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Conserved domains on  [gi|513197508|ref|XP_004936728|]
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ubiquitin carboxyl-terminal hydrolase 33 isoform X2 [Gallus gallus]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 12031674)

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
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
200-728 3.78e-69

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 232.72  E-value: 3.78e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  200 TGLKNIGNTCYMNAALQALSNCPPLTHFFLDCGGLARTDKKP---AICKSYLKLMTELWHKNRPGSVVPTGLFQGIKSVN 276
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  277 PTFRGYSQQDAQEFLRCLMDLLHEELKepivevedaqtmsveesmevdksqsdvgfqpcescgtcdkiendavfkpvled 356
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  357 paettmliqddennsitskdwqkekissnklnransmedlekdtnstseaneflnnqgtvkvqihsrfseyindvhmndv 436
Cdd:pfam00443     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  437 sgaqtlssnegtntrlsssppksctscssstpihkkvstvsspkRKKCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLE 516
Cdd:pfam00443 108 --------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFE 143

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  517 TFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapqgwiaffmeyfkrfvvscvpswfWGPVVTLQDCLAAFFARD 596
Cdd:pfam00443 144 PFSDLSLPIPGDSA------------------------------------------------ELKTASLQICFLQFSKLE 175

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  597 ELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEgLDLQPFLAKDSPAQIV---TY 673
Cdd:pfam00443 176 ELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDY 254

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 513197508  674 DLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 728
Cdd:pfam00443 255 RLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
DUSP smart00695
Domain in ubiquitin-specific proteases;
856-937 6.51e-27

Domain in ubiquitin-specific proteases;


:

Pssm-ID: 197831  Cd Length: 88  Bit Score: 105.13  E-value: 6.51e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508   856 EEESPSTFYCISMQWFREWEEFVKGKDSDPPGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEII 932
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGPRLkehLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80


                   ....*
gi 513197508   933 HRPPV 937
Cdd:smart00695  81 PRKVV 85
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
78-138 3.28e-17

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 76.53  E-value: 3.28e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 513197508   78 CQDCKVRGpNLWACLEnrCTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRVWCYACSKEV 138
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
DUSP super family cl12116
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 748-830 1.33e-16

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.


The actual alignment was detected with superfamily member smart00695:

Pssm-ID: 416436  Cd Length: 88  Bit Score: 75.47  E-value: 1.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508   748 MMEPSLLQFYVSRQWLNKFKTFAE------PGPISNNDFLCMHGGVPPHKASFIEDLVVMLPQNIWDNLYSRYGGGPAvn 821
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78


                   ....*....
gi 513197508   822 HLYVCHTCQ 830
Cdd:smart00695  79 PIPRKVVCQ 87
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
200-728 3.78e-69

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 232.72  E-value: 3.78e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  200 TGLKNIGNTCYMNAALQALSNCPPLTHFFLDCGGLARTDKKP---AICKSYLKLMTELWHKNRPGSVVPTGLFQGIKSVN 276
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  277 PTFRGYSQQDAQEFLRCLMDLLHEELKepivevedaqtmsveesmevdksqsdvgfqpcescgtcdkiendavfkpvled 356
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  357 paettmliqddennsitskdwqkekissnklnransmedlekdtnstseaneflnnqgtvkvqihsrfseyindvhmndv 436
Cdd:pfam00443     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  437 sgaqtlssnegtntrlsssppksctscssstpihkkvstvsspkRKKCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLE 516
Cdd:pfam00443 108 --------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFE 143

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  517 TFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapqgwiaffmeyfkrfvvscvpswfWGPVVTLQDCLAAFFARD 596
Cdd:pfam00443 144 PFSDLSLPIPGDSA------------------------------------------------ELKTASLQICFLQFSKLE 175

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  597 ELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEgLDLQPFLAKDSPAQIV---TY 673
Cdd:pfam00443 176 ELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDY 254

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 513197508  674 DLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 728
Cdd:pfam00443 255 RLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 489-729 5.09e-61

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 207.14  E-value: 5.09e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 489 SVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAklhsashqtslvktgscgeayapqgwiaffmeyfkr 568
Cdd:cd02674   38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 569 fvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTH 648
Cdd:cd02674   82 ------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTP 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 649 VSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFY 728
Cdd:cd02674  150 VTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229


                 .
gi 513197508 729 R 729
Cdd:cd02674  230 E 230
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
195-732 5.74e-45

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 175.07  E-value: 5.74e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 195 KTRGLTGLKNIGNTCYMNAALQALSNCPPLTHFFLDCG---GLARTDKKP---AICKSYLKLMTELwHKNRPGSVVPTGL 268
Cdd:COG5560  261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGF 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 269 FQGIKSVNPTFRGYSQQDAQEFLRCLMDLLHEELKEPIVEVEDAQTMSVEESMEVDKSQSDvgfqpceSCGTCDKIENDA 348
Cdd:COG5560  340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVKKKAK-------ECWWEHLKRNDS 412

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 349 V--------FKPVLEDPAETTMLIQDDENNSIT-----SKDWQKE-------------KISSNKLNRANSMEDL-----E 397
Cdd:COG5560  413 IitdlfqgmYKSTLTCPGCGSVSITFDPFMDLTlplpvSMVWKHTivvfpesgrrqplKIELDASSTIRGLKKLvdaeyG 492

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 398 KDTNSTSEANE--------FLNNQG-TVKVQIHSR-----FSEYIND-----VHMNDVSGAQT-------------LSSN 445
Cdd:COG5560  493 KLGCFEIKVMCiyyggnynMLEPADkVLLQDIPQTdfvylYETNDNGievpvVHLRIEKGYKSkrlfgdpflqlnvLIKA 572

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 446 EGTNTRLSSSppKSCTSCSSSTPIHKKVSTVSSPkrkkCKKYRSVISDIFDgtiissvqCLTcDRLSVTLETFQDLS-LP 524
Cdd:COG5560  573 SIYDKLVKEF--EELLVLVEMKKTDVDLVSEQVR----LLREESSPSSWLK--------LET-EIDTKREEQVEEEGqMN 637

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 525 IPGKEDLAKLHSASHQTSLVKTGSCGeayaPQGWIAFFMeyfkrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMY 604
Cdd:COG5560  638 FNDAVVISCEWEEKRYLSLFSYDPLW----TIREIGAAE-----------------RTITLQDCLNEFSKPEQLGLSDSW 696

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 605 SCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHG 683
Cdd:COG5560  697 YCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYG 774

                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*....
gi 513197508 684 TASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSN 732
Cdd:COG5560  775 GLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
DUSP smart00695
Domain in ubiquitin-specific proteases;
856-937 6.51e-27

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 105.13  E-value: 6.51e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508   856 EEESPSTFYCISMQWFREWEEFVKGKDSDPPGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEII 932
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGPRLkehLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80


                   ....*
gi 513197508   933 HRPPV 937
Cdd:smart00695  81 PRKVV 85
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 860-934 3.70e-21

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: 88.19  E-value: 3.70e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 513197508  860 PSTFYCISMQWFREWEEFVKGKDSDPpGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEIIHR 934
Cdd:pfam06337   1 GDKVYLISSKWLNKWKSYVKEPNNEP-GPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
78-138 3.28e-17

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 76.53  E-value: 3.28e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 513197508   78 CQDCKVRGpNLWACLEnrCTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRVWCYACSKEV 138
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
DUSP smart00695
Domain in ubiquitin-specific proteases;
748-830 1.33e-16

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 75.47  E-value: 1.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508   748 MMEPSLLQFYVSRQWLNKFKTFAE------PGPISNNDFLCMHGGVPPHKASFIEDLVVMLPQNIWDNLYSRYGGGPAvn 821
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78


                   ....*....
gi 513197508   822 HLYVCHTCQ 830
Cdd:smart00695  79 PIPRKVVCQ 87
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 756-826 5.81e-13

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: 65.08  E-value: 5.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  756 FYVSRQWLNKFKTFAE-----PGPISNNDFLCmhggvPPHKASFIEDLV-----VMLPQNIWDNLYSRYGGGPAVNHLYV 825
Cdd:pfam06337   5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLD-----DESNGQLKPNLQegvdyVIVPEEVWEFLVEWYGGGPEIKRNVV 79


                  .
gi 513197508  826 C 826
Cdd:pfam06337  80 N 80
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
77-129 3.28e-09

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 53.52  E-value: 3.28e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 513197508    77 SCQDCKvRGPNLWACLEnrCTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRV 129
Cdd:smart00290   1 RCSVCG-TIENLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
200-728 3.78e-69

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 232.72  E-value: 3.78e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  200 TGLKNIGNTCYMNAALQALSNCPPLTHFFLDCGGLARTDKKP---AICKSYLKLMTELWHKNRPGSVVPTGLFQGIKSVN 276
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  277 PTFRGYSQQDAQEFLRCLMDLLHEELKepivevedaqtmsveesmevdksqsdvgfqpcescgtcdkiendavfkpvled 356
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  357 paettmliqddennsitskdwqkekissnklnransmedlekdtnstseaneflnnqgtvkvqihsrfseyindvhmndv 436
Cdd:pfam00443     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  437 sgaqtlssnegtntrlsssppksctscssstpihkkvstvsspkRKKCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLE 516
Cdd:pfam00443 108 --------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFE 143

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  517 TFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapqgwiaffmeyfkrfvvscvpswfWGPVVTLQDCLAAFFARD 596
Cdd:pfam00443 144 PFSDLSLPIPGDSA------------------------------------------------ELKTASLQICFLQFSKLE 175

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  597 ELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEgLDLQPFLAKDSPAQIV---TY 673
Cdd:pfam00443 176 ELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDY 254

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 513197508  674 DLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 728
Cdd:pfam00443 255 RLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 489-729 5.09e-61

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 207.14  E-value: 5.09e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 489 SVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAklhsashqtslvktgscgeayapqgwiaffmeyfkr 568
Cdd:cd02674   38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 569 fvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTH 648
Cdd:cd02674   82 ------------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTP 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 649 VSFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFY 728
Cdd:cd02674  150 VTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229


                 .
gi 513197508 729 R 729
Cdd:cd02674  230 E 230
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 477-729 1.61e-52

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: 184.22  E-value: 1.61e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 477 SSPKRKKCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapq 556
Cdd:cd02257   43 SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGL-------------------------- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 557 gwiaffmeyfkrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKlRNGVKFCKVQKFPEILCIHLKRFR 636
Cdd:cd02257   97 ------------------------PQVSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFS 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 637 H-ELMFSTKIGTHVSFPLEgLDLQPFLAK-----DSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFDDQS 709
Cdd:cd02257  152 FnEDGTKEKLNTKVSFPLE-LDLSPYLSEgekdsDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDK 230

                        250       260
                 ....*....|....*....|....*
gi 513197508 710 VTEVSESTVQ-----NAEAYVLFYR 729
Cdd:cd02257  231 VTEVSEEEVLefgslSSSAYILFYE 255
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 490-728 7.22e-46

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: 167.93  E-value: 7.22e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 490 VISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAKLHSASHQTSLVktgscgeayapqgwiaffmeyfkrf 569
Cdd:cd02660  122 IIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGESGVSGTP------------------------- 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 570 vvscvpswfwgpvvTLQDCLAaFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELM-FSTKIGTH 648
Cdd:cd02660  177 --------------TLSDCLD-RFTRPEKLGDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNkTSRKIDTY 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 649 VSFPLEgLDLQPFLA--------KDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNlNNLWYEFDDQSVTEVSESTVQN 720
Cdd:cd02660  242 VQFPLE-LNMTPYTSssigdtqdSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVSEEEVLK 319


                 ....*...
gi 513197508 721 AEAYVLFY 728
Cdd:cd02660  320 SQAYLLFY 327
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
195-732 5.74e-45

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 175.07  E-value: 5.74e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 195 KTRGLTGLKNIGNTCYMNAALQALSNCPPLTHFFLDCG---GLARTDKKP---AICKSYLKLMTELwHKNRPGSVVPTGL 268
Cdd:COG5560  261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGF 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 269 FQGIKSVNPTFRGYSQQDAQEFLRCLMDLLHEELKEPIVEVEDAQTMSVEESMEVDKSQSDvgfqpceSCGTCDKIENDA 348
Cdd:COG5560  340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVKKKAK-------ECWWEHLKRNDS 412

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 349 V--------FKPVLEDPAETTMLIQDDENNSIT-----SKDWQKE-------------KISSNKLNRANSMEDL-----E 397
Cdd:COG5560  413 IitdlfqgmYKSTLTCPGCGSVSITFDPFMDLTlplpvSMVWKHTivvfpesgrrqplKIELDASSTIRGLKKLvdaeyG 492

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 398 KDTNSTSEANE--------FLNNQG-TVKVQIHSR-----FSEYIND-----VHMNDVSGAQT-------------LSSN 445
Cdd:COG5560  493 KLGCFEIKVMCiyyggnynMLEPADkVLLQDIPQTdfvylYETNDNGievpvVHLRIEKGYKSkrlfgdpflqlnvLIKA 572

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 446 EGTNTRLSSSppKSCTSCSSSTPIHKKVSTVSSPkrkkCKKYRSVISDIFDgtiissvqCLTcDRLSVTLETFQDLS-LP 524
Cdd:COG5560  573 SIYDKLVKEF--EELLVLVEMKKTDVDLVSEQVR----LLREESSPSSWLK--------LET-EIDTKREEQVEEEGqMN 637

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 525 IPGKEDLAKLHSASHQTSLVKTGSCGeayaPQGWIAFFMeyfkrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMY 604
Cdd:COG5560  638 FNDAVVISCEWEEKRYLSLFSYDPLW----TIREIGAAE-----------------RTITLQDCLNEFSKPEQLGLSDSW 696

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 605 SCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHG 683
Cdd:COG5560  697 YCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYG 774

                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*....
gi 513197508 684 TASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSN 732
Cdd:COG5560  775 GLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 475-728 1.87e-44

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: 163.22  E-value: 1.87e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 475 TVSSPKRKKCKKY------RSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGkedlaklhsashqtslvktgs 548
Cdd:cd02661  102 KACLDRFKKLKAVdpssqeTTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG--------------------- 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 549 cgeayapqgwiaffmeyfkrfvvscvpswfwgpVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEIL 628
Cdd:cd02661  161 ---------------------------------ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVL 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 629 CIHLKRFrhELMFSTKIGTHVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRnNLNNLWYEFDD 707
Cdd:cd02661  208 TIHLKRF--SNFRGGKINKQISFPET-LDLSPYMS-QPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVK-SSNGKWYNMDD 282

                        250       260
                 ....*....|....*....|.
gi 513197508 708 QSVTEVSESTVQNAEAYVLFY 728
Cdd:cd02661  283 SKVSPVSIETVLSQKAYILFY 303
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 491-732 5.41e-36

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 139.31  E-value: 5.41e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 491 ISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAklhsashqtslvktgscgeayapqgwiaffmEYFKRFV 570
Cdd:cd02659  113 IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLE-------------------------------ESLDAYV 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 571 VScvpswfwgpvvtlqdclaaffarDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRH--ELMFSTKIGTH 648
Cdd:cd02659  162 QG-----------------------ETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKINDR 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 649 VSFPLEgLDLQPFLAKDSPAQIV----------TYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV 718
Cdd:cd02659  219 FEFPLE-LDMEPYTEKGLAKKEGdsekkdsesyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDA 297

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 513197508 719 QNA----------------------EAYVLFYRKSN 732
Cdd:cd02659  298 EEEcfggeetqktydsgprafkrttNAYMLFYERKS 333
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 488-729 1.08e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 122.50  E-value: 1.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 488 RSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDlaklhsashqtslvktgscgeayapqgwiaffmeyfk 567
Cdd:cd02667   66 RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK------------------------------------- 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 568 rfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRngvKFCKVQKFPEILCIHLKRFRHELMFST-KIG 646
Cdd:cd02667  109 -------------SECSIESCLKQFTEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQPRSANLrKVS 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 647 THVSFPlEGLDLQPFL--------AKDSpaqiVTYDLLSVICHHGTASSGHYIAYCR-NNLNNL---------------- 701
Cdd:cd02667  173 RHVSFP-EILDLAPFCdpkcnsseDKSS----VLYRLYGVVEHSGTMRSGHYVAYVKvRPPQQRlsdltkskpaadeagp 247

                        250       260       270
                 ....*....|....*....|....*....|..
gi 513197508 702 ----WYEFDDQSVTEVSESTVQNAEAYVLFYR 729
Cdd:cd02667  248 gsgqWYYISDSDVREVSLEEVLKSEAYLLFYE 279
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 483-728 7.20e-28

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: 114.71  E-value: 7.20e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 483 KCKKYRSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPgkedlaklhsashqtslvktgscgeayapqgwiaff 562
Cdd:cd02663  101 NAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVE------------------------------------ 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 563 meyfkrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFS 642
Cdd:cd02663  145 ------------------QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLN 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 643 --TKIGTHVSFPLEgldLQPF-LAKDSPAQIVTYDLLSVICHHG-TASSGHYIAYCRNnlNNLWYEFDDQSVTEVSESTV 718
Cdd:cd02663  207 ryIKLFYRVVFPLE---LRLFnTTDDAENPDRLYELVAVVVHIGgGPNHGHYVSIVKS--HGGWLLFDDETVEKIDENAV 281

                        250
                 ....*....|....*...
gi 513197508 719 QN--------AEAYVLFY 728
Cdd:cd02663  282 EEffgdspnqATAYVLFY 299
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 485-712 6.12e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 112.51  E-value: 6.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 485 KKYRSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEdlaklhsashqtslvktgscgeayapqgwiaffme 564
Cdd:cd02668  112 PDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHK----------------------------------- 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 565 yfkrfvvscvpswfwgpvvTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHEL--MFS 642
Cdd:cd02668  157 -------------------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRktGAK 217

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 513197508 643 TKIGTHVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFDDQSVTE 712
Cdd:cd02668  218 KKLNASISFPEI-LDMGEYLA-ESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDVEE 286
DUSP smart00695
Domain in ubiquitin-specific proteases;
856-937 6.51e-27

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 105.13  E-value: 6.51e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508   856 EEESPSTFYCISMQWFREWEEFVKGKDSDPPGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEII 932
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDGKDPGPIDNSGILCSHGGPRLkehLVEGEDYVLIPEELWNKLVRWYGGGPGPI 80


                   ....*
gi 513197508   933 HRPPV 937
Cdd:smart00695  81 PRKVV 85
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 495-728 1.60e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 100.52  E-value: 1.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 495 FDGTIISSVQCLTCDRLS-VTLETFQDLSLPIPGKEdlaklhsashqtslvktgscgeayapqgwiaffmeyfkrfvvsc 573
Cdd:cd02662   56 FDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQS-------------------------------------------- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 574 vpswfWGPVVTLQDCLAAFFARDELKGdnmYSCGRCKklrngvkfCKVQKFPEILCIHLKRFR-HELMFSTKIGTHVSFP 652
Cdd:cd02662   92 -----SGSGTTLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVfDGRGTSTKNSCKVSFP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 653 LegldlqpFLakdspaQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNL--------------------WYEFDDQSVTE 712
Cdd:cd02662  156 E-------RL------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKdkepgsfvrmregpsstshpWWRISDTTVKE 222

                        250
                 ....*....|....*..
gi 513197508 713 VSESTV-QNAEAYVLFY 728
Cdd:cd02662  223 VSESEVlEQKSAYMLFY 239
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 860-934 3.70e-21

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: 88.19  E-value: 3.70e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 513197508  860 PSTFYCISMQWFREWEEFVKGKDSDPpGPIDNGKIAITKCGNAV---LKQGADSGQISEETWNFLQSIYGGGPEIIHR 934
Cdd:pfam06337   1 GDKVYLISSKWLNKWKSYVKEPNNEP-GPIDNSDLLDDESNGQLkpnLQEGVDYVIVPEEVWEFLVEWYGGGPEIKRN 77
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 489-729 1.76e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 93.71  E-value: 1.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 489 SVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLpipgkedlaklhsashqtslvktgscgeayapqgwiaffmeyfkr 568
Cdd:cd02664   97 TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL--------------------------------------------- 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 569 fvvsCVPSwfwgpvvtLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFR--HELMFSTKIG 646
Cdd:cd02664  132 ----SFPS--------VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydQKTHVREKIM 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 647 THVSFPlEGLDL----------QPFLAKDSPA--------QIVTYDLLSVICHHGTAS-SGHYIAYCRN----------- 696
Cdd:cd02664  200 DNVSIN-EVLSLpvrvesksseSPLEKKEEESgddgelvtRQVHYRLYAVVVHSGYSSeSGHYFTYARDqtdadstgqec 278

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 513197508 697 ---------NLNNLWYEFDDQSVTEVSESTVQNAE-------AYVLFYR 729
Cdd:cd02664  279 pepkdaeenDESKNWYLFNDSRVTFSSFESVQNVTsrfpkdtPYILFYE 327
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 488-729 6.72e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 91.88  E-value: 6.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 488 RSVISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEdLAKLHSASHQTSLVKTgscgeayapqgwiaffmeyfk 567
Cdd:cd02671  120 QELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESE-LSKSEESSEISPDPKT--------------------- 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 568 rfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFS----- 642
Cdd:cd02671  178 -------------EMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcygg 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 643 -TKIGTHVSFPlegLDLQPFLAKDSPAQIVtYDLLSVICHHG-TASSGHYIAYCRnnlnnlWYEFDDQSV---------T 711
Cdd:cd02671  245 lSKVNTPLLTP---LKLSLEEWSTKPKNDV-YRLFAVVMHSGaTISSGHYTAYVR------WLLFDDSEVkvteekdflE 314

                        250
                 ....*....|....*...
gi 513197508 712 EVSESTVQNAEAYVLFYR 729
Cdd:cd02671  315 ALSPNTSSTSTPYLLFYK 332
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 584-718 2.13e-17

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 87.62  E-value: 2.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  584 TLQDCLAAFFARDELKGDNMYSCGR--CKKLRNGVKFckvQKFPEILCIHLKRFRHELMFST--KIGTHVSFPLEgLDLQ 659
Cdd:COG5077   339 NLQESFRRYIQVETLDGDNRYNAEKhgLQDAKKGVIF---ESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPLE-IDLL 414

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 513197508  660 PFLAKD---SPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV 718
Cdd:COG5077   415 PFLDRDadkSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
78-138 3.28e-17

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 76.53  E-value: 3.28e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 513197508   78 CQDCKVRGpNLWACLEnrCTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRVWCYACSKEV 138
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
DUSP smart00695
Domain in ubiquitin-specific proteases;
748-830 1.33e-16

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 75.47  E-value: 1.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508   748 MMEPSLLQFYVSRQWLNKFKTFAE------PGPISNNDFLCMHGGVPPHKASFIEDLVVMLPQNIWDNLYSRYGGGPAvn 821
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG-- 78


                   ....*....
gi 513197508   822 HLYVCHTCQ 830
Cdd:smart00695  79 PIPRKVVCQ 87
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 625-729 4.42e-16

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: 80.07  E-value: 4.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 625 PEILCIHLKRF--RHELMFSTKIGTHVSFPLEgLDLQPFLakdSPAQIvtYDLLSVICHHG-TASSGHYIAYCRNNLNNL 701
Cdd:cd02657  197 PKYLTVQFVRFfwKRDIQKKAKILRKVKFPFE-LDLYELC---TPSGY--YELVAVITHQGrSADSGHYVAWVRRKNDGK 270

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 513197508 702 WYEFDDQSVTEVSESTVQNAE-------AYVLFYR 729
Cdd:cd02657  271 WIKFDDDKVSEVTEEDILKLSgggdwhiAYILLYK 305
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
623-730 3.12e-15

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 77.15  E-value: 3.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 623 KFPEILCIHLKRFRHELMFsTKIGTHVSFPLEgldlQPFLaKDSPAQIVT---YDLLSVICHHGTASSGHYIAYCRNnlN 699
Cdd:COG5533  178 KLPKILTIQLKRFANLGGN-QKIDTEVDEKFE----LPVK-HDQILNIVKetyYDLVGFVLHQGSLEGGHYIAYVKK--G 249

                         90       100       110
                 ....*....|....*....|....*....|....
gi 513197508 700 NLWYEFDDQSVTEVSESTVQNA---EAYVLFYRK 730
Cdd:COG5533  250 GKWEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 608-729 3.79e-15

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: 78.90  E-value: 3.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 608 RCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKIGTHVSFPLEGLDLQPFLAKDSPAQI--VTYDLLSVICHHGT- 684
Cdd:cd02669  316 TETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNlsTKYNLVANIVHEGTp 395

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 513197508 685 ASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYR 729
Cdd:cd02669  396 QEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 491-729 3.05e-13

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: 71.59  E-value: 3.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 491 ISDIFDGTIISSVQCLTCDRLSVTLETFQDLSLPIPGKEDLAKLHSAshqtslvktgscgEAYAPqgwiaffmeyfkrfv 570
Cdd:cd02658  126 PNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATEKEEGE-------------LVYEP--------------- 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 571 vscvpswfwgpvVTLQDCLAAFFARDELKgdnmYSCGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMF-STKIGTHV 649
Cdd:cd02658  178 ------------VPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLENWvPKKLDVPI 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 650 SFPLEGLDlqpflakdspaqiVTYDLLSVICHHGT-ASSGHYIAYCRNNLNN--LWYEFDDQSVTEVSESTVQNAEAYVL 726
Cdd:cd02658  242 DVPEELGP-------------GKYELIAFISHKGTsVHSGHYVAHIKKEIDGegKWVLFNDEKVVASQDPPEMKKLGYIY 308


                 ...
gi 513197508 727 FYR 729
Cdd:cd02658  309 FYQ 311
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 756-826 5.81e-13

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: 65.08  E-value: 5.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  756 FYVSRQWLNKFKTFAE-----PGPISNNDFLCmhggvPPHKASFIEDLV-----VMLPQNIWDNLYSRYGGGPAVNHLYV 825
Cdd:pfam06337   5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLD-----DESNGQLKPNLQegvdyVIVPEEVWEFLVEWYGGGPEIKRNVV 79


                  .
gi 513197508  826 C 826
Cdd:pfam06337  80 N 80
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 201-329 8.74e-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 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: 64.27  E-value: 8.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 201 GLKNIGNTCYMNAALQALSNCPPLTHFFLDCGGLARTDKKPA--ICKSYLKLMTELWHKNRPgsVVPTGLFQGIKSVNPT 278
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSdnLTNALRDLFDTMDKKQEP--VPPIEFLQLLRMAFPQ 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 279 F------RGYSQQDAQEFLRCLMDLLHEELKEPIVE---VEDAQTMSVEESMEVDKSQSD 329
Cdd:cd02657   79 FaekqnqGGYAQQDAEECWSQLLSVLSQKLPGAGSKgsfIDQLFGIELETKMKCTESPDE 138
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 673-728 3.36e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 62.89  E-value: 3.36e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 513197508 673 YDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV------QNAEAYVLFY 728
Cdd:cd02666  281 YRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVflftlgNTATPYFLVY 342
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
77-129 3.28e-09

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 53.52  E-value: 3.28e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 513197508    77 SCQDCKvRGPNLWACLEnrCTYVGCGETHVDHSTTHSQETKHCLTVNLTTLRV 129
Cdd:smart00290   1 RCSVCG-TIENLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
201-307 7.35e-09

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 57.89  E-value: 7.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 201 GLKNIGNTCYMNAALQALS-NCPPLTHFFLDCGGLART-------DKKPAICKSYLKLMTELWHKNRPgsvvptglfqgi 272
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEH------------ 68

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 513197508 273 kSVNPTFRGYSQQDAQEFLRCLMDllheELKEPIV 307
Cdd:COG5533   69 -KVGWIPPMGSQEDAHELLGKLLD----ELKLDLV 98
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 606-728 2.88e-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: 55.61  E-value: 2.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 606 CGRCKKlRNGVKFCKVQKFPEILCIHLKRFRhelmFSTKIGTHvsfplegldlqpfLAKDSPA------QIVTYDLLSVI 679
Cdd:cd02673  129 CSSCKC-ESAISSERIMTFPECLSINLKRYK----LRIATSDY-------------LKKNEEImkkycgTDAKYSLVAVI 190

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 513197508 680 CHHG-TASSGHYIAYCRNNLN-NLWYEFDDQSVTEVSESTVQNA---EAYVLFY 728
Cdd:cd02673  191 CHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 623-728 8.10e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 54.10  E-value: 8.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 623 KFPEILCIHLKRFRHELMFSTKIGTHVSFPLEgldlqpflakdspAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLW 702
Cdd:cd02665  127 ELPPVLTFELSRFEFNQGRPEKIHDKLEFPQI-------------IQQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEW 193

                         90       100       110
                 ....*....|....*....|....*....|....
gi 513197508 703 YEFDDQSVTEVSESTVQ--------NAEAYVLFY 728
Cdd:cd02665  194 EKYNDISVTESSWEEVErdsfgggrNPSAYCLMY 227
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 568-729 9.30e-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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 54.07  E-value: 9.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 568 RFVVSCVPSWFWGPVVTLQDCLAAFFardelkgdnmyscgrckklRNGVkfckVQKFPEILCIHLKRFRHELMFSTKIGT 647
Cdd:cd02670   65 RLLQIPVPDDDDGGGITLEQCLEQYF-------------------NNSV----FAKAPSCLIICLKRYGKTEGKAQKMFK 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 648 HVsFPLEGLDLQPFLAKDSPA-------QIVTYD--------------LLSVICHHGTA-SSGHYIAYCRNN-------- 697
Cdd:cd02670  122 KI-LIPDEIDIPDFVADDPRAcskcqleCRVCYDdkdfsptcgkfklsLCSAVCHRGTSlETGHYVAFVRYGsysltetd 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 513197508 698 ---LNNLWYEFDD-------QSVTEVSESTVQnAEAYVLFYR 729
Cdd:cd02670  201 neaYNAQWVFFDDmadrdgvSNGFNIPAARLL-EDPYMLFYQ 241
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 201-303 5.17e-07

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: 52.71  E-value: 5.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 201 GLKNIGNTCYMNAALQALSNCPPL-THFFLDCGGLARTDKKPAIC------------KS--YLKLMTELW-HKNRPGSVV 264
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVLFSIPSFqWRYDDLENKFPSDVVDPANDlncqlikladglLSgrYSKPASLKSeNDPYQVGIK 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 513197508 265 PTGLFQGIKSVNPTFRGYSQQDAQEFLRCLMDLLHEELK 303
Cdd:cd02658   81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESF 119
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 606-728 1.67e-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: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 50.59  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508 606 CGRCKKLRNGVKFCKVQKFPEI----LCIHLKRF-------RHELMFSTKIGTHVSFPLEglDLQPFLAKDSPAQIVTYD 674
Cdd:cd02672  137 CDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTngefddiNVVLPSGKVMQNKVSPKAI--DHDKLVKNRGQESIYKYE 214

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 513197508 675 LLSVICH-HGTASSGHY----IAYCRNNLNNLWYEFDDQSVTEVSEStvqnaeAYVLFY 728
Cdd:cd02672  215 LVGYVCEiNDSSRGQHNvvfvIKVNEESTHGRWYLFNDFLVTPVSEL------AYILLY 267
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
606-710 4.10e-06

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 49.58  E-value: 4.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513197508  606 CGRCKKLRNGVKFCKVQKFPEILCIHLKRFRHElmFSTKIGTHVSFPLEgLDLQPFLAKDSPAQIVTYDLLSVICH-HGT 684
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPE-IGLTLSDDLQGDNEIVKYELRGVVVHiGDS 272

                          90       100       110
                  ....*....|....*....|....*....|...
gi 513197508  685 ASSGHYIAYCRNNLNNL-------WYEFDDQSV 710
Cdd:pfam13423 273 GTSGHLVSFVKVADSELedptesqWYLFNDFLV 305
 
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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