSLHEDLNRIIKKEYTEKPSLspgddvndwnvvkkladdtwemhlkrncSVITD 524
Cdd:cd02257   21 -------------EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLK----------------------------SLIHD 59
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 6322264   525 LFVGMYKSTLYCPECQNVSITFDPYNDVTLPLPVDTVWDKTI 566
Cdd:cd02257   60 LFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGLPQVSL 101
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
964-1109 8.54e-17

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: 83.08  E-value: 8.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   964 LDDCLQLFSKPEILGLTDSWYCPTCKEHRQATKQIQLWNTPDILLIHLKRFE--SQRSFSDKIDATVNFPITdLDLSRYV 1041
Cdd:cd02659  153 LEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfdFETMMRIKINDRFEFPLE-LDMEPYT 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264  1042 V----------YKDDPRGLIYDLYAVDNHYGGLGGGHYTAYVKNFADNKWYYFDDSRVTETAPENSIA------------ 1099
Cdd:cd02659  232 EkglakkegdsEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEecfggeetqkty 311
                        170       180
                 ....*....|....*....|
gi 6322264  1100 ----------GSAYLLFYIR 1109
Cdd:cd02659  312 dsgprafkrtTNAYMLFYER 331
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
365-559 1.03e-14

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: 75.89  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   365 GLVNLGNTCYMNSALQCLVHIPQLRDYFLYDgyedeineenplgyhgyvarafsdlvqklfqnrmsimqrnaafpPSMFK 444
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET--------------------------------------------PKELF 36
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   445 STIGHFNSMFSGYMQQDSQEFLAFLLDSLHedlnriikkeytekpslspgddvndwnvvkkladdtwemhlkrncSVITD 524
Cdd:cd02667   37 SQVCRKAPQFKGYQQQDSHELLRYLLDGLR---------------------------------------------TFIDS 71
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 6322264   525 LFVGMYKSTLYCPECQNVSITFDPYNDVTLPLPVD 559
Cdd:cd02667   72 IFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDE 106
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
959-1107 1.32e-14

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: 76.19  E-value: 1.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   959 ERTITLDDCLQLFSKPEILGLTDSWYCPTCKEHRQATKQIQLWNTPDILLIHLKRFESQRSFS--DKIDATVNFPITdLD 1036
Cdd:cd02663  144 EQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNryIKLFYRVVFPLE-LR 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264  1037 LSRYVVYKDDPRgLIYDLYAVDNHY-GGLGGGHYTAYVKnfADNKWYYFDDSRVtETAPENSIA---------GSAYLLF 1106
Cdd:cd02663  223 LFNTTDDAENPD-RLYELVAVVVHIgGGPNHGHYVSIVK--SHGGWLLFDDETV-EKIDENAVEeffgdspnqATAYVLF 298

                 .
gi 6322264  1107 Y 1107
Cdd:cd02663  299 Y 299
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
365-477 1.99e-14

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: 75.45  E-value: 1.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   365 GLVNLGNTCYMNSALQCLVHIPQLRDYFLYDGYEDEINEENplgyHGYVARAFSDLVQKLFQNRMSImqrnaafPPSMFK 444
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQS----SDNLTNALRDLFDTMDKKQEPV-------PPIEFL 69
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 6322264   445 STIGHFNSMFS------GYMQQDSQEFLAFLLDSLHEDL 477
Cdd:cd02657   70 QLLRMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKL 108
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
941-1107 5.91e-14

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: 74.54  E-value: 5.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   941 TLPNKELENAKLERS-----NAKERTITLDDCLQLFSKPEILGLTDSWYCPTCKEHRQATKQIQLWNTPDILLIHLKRFE 1015
Cdd:cd02671  154 SVPVQESELSKSEESseispDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFA 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264  1016 SQRSFSDKID--ATVNFPI-TDLDLSRYvVYKDDPRGLIYDLYAVDNHY-GGLGGGHYTAYVknfadnKWYYFDDSRVTE 1091
Cdd:cd02671  234 ANGSEFDCYGglSKVNTPLlTPLKLSLE-EWSTKPKNDVYRLFAVVMHSgATISSGHYTAYV------RWLLFDDSEVKV 306
                        170       180
                 ....*....|....*....|....*
gi 6322264  1092 T---------APENSIAGSAYLLFY 1107
Cdd:cd02671  307 TeekdflealSPNTSSTSTPYLLFY 331
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
365-559 1.25e-11

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 66.95  E-value: 1.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   365 GLVNLGNTCYMNSALQCLVHipqlrdYFLYDgyedeineenplgyhgyvarAFSDLVQKLFQNRmsimQRNAAFPPSMFK 444
Cdd:cd02663    1 GLENFGNTCYCNSVLQALYF------ENLLT--------------------CLKDLFESISEQK----KRTGVISPKKFI 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   445 STIGHFNSMFSGYMQQDSQEFLAFLLDSLHEDLNRIIKKEYTEKPSLspgddvndwNVVKKLADDTWemhlkrncsvITD 524
Cdd:cd02663   51 TRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLN---------NNNNAEPQPTW----------VHE 111
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 6322264   525 LFVGMYKSTLYCPECQNVSITFDPYNDvtlpLPVD 559
Cdd:cd02663  112 IFQGILTNETRCLTCETVSSRDETFLD----LSID 142
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1004-1109 3.11e-11

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 65.59  E-value: 3.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264  1004 PDILLIHLKRFESQRSFSdKIDATVNFPItdldlsRYVVYKDDPRGL----IYDLYAVDNHYGGLGGGHYTAYVKNfaDN 1079
Cdd:COG5533  180 PKILTIQLKRFANLGGNQ-KIDTEVDEKF------ELPVKHDQILNIvketYYDLVGFVLHQGSLEGGHYIAYVKK--GG 250
                         90       100       110
                 ....*....|....*....|....*....|...
gi 6322264  1080 KWYYFDDSRVTETAPENSI---AGSAYLLFYIR 1109
Cdd:COG5533  251 KWEKANDSDVTPVSEEEAInekAKNAYLYFYER 283
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
877-1107 4.28e-10

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 61.61  E-value: 4.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   877 VEEDAStepeltdkpEALDKIKDSLTS---TPFAILsMNDIIVCewSELGSNEAFSDDKIYNWENPatLPNKELENakle 953
Cdd:cd02662   33 EQQDAH---------ELFQVLLETLEQllkFPFDGL-LASRIVC--LQCGESSKVRYESFTMLSLP--VPNQSSGS---- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   954 rsnakerTITLDDCLQLFSKPEILgltDSWYCPTCKehrqaTKQIQLwntPDILLIHLKRFE-SQRSFSDKIDATVNFPi 1032
Cdd:cd02662   95 -------GTTLEHCLDDFLSTEII---DDYKCDRCQ-----TVIVRL---PQILCIHLSRSVfDGRGTSTKNSCKVSFP- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264  1033 tdLDLSRYvvykddprglIYDLYAVDNHYGGLGGGHYTAY--------------------VKNFADNKWYYFDDSRVTET 1092
Cdd:cd02662  156 --ERLPKV----------LYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEV 223
                        250
                 ....*....|....*.
gi 6322264  1093 APENSI-AGSAYLLFY 1107
Cdd:cd02662  224 SESEVLeQKSAYMLFY 239
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
362-483 4.95e-10

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 63.49  E-value: 4.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   362 GTTGLVNLGNTCYMNSALQCLVHIPQLRDYFL-YDGYEDEINEENPLgyhgyVARaFSDLVQKLFQnrmsimqrnaafpP 440
Cdd:cd02669  118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLlYENYENIKDRKSEL-----VKR-LSELIRKIWN-------------P 178
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6322264   441 SMFKSTIG----------HFNSMFSGYMQQDSQEFLAFLLDSLHEDLNRIIKK 483
Cdd:cd02669  179 RNFKGHVSphellqavskVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGSKKP 231
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
365-474 6.66e-10

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 62.12  E-value: 6.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   365 GLVNLGNTCYMNSALQCLVHIPQLRDYFLyDGYEDEINEENPLGyhgyvarafsdLVQKLFQNRMSIMQRNAAFPPSMFk 444
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDFRRQVL-SLNLPRLGDSQSVM-----------KKLQLLQAHLMHTQRRAEAPPDYF- 67
                         90       100       110
                 ....*....|....*....|....*....|....
gi 6322264   445 stighFNSM----FSGYMQQDSQEFLAFLLDSLH 474
Cdd:cd02664   68 -----LEASrppwFTPGSQQDCSEYLRYLLDRLH 96
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1004-1107 7.65e-10

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 61.58  E-value: 7.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264  1004 PDILLIHLKRFESQRSFSD--KIDATVNFPITdLDLSRYVvykdDPRGLiYDLYAVDNHYGGLGGG-HYTAYVKNFADNK 1080
Cdd:cd02657  197 PKYLTVQFVRFFWKRDIQKkaKILRKVKFPFE-LDLYELC----TPSGY-YELVAVITHQGRSADSgHYVAWVRRKNDGK 270
                         90       100       110
                 ....*....|....*....|....*....|....
gi 6322264  1081 WYYFDDSRVTETAPEN--SIAG-----SAYLLFY 1107
Cdd:cd02657  271 WIKFDDDKVSEVTEEDilKLSGggdwhIAYILLY 304
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
963-1139 2.69e-09

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 61.81  E-value: 2.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   963 TLDDCLQLFSKPEILGLTDSWYCPTckeH--RQATKQIQLWNTPDILLIHLKRFES--QRSFSDKIDATVNFPITdLDLS 1038
Cdd:COG5077  339 NLQESFRRYIQVETLDGDNRYNAEK---HglQDAKKGVIFESLPPVLHLQLKRFEYdfERDMMVKINDRYEFPLE-IDLL 414
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264  1039 RYV---VYKDDPRGLIYDLYAVDNHYGGLGGGHYTAYVKNFADNKWYYFDDSRVTET----APENSIAG----------- 1100
Cdd:COG5077  415 PFLdrdADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRAtekeVLEENFGGdhpykdkirdh 494
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 6322264  1101 -------SAYLLFYIRRHKDGNGLGSSKLQEIIQKSRHGYDERIKK 1139
Cdd:COG5077  495 sgikrfmSAYMLVYLRKSMLDDLLNPVAAVDIPPHVEEVLSEEIDK 540
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1004-1107 2.98e-09

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 60.80  E-value: 2.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264  1004 PDILLIHLKRFESQRSFSDKIDATVNFPITDLDLSRYV--VYKDDPRGLIYDLYAVDNHYGGLGGGH-YTAYVKNFADNK 1080
Cdd:cd02669  333 PKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVhfDKPSLNLSTKYNLVANIVHEGTPQEDGtWRVQLRHKSTNK 412
                         90       100
                 ....*....|....*....|....*..
gi 6322264  1081 WYYFDDSRVTETAPENSIAGSAYLLFY 1107
Cdd:cd02669  413 WFEIQDLNVKEVLPQLIFLSESYIQIW 439
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
365-554 3.46e-09

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: 59.96  E-value: 3.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   365 GLVNLGNTCYMNSALQCLVHIPQLRDYfLYDGYEDEINEENPlgyhgyvarAFSDLVQKLF-QNRMSIMQRNAAFPPSMF 443
Cdd:cd02659    4 GLKNQGATCYMNSLLQQLYMTPEFRNA-VYSIPPTEDDDDNK---------SVPLALQRLFlFLQLSESPVKTTELTDKT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   444 KStighFNSMFS-GYMQQDSQEFLAFLLDSLHEDLnriiKKeyTEKPSLspgddvndwnvvkkladdtwemhlkrncsvI 522
Cdd:cd02659   74 RS----FGWDSLnTFEQHDVQEFFRVLFDKLEEKL----KG--TGQEGL------------------------------I 113
                        170       180       190
                 ....*....|....*....|....*....|..
gi 6322264   523 TDLFVGMYKSTLYCPECQNVSITFDPYNDVTL 554
Cdd:cd02659  114 KNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
963-1107 1.21e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 58.27  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   963 TLDDCLQLFSKPEILGLTDSWYCPTCKEHRQATKQIQLWNTPDILLIHLKRF------ESQRSFSDK--IDATVNFPITD 1034
Cdd:cd02664  135 SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFsydqktHVREKIMDNvsINEVLSLPVRV 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264  1035 LDLSRYVVY--KDDPRG---------LIYDLYAVDNHY-GGLGGGHYTAYVKNFADNK--------------------WY 1082
Cdd:cd02664  215 ESKSSESPLekKEEESGddgelvtrqVHYRLYAVVVHSgYSSESGHYFTYARDQTDADstgqecpepkdaeendesknWY 294
                        170       180       190
                 ....*....|....*....|....*....|..
gi 6322264  1083 YFDDSRVTETAPEN----SIAGS---AYLLFY 1107
Cdd:cd02664  295 LFNDSRVTFSSFESvqnvTSRFPkdtPYILFY 326
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
936-1107 1.23e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 58.10  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   936 WENPATLPNKELENAKLERSNAKERTITLDDCLQLFSKPEILGLtdswYCPTCKEHRQATKQIQLWNTPDILLIHLKRFE 1015
Cdd:cd02658  152 LSEILSLPVPKDEATEKEEGELVYEPVPLEDCLKAYFAPETIED----FCSTCKEKTTATKTTGFKTFPDYLVINMKRFQ 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264  1016 -SQRSFSDKIDATVNFPitdldlsryvvykDDPRGLIYDLYAVDNHY-GGLGGGHYTAYVKNFADN--KWYYFDDSRVTE 1091
Cdd:cd02658  228 lLENWVPKKLDVPIDVP-------------EELGPGKYELIAFISHKgTSVHSGHYVAHIKKEIDGegKWVLFNDEKVVA 294
                        170
                 ....*....|....*.
gi 6322264  1092 TAPENSIAGSAYLLFY 1107
Cdd:cd02658  295 SQDPPEMKKLGYIYFY 310
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
348-475 2.55e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 57.21  E-value: 2.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   348 PSNYFAYNKLEPASGTTGLVNLGNTCYMNSALQCLVHIPQLRD--YFLYDGYEDEIN-----EENPLGYHgyvarafsDL 420
Cdd:cd02671    9 PSSATSCEKRENLLPFVGLNNLGNTCYLNSVLQVLYFCPGFKHglKHLVSLISSVEQlqssfLLNPEKYN--------DE 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6322264   421 VqklfqnrmsimqrnAAFPPSMFKSTIGHFNSMFSGYMQQDSQEFLAFLLDSLHE 475
Cdd:cd02671   81 L--------------ANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE 121
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
120-200 3.15e-08

DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.


Pssm-ID: 399383  Cd Length: 80  Bit Score: 51.98  E-value: 3.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264     120 GDKVCIVPKVWYDKFFDPDVTDPEDIGPINTRMICRDFENFVL--EDYNRCPYLSIAEPVFNFLSEIYGmtsGSYPVVTN 197
Cdd:pfam06337    1 GDKVYLISSKWLNKWKSYVKEPNNEPGPIDNSDLLDDESNGQLkpNLQEGVDYVIVPEEVWEFLVEWYG---GGPEIKRN 77

                   ...
gi 6322264     198 LVI 200
Cdd:pfam06337   78 VVN 80
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
365-509 4.86e-08

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 55.96  E-value: 4.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   365 GLVNLGNTCYMNSALQCLVHipqlrdyflydgYEDEINEenplgYHGYVARAFSDLVQKlFQNRMSIMQRNAA--FPPSM 442
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAL------------YLPKLDE-----LLDDLSKELKVLKNV-IRKPEPDLNQEEAlkLFTAL 62
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322264   443 FKSTIGHFNSMFSGYMQQDSQEFLAFLLDSLHEDLNRIIKKEYT------EKPSLSPGDDVNDWNVVKKLADD 509
Cdd:COG5533   63 WSSKEHKVGWIPPMGSQEDAHELLGKLLDELKLDLVNSFTIRIFkttkdkKKTSTGDWFDIIIELPDQTWVNN 135
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
365-439 1.29e-06

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 51.21  E-value: 1.29e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322264   365 GLVNLGNTCYMNSALQCLVHIPQLRDYFlydgyeDEINEENplgyhgyvarafsDLvQKLFQNRMSIMQRNAAFP 439
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALASLPSLIEYL------EEFLEQQ-------------DA-HELFQVLLETLEQLLKFP 55
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
365-545 2.60e-06

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 50.88  E-value: 2.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   365 GLVNLGNTCYMNSALQCLVHIPQLRDYFLY-----DGYEDEINEENPLGYHGYVarafsDLVQKLFQNrMSIMQRNaAFP 439
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnsteDAELKNMPPDKPHEPQTII-----DQLQLIFAQ-LQFGNRS-VVD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   440 PSMFKSTIGHFNSmfsgyMQQDSQEFLAFLLdSLHEDlnriikkeytekpSLSPGDDVNDWNVVKkladdtwemhlkrnc 519
Cdd:cd02668   74 PSGFVKALGLDTG-----QQQDAQEFSKLFL-SLLEA-------------KLSKSKNPDLKNIVQ--------------- 119
                        170       180
                 ....*....|....*....|....*.
gi 6322264   520 svitDLFVGMYKSTLYCPECQNVSIT 545
Cdd:cd02668  120 ----DLFRGEYSYVTQCSKCGRESSL 141
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
350-473 2.33e-04

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 45.63  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   350 NYFAYNKLEpASGTTGLVNLGNTCYMNSALQCLVHIpqlrDYFLYDGYEDEINEENPLGYHGYvarafsdLVQKLFQNrM 429
Cdd:COG5077  181 SFLNYNSKK-ETGYVGLRNQGATCYMNSLLQSLFFI----AKFRKDVYGIPTDHPRGRDSVAL-------ALQRLFYN-L 247
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 6322264   430 SIMQRnaafPPSMFKSTIGHFNSMFSGYMQQDSQEFLAFLLDSL 473
Cdd:COG5077  248 QTGEE----PVDTTELTRSFGWDSDDSFMQHDIQEFNRVLQDNL 287
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
985-1107 2.34e-04

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: 44.44  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264   985 CPTCKeHRQATKQIQLWNTPDILLIHLKRFESQRSFSDkidatvnfpitDLDLSRYVVYKDDPRGLIYDLYAVDNHY-GG 1063
Cdd:cd02673  129 CSSCK-CESAISSERIMTFPECLSINLKRYKLRIATSD-----------YLKKNEEIMKKYCGTDAKYSLVAVICHLgES 196
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 6322264  1064 LGGGHYTAYVKN-FADNKWYYFDDSRVTETAPEN---SIAGSAYLLFY 1107
Cdd:cd02673  197 PYDGHYIAYTKElYNGSSWLYCSDDEIRPVSKNDvstNARSSGYLIFY 244
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
985-1089 4.42e-04

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 43.80  E-value: 4.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322264     985 CPTCKEHRQATKQIQLWNTPDILLIHLKRFESQrsfSDKIDATVNFPITDLDLSRYVVYKDDPRGLIYDLYAVDNH-YGG 1063
Cdd:pfam13423  196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE---WRQLWKTPGWLPPEIGLTLSDDLQGDNEIVKYELRGVVVHiGDS 272
                           90       100       110
                   ....*....|....*....|....*....|...
gi 6322264    1064 LGGGHYTAYVK-------NFADNKWYYFDDSRV 1089
Cdd:pfam13423  273 GTSGHLVSFVKvadseleDPTESQWYLFNDFLV 305
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
364-409 4.82e-04

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 44.02  E-value: 4.82e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 6322264   364 TGLVNLGNTCYMNSALQCLVHIPQLRDYFL-YDGYEDEINEENPLGY 409
Cdd:cd02666    2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLnFDESKAELASDYPTER 48
 
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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