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Conserved domains on  [gi|1907149175|ref|XP_036018806|]
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ubiquitin carboxyl-terminal hydrolase 33 isoform X2 [Mus musculus]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 12031672)

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;
154-679 3.41e-71

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 236.18  E-value: 3.41e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 154 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPANLFQGIKTVN 230
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 231 PTFRGYSQQDAQEFLRCLMDLLHEELKeqvmemeeepqtltseetveeeksqsdvdfqscescsssekaenesgskgfpe 310
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 311 dsnettmliqdeddlemakdwqkekvcnkinkanadveldkdrdtvcetvdlnsqetvkvqihgrasesitdvhlndlat 390
Cdd:pfam00443     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 391 sqilpsnesvsprlsasppklgslwpglspphkkaqstsakrKKQHKKYRSVISDIFDGTVISSVQCLTCDRVSITLETF 470
Cdd:pfam00443 108 ------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPF 145
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 471 QDLSLPIPGKEDlaklhssshptivkagscgeayapqgwiaffmeyvkrfvvscvpswfWGPVVTLQDCLAAFFARDELK 550
Cdd:pfam00443 146 SDLSLPIPGDSA-----------------------------------------------ELKTASLQICFLQFSKLEELD 178
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 551 GDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKDSPAQIV---TYDLL 627
Cdd:pfam00443 179 DEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDYRLV 257
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907149175 628 SVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 679
Cdd:pfam00443 258 AVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
30-90 3.30e-18

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 79.23  E-value: 3.30e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907149175  30 CQDCKVRGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEV 90
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 ...
701-770 3.71e-17

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: 77.01  E-value: 3.71e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907149175  701 EPSLLQFYISRQWLNKFKTFAE------PGPISNNDFLCIHGGIPPRKASYIEDLVLMLPQNIWDNLYSRYGGGPA 770
Cdd:smart00695   3 EEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG 78
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
154-679 3.41e-71

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 236.18  E-value: 3.41e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 154 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPANLFQGIKTVN 230
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 231 PTFRGYSQQDAQEFLRCLMDLLHEELKeqvmemeeepqtltseetveeeksqsdvdfqscescsssekaenesgskgfpe 310
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 311 dsnettmliqdeddlemakdwqkekvcnkinkanadveldkdrdtvcetvdlnsqetvkvqihgrasesitdvhlndlat 390
Cdd:pfam00443     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 391 sqilpsnesvsprlsasppklgslwpglspphkkaqstsakrKKQHKKYRSVISDIFDGTVISSVQCLTCDRVSITLETF 470
Cdd:pfam00443 108 ------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPF 145
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 471 QDLSLPIPGKEDlaklhssshptivkagscgeayapqgwiaffmeyvkrfvvscvpswfWGPVVTLQDCLAAFFARDELK 550
Cdd:pfam00443 146 SDLSLPIPGDSA-----------------------------------------------ELKTASLQICFLQFSKLEELD 178
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 551 GDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKDSPAQIV---TYDLL 627
Cdd:pfam00443 179 DEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDYRLV 257
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907149175 628 SVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 679
Cdd:pfam00443 258 AVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
441-680 4.27e-63

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 211.38  E-value: 4.27e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 441 SVISDIFDGTVISSVQCLTCDRVSITLETFQDLSLPIPGKEDLAklhssshptivkagscgeayapqgwiaffmeyvkrf 520
Cdd:cd02674    38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 521 vvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKISTHV 600
Cdd:cd02674    82 -----------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 601 SFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYR 680
Cdd:cd02674   151 TFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
149-683 6.38e-46

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 177.00  E-value: 6.38e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 149 KARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCG---GLARTDKKP---AICKSYLKLMTELwHKSRPGSVVPANL 222
Cdd:COG5560   261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGF 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 223 FQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEEL----------KEQVMEMEEEPQTLTSEETVEEEKSQSD---VDFQS 289
Cdd:COG5560   340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLnriikkpytsKPDLSPGDDVVVKKKAKECWWEHLKRNDsiiTDLFQ 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 290 CESCSSSEKAENESGSKGFpEDSNETTMliqdedDLEMAKDWQKEKVCNKINKANADVELDKDRDTvcETVDLNSQETVK 369
Cdd:COG5560   420 GMYKSTLTCPGCGSVSITF-DPFMDLTL------PLPVSMVWKHTIVVFPESGRRQPLKIELDASS--TIRGLKKLVDAE 490
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 370 VQIHGRASESITDVHLN---------DLATSQILPSNESVsprLSASPPKLGSLWPGLSPPHKKAQSTsaKRKKQHKKYR 440
Cdd:COG5560   491 YGKLGCFEIKVMCIYYGgnynmlepaDKVLLQDIPQTDFV---YLYETNDNGIEVPVVHLRIEKGYKS--KRLFGDPFLQ 565
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 441 SVISD---IFDGTVISSVQCLTCDRVSITLETFQDLSLPIPGKEDLAklhSSSHPTIVKAGSCGEAYAPQGWIAFFMEYV 517
Cdd:COG5560   566 LNVLIkasIYDKLVKEFEELLVLVEMKKTDVDLVSEQVRLLREESSP---SSWLKLETEIDTKREEQVEEEGQMNFNDAV 642
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 518 --------KR--FVVSCVPSW------FWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCI 581
Cdd:COG5560   643 visceweeKRylSLFSYDPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILII 722
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 582 HLKRFRHELMFSTKISTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQS 660
Cdd:COG5560   723 HLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSR 800
                         570       580
                  ....*....|....*....|...
gi 1907149175 661 VTEVSESTVQNAEAYVLFYRKSS 683
Cdd:COG5560   801 ITEVDPEDSVTSSAYVLFYRRKS 823
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
30-90 3.30e-18

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 79.23  E-value: 3.30e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907149175  30 CQDCKVRGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEV 90
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
DUSP smart00695
Domain in ubiquitin-specific proteases;
701-770 3.71e-17

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 77.01  E-value: 3.71e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907149175  701 EPSLLQFYISRQWLNKFKTFAE------PGPISNNDFLCIHGGIPPRKASYIEDLVLMLPQNIWDNLYSRYGGGPA 770
Cdd:smart00695   3 EEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG 78
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
707-777 5.29e-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: 5.29e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907149175 707 FYISRQWLNKFKTFAE-----PGPISNNDFLCI--HGGIPPRKAsYIEDLVLmLPQNIWDNLYSRYGGGPAVNHLYIC 777
Cdd:pfam06337   5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLDDesNGQLKPNLQ-EGVDYVI-VPEEVWEFLVEWYGGGPEIKRNVVN 80
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
30-81 1.78e-09

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 53.91  E-value: 1.78e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907149175   30 CQDCKvRGPNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRV 81
Cdd:smart00290   2 CSVCG-TIENLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
154-679 3.41e-71

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 236.18  E-value: 3.41e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 154 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKP---AICKSYLKLMTELWHKSRPGSVVPANLFQGIKTVN 230
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNkdiNLLCALRDLFKALQKNSKSSSVSPKMFKKSLGKLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 231 PTFRGYSQQDAQEFLRCLMDLLHEELKeqvmemeeepqtltseetveeeksqsdvdfqscescsssekaenesgskgfpe 310
Cdd:pfam00443  81 PDFSGYKQQDAQEFLLFLLDGLHEDLN----------------------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 311 dsnettmliqdeddlemakdwqkekvcnkinkanadveldkdrdtvcetvdlnsqetvkvqihgrasesitdvhlndlat 390
Cdd:pfam00443     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 391 sqilpsnesvsprlsasppklgslwpglspphkkaqstsakrKKQHKKYRSVISDIFDGTVISSVQCLTCDRVSITLETF 470
Cdd:pfam00443 108 ------------------------------------------GNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPF 145
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 471 QDLSLPIPGKEDlaklhssshptivkagscgeayapqgwiaffmeyvkrfvvscvpswfWGPVVTLQDCLAAFFARDELK 550
Cdd:pfam00443 146 SDLSLPIPGDSA-----------------------------------------------ELKTASLQICFLQFSKLEELD 178
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 551 GDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKISTHVSFPLEgLDLQPFLAKDSPAQIV---TYDLL 627
Cdd:pfam00443 179 DEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELKPKTNnlqDYRLV 257
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907149175 628 SVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSEST-VQNAEAYVLFY 679
Cdd:pfam00443 258 AVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
441-680 4.27e-63

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 211.38  E-value: 4.27e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 441 SVISDIFDGTVISSVQCLTCDRVSITLETFQDLSLPIPGKEDLAklhssshptivkagscgeayapqgwiaffmeyvkrf 520
Cdd:cd02674    38 SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA------------------------------------ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 521 vvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKISTHV 600
Cdd:cd02674    82 -----------PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGSTRKLTTPV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 601 SFPLEGLDLQPFLAKDSPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYR 680
Cdd:cd02674   151 TFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
429-680 1.73e-54

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: 188.85  E-value: 1.73e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 429 SAKRKKQHKKYRSVISDIFDGTVISSVQCLTCDRVSITLETFQDLSLPIPGKEDlaklhssshptivkagscgeayapqg 508
Cdd:cd02257    43 SSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGL-------------------------- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 509 wiaffmeyvkrfvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKlRNGVKFCKVQKFPEILCIHLKRFRH 588
Cdd:cd02257    97 -----------------------PQVSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFSF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 589 -ELMFSTKISTHVSFPLEgLDLQPFLAK-----DSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFDDQSV 661
Cdd:cd02257   153 nEDGTKEKLNTKVSFPLE-LDLSPYLSEgekdsDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDKV 231
                         250       260
                  ....*....|....*....|....
gi 1907149175 662 TEVSESTVQ-----NAEAYVLFYR 680
Cdd:cd02257   232 TEVSEEEVLefgslSSSAYILFYE 255
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
154-679 4.16e-49

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: 175.54  E-value: 4.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 154 TGLKNIGNTCYMNAALQALSNCPPLTQFFLDcGGLARTDKKPAICKS-YLKLMTELWHKSRPGSVVPANLFQGIKTVNPT 232
Cdd:cd02661     2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLS-REHSKDCCNEGFCMMcALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 233 FRGYSQQDAQEFLRCLMDLLHeelkeqvmemeeepqtltseetveeeksqsdvdfqscescsssekaenesgskgfpeds 312
Cdd:cd02661    81 FRIGRQEDAHEFLRYLLDAMQ----------------------------------------------------------- 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 313 nettmliqdeddlemakdwqkeKVCnkinkanadveldkdrdtvcetvdlnsqetvkvqihgrasesitdvhlndlatsq 392
Cdd:cd02661   102 ----------------------KAC------------------------------------------------------- 104
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 393 iLPSNesvsprlsasppklgslwPGLSPPHKKAQSTSakrkkqhkkyrsVISDIFDGTVISSVQCLTCDRVSITLETFQD 472
Cdd:cd02661   105 -LDRF------------------KKLKAVDPSSQETT------------LVQQIFGGYLRSQVKCLNCKHVSNTYDPFLD 153
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 473 LSLPIPGkedlaklhssshptivkagscgeayapqgwiaffmeyvkrfvvscvpswfwgpVVTLQDCLAAFFARDELKGD 552
Cdd:cd02661   154 LSLDIKG-----------------------------------------------------ADSLEDALEQFTKPEQLDGE 180
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 553 NMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFrhELMFSTKISTHVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICH 632
Cdd:cd02661   181 NKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRF--SNFRGGKINKQISFPET-LDLSPYMS-QPNDGPLKYKLYAVLVH 256
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 1907149175 633 HGT-ASSGHYIAYCRnNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFY 679
Cdd:cd02661   257 SGFsPHSGHYYCYVK-SSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
155-679 4.51e-49

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: 176.41  E-value: 4.51e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 155 GLKNIGNTCYMNAALQALSNCPPLTQFFLD---CGGLARTDKKPAICKSYLKLMTELWHKSRPGSVVPANLFQGIKTVNP 231
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSdrhSCTCLSCSPNSCLSCAMDEIFQEFYYSGDRSPYGPINLLYLSWKHSR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 232 TFRGYSQQDAQEFLRCLMDLLHEELKeqvmemeeepqtltseetveeeksqsdvdfqscescsssekaenesgsKGFPED 311
Cdd:cd02660    82 NLAGYSQQDAHEFFQFLLDQLHTHYG------------------------------------------------GDKNEA 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 312 SNEttmliqdeddlemakdwqkeKVCNKInkanadveldkdrdtvcetvdlnsqetvkvqIHgrasesitdvhlndlats 391
Cdd:cd02660   114 NDE--------------------SHCNCI-------------------------------IH------------------ 124
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 392 qilpsnesvsprlsasppklgslwpglspphkkaqstsakrkkqhkkyrsvisDIFDGTVISSVQCLTCDRVSITLETFQ 471
Cdd:cd02660   125 -----------------------------------------------------QTFSGSLQSSVTCQRCGGVSTTVDPFL 151
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 472 DLSLPIPGKEDLAKLHSSSHPTIVKagscgeayapqgwiaffmeyvkrfvvscvpswfwgpvvTLQDCLAaFFARDELKG 551
Cdd:cd02660   152 DLSLDIPNKSTPSWALGESGVSGTP--------------------------------------TLSDCLD-RFTRPEKLG 192
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 552 DNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELM-FSTKISTHVSFPLEgLDLQPFLA--------KDSPAQIV 622
Cdd:cd02660   193 DFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNkTSRKIDTYVQFPLE-LNMTPYTSssigdtqdSNSLDPDY 271
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907149175 623 TYDLLSVICHHGTASSGHYIAYCRNNlNNLWYEFDDQSVTEVSESTVQNAEAYVLFY 679
Cdd:cd02660   272 TYDLFAVVVHKGTLDTGHYTAYCRQG-DGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
149-683 6.38e-46

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 177.00  E-value: 6.38e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 149 KARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCG---GLARTDKKP---AICKSYLKLMTELwHKSRPGSVVPANL 222
Cdd:COG5560   261 KEAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEyeeSINEENPLGmhgSVASAYADLIKQL-YDGNLHAFTPSGF 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 223 FQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEEL----------KEQVMEMEEEPQTLTSEETVEEEKSQSD---VDFQS 289
Cdd:COG5560   340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLnriikkpytsKPDLSPGDDVVVKKKAKECWWEHLKRNDsiiTDLFQ 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 290 CESCSSSEKAENESGSKGFpEDSNETTMliqdedDLEMAKDWQKEKVCNKINKANADVELDKDRDTvcETVDLNSQETVK 369
Cdd:COG5560   420 GMYKSTLTCPGCGSVSITF-DPFMDLTL------PLPVSMVWKHTIVVFPESGRRQPLKIELDASS--TIRGLKKLVDAE 490
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 370 VQIHGRASESITDVHLN---------DLATSQILPSNESVsprLSASPPKLGSLWPGLSPPHKKAQSTsaKRKKQHKKYR 440
Cdd:COG5560   491 YGKLGCFEIKVMCIYYGgnynmlepaDKVLLQDIPQTDFV---YLYETNDNGIEVPVVHLRIEKGYKS--KRLFGDPFLQ 565
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 441 SVISD---IFDGTVISSVQCLTCDRVSITLETFQDLSLPIPGKEDLAklhSSSHPTIVKAGSCGEAYAPQGWIAFFMEYV 517
Cdd:COG5560   566 LNVLIkasIYDKLVKEFEELLVLVEMKKTDVDLVSEQVRLLREESSP---SSWLKLETEIDTKREEQVEEEGQMNFNDAV 642
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 518 --------KR--FVVSCVPSW------FWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCI 581
Cdd:COG5560   643 visceweeKRylSLFSYDPLWtireigAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILII 722
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 582 HLKRFRHELMFSTKISTHVSFPLEGLDLQPFLA-KDSPAQIvtYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQS 660
Cdd:COG5560   723 HLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYmVDDPRLI--YDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSR 800
                         570       580
                  ....*....|....*....|...
gi 1907149175 661 VTEVSESTVQNAEAYVLFYRKSS 683
Cdd:COG5560   801 ITEVDPEDSVTSSAYVLFYRRKS 823
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
443-683 1.65e-37

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 143.55  E-value: 1.65e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 443 ISDIFDGTVISSVQCLTCDRVSITLETFQDLSLPIPGKEDLaklhssshptivkagscgeayapqgwiaffmeyvkrfvv 522
Cdd:cd02659   113 IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNL--------------------------------------- 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 523 scvpswfwgpvvtlQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRH--ELMFSTKISTHV 600
Cdd:cd02659   154 --------------EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFdfETMMRIKINDRF 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 601 SFPLEgLDLQPFLAKDSPAQIV----------TYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQ 670
Cdd:cd02659   220 EFPLE-LDMEPYTEKGLAKKEGdsekkdsesyIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAE 298
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907149175 671 NA----------------------EAYVLFYRKSS 683
Cdd:cd02659   299 EEcfggeetqktydsgprafkrttNAYMLFYERKS 333
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
440-680 2.48e-33

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 129.81  E-value: 2.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 440 RSVISDIFDGTVISSVQCLTCDRVSITLETFQDLSLPIPGKEDlaklhssshptivkagscgeayapqgwiaffmeyvkr 519
Cdd:cd02667    66 RTFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIK------------------------------------- 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 520 fvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRngvKFCKVQKFPEILCIHLKRFRHELMFST-KIST 598
Cdd:cd02667   109 ------------SECSIESCLKQFTEVEILEGNNKFACENCTKAK---KQYLISKLPPVLVIHLKRFQQPRSANLrKVSR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 599 HVSFPlEGLDLQPFL--------AKDSpaqiVTYDLLSVICHHGTASSGHYIAYCR-NNLNNL----------------- 652
Cdd:cd02667   174 HVSFP-EILDLAPFCdpkcnsseDKSS----VLYRLYGVVEHSGTMRSGHYVAYVKvRPPQQRlsdltkskpaadeagpg 248
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907149175 653 ---WYEFDDQSVTEVSESTVQNAEAYVLFYR 680
Cdd:cd02667   249 sgqWYYISDSDVREVSLEEVLKSEAYLLFYE 279
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
443-679 2.74e-31

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: 124.34  E-value: 2.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 443 ISDIFDGTVISSVQCLTCDRVSITLETFQDLSLPIPGkedlaklHSSshptivkagscgeayapqgwiaffmeyvkrfvv 522
Cdd:cd02663   109 VHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQ-------NTS--------------------------------- 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 523 scvpswfwgpvvtLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFS--TKISTHV 600
Cdd:cd02663   149 -------------ITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNryIKLFYRV 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 601 SFPLEgldLQPF-LAKDSPAQIVTYDLLSVICHHG-TASSGHYIAYCRNnlNNLWYEFDDQSVTEVSESTVQN------- 671
Cdd:cd02663   216 VFPLE---LRLFnTTDDAENPDRLYELVAVVVHIGgGPNHGHYVSIVKS--HGGWLLFDDETVEKIDENAVEEffgdspn 290

                  ....*....
gi 1907149175 672 -AEAYVLFY 679
Cdd:cd02663   291 qATAYVLFY 299
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
433-663 1.09e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 120.60  E-value: 1.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 433 KKQHKKYRSVISDIFDGTVISSVQCLTCDRVSITLETFQDLSLPIPGKEdlaklhssshptivkagscgeayapqgwiaf 512
Cdd:cd02668   108 KSKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHK------------------------------- 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 513 fmeyvkrfvvscvpswfwgpvvTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHEL-- 590
Cdd:cd02668   157 ----------------------TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRkt 214
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907149175 591 MFSTKISTHVSFPLEgLDLQPFLAkDSPAQIVTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFDDQSVTE 663
Cdd:cd02668   215 GAKKKLNASISFPEI-LDMGEYLA-ESDEGSYVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDVEE 286
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
447-679 1.70e-24

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: 103.21  E-value: 1.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 447 FDGTVISSVQCLTCDRVS-ITLETFQDLSLPIPGKedlaklhSSSHPTivkagscgeayapqgwiaffmeyvkrfvvscv 525
Cdd:cd02662    56 FDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQ-------SSGSGT-------------------------------- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 526 pswfwgpvvTLQDCLAAFFARDELKGdnmYSCEKCKklrngvkfCKVQKFPEILCIHLKRFR-HELMFSTKISTHVSFPL 604
Cdd:cd02662    97 ---------TLEHCLDDFLSTEIIDD---YKCDRCQ--------TVIVRLPQILCIHLSRSVfDGRGTSTKNSCKVSFPE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 605 egldlqpFLakdspaQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNL--------------------WYEFDDQSVTEV 664
Cdd:cd02662   157 -------RL------PKVLYRLRAVVVHYGSHSSGHYVCYRRKPLFSKdkepgsfvrmregpsstshpWWRISDTTVKEV 223
                         250
                  ....*....|....*.
gi 1907149175 665 SESTV-QNAEAYVLFY 679
Cdd:cd02662   224 SESEVlEQKSAYMLFY 239
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
441-680 1.65e-22

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: 99.49  E-value: 1.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 441 SVISDIFDGTVISSVQCLTCDRVSITLETFQDLSLpipgkedlaklhssshptivkagscgeayapqgwiaffmeyvkrf 520
Cdd:cd02664    97 TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL--------------------------------------------- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 521 vvsCVPSwfwgpvvtLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFR--HELMFSTKIST 598
Cdd:cd02664   132 ---SFPS--------VQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSydQKTHVREKIMD 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 599 HVSFPlEGLDL----------QPFLAKDSPA--------QIVTYDLLSVICHHGTAS-SGHYIAYCRN------------ 647
Cdd:cd02664   201 NVSIN-EVLSLpvrvesksseSPLEKKEEESgddgelvtRQVHYRLYAVVVHSGYSSeSGHYFTYARDqtdadstgqecp 279
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1907149175 648 --------NLNNLWYEFDDQSVTEVSESTVQNAE-------AYVLFYR 680
Cdd:cd02664   280 epkdaeenDESKNWYLFNDSRVTFSSFESVQNVTsrfpkdtPYILFYE 327
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
440-680 9.71e-22

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: 97.27  E-value: 9.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 440 RSVISDIFDGTVISSVQCLTCDRVSITLETFQDLSLPIPGKEDLAKLHSSSHPTIVKAgscgeayapqgwiaffmeyvkr 519
Cdd:cd02671   120 QELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESSEISPDPKT---------------------- 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 520 fvvscvpswfwgPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFS------ 593
Cdd:cd02671   178 ------------EMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFdcyggl 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 594 TKISTHVSFPlegLDLQPFLAKDSPAQIVtYDLLSVICHHG-TASSGHYIAYCRnnlnnlWYEFDDQSV---------TE 663
Cdd:cd02671   246 SKVNTPLLTP---LKLSLEEWSTKPKNDV-YRLFAVVMHSGaTISSGHYTAYVR------WLLFDDSEVkvteekdflEA 315
                         250
                  ....*....|....*..
gi 1907149175 664 VSESTVQNAEAYVLFYR 680
Cdd:cd02671   316 LSPNTSSTSTPYLLFYK 332
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
535-669 6.31e-19

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 92.24  E-value: 6.31e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175  535 TLQDCLAAFFARDELKGDNMYSCEK--CKKLRNGVKFckvQKFPEILCIHLKRFRHELMFST--KISTHVSFPLEgLDLQ 610
Cdd:COG5077    339 NLQESFRRYIQVETLDGDNRYNAEKhgLQDAKKGVIF---ESLPPVLHLQLKRFEYDFERDMmvKINDRYEFPLE-IDLL 414
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907149175  611 PFLAKD---SPAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV 669
Cdd:COG5077    415 PFLDRDadkSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEV 476
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
30-90 3.30e-18

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 79.23  E-value: 3.30e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907149175  30 CQDCKVRGpNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKEV 90
Cdd:pfam02148   1 CSLCGNTS-NLWLCLT--CGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYV 58
DUSP smart00695
Domain in ubiquitin-specific proteases;
701-770 3.71e-17

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 77.01  E-value: 3.71e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907149175  701 EPSLLQFYISRQWLNKFKTFAE------PGPISNNDFLCIHGGIPPRKASYIEDLVLMLPQNIWDNLYSRYGGGPA 770
Cdd:smart00695   3 EEGLTWYLISTRWYRQWADFVEgkdgkdPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRWYGGGPG 78
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
576-680 2.87e-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: 80.45  E-value: 2.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 576 PEILCIHLKRF--RHELMFSTKISTHVSFPLEgLDLQPFLakdSPAQIvtYDLLSVICHHG-TASSGHYIAYCRNNLNNL 652
Cdd:cd02657   197 PKYLTVQFVRFfwKRDIQKKAKILRKVKFPFE-LDLYELC---TPSGY--YELVAVITHQGrSADSGHYVAWVRRKNDGK 270
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907149175 653 WYEFDDQSVTEVSESTVQNAE-------AYVLFYR 680
Cdd:cd02657   271 WIKFDDDKVSEVTEEDILKLSgggdwhiAYILLYK 305
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
432-680 8.21e-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 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: 79.29  E-value: 8.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 432 RKKQHKKYRSVISDIFDGTVISSVQCLTCDRVSITLETFQDLSLPIPGKEDLAKLHSSshptivkagscgEAYAPqgwia 511
Cdd:cd02658   115 DRESFKNLGLNPNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDEATEKEEGE------------LVYEP----- 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 512 ffmeyvkrfvvscvpswfwgpvVTLQDCLAAFFARDELKgdnmYSCEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELM 591
Cdd:cd02658   178 ----------------------VPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLEN 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 592 F-STKISTHVSFPLEGLDlqpflakdspaqiVTYDLLSVICHHGT-ASSGHYIAYCRNNLNN--LWYEFDDQSVTEVSES 667
Cdd:cd02658   232 WvPKKLDVPIDVPEELGP-------------GKYELIAFISHKGTsVHSGHYVAHIKKEIDGegKWVLFNDEKVVASQDP 298
                         250
                  ....*....|...
gi 1907149175 668 TVQNAEAYVLFYR 680
Cdd:cd02658   299 PEMKKLGYIYFYQ 311
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
574-681 2.22e-15

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 77.54  E-value: 2.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 574 KFPEILCIHLKRFRHELMFsTKISTHVSFPLEgldlQPFLaKDSPAQIVT---YDLLSVICHHGTASSGHYIAYCRNnlN 650
Cdd:COG5533   178 KLPKILTIQLKRFANLGGN-QKIDTEVDEKFE----LPVK-HDQILNIVKetyYDLVGFVLHQGSLEGGHYIAYVKK--G 249
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907149175 651 NLWYEFDDQSVTEVSESTVQNA---EAYVLFYRK 681
Cdd:COG5533   250 GKWEKANDSDVTPVSEEEAINEkakNAYLYFYER 283
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
532-680 8.13e-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: 77.74  E-value: 8.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 532 PVVTLQDCLAAFFArdelkgdnmyscEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQP 611
Cdd:cd02669   301 PQVPLKQLLKKYDG------------KTETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSD 368
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907149175 612 FLAKDSPAQI--VTYDLLSVICHHGT-ASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYR 680
Cdd:cd02669   369 YVHFDKPSLNlsTKYNLVANIVHEGTpQEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
155-287 4.34e-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 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: 70.82  E-value: 4.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 155 GLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKPA--ICKSYLKLMTELWHKSRPgsVVPANLFQGIKTVNPT 232
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSdnLTNALRDLFDTMDKKQEP--VPPIEFLQLLRMAFPQ 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 233 F------RGYSQQDAQEFLRCLMDLLHEELK---------EQVMEMEEEPQTLTSEETVEEEKSQSDVDF 287
Cdd:cd02657    79 FaekqnqGGYAQQDAEECWSQLLSVLSQKLPgagskgsfiDQLFGIELETKMKCTESPDEEEVSTESEYK 148
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
707-777 5.29e-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: 5.29e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907149175 707 FYISRQWLNKFKTFAE-----PGPISNNDFLCI--HGGIPPRKAsYIEDLVLmLPQNIWDNLYSRYGGGPAVNHLYIC 777
Cdd:pfam06337   5 YLISSKWLNKWKSYVKepnnePGPIDNSDLLDDesNGQLKPNLQ-EGVDYVI-VPEEVWEFLVEWYGGGPEIKRNVVN 80
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
624-679 3.34e-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: 62.51  E-value: 3.34e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907149175 624 YDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTV------QNAEAYVLFY 679
Cdd:cd02666   281 YRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVflftlgNTATPYFLVY 342
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
155-351 8.99e-10

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 60.59  E-value: 8.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 155 GLKNIGNTCYMNAALQALS-NCPPLTQFFLDCGGLART-------DKKPAICKSYLKLMTELWHKSRPgsvvpanlfqgi 226
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEH------------ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 227 kTVNPTFRGYSQQDAQEFLRCLMDLLHEELKEQvmemeeepQTLTSEETVEEEKSQSDVD-FQSCESCSSSEKAENESGS 305
Cdd:COG5533    69 -KVGWIPPMGSQEDAHELLGKLLDELKLDLVNS--------FTIRIFKTTKDKKKTSTGDwFDIIIELPDQTWVNNLKTL 139
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907149175 306 KGFPEDSNEttmLIQDEDDLEmAKDWQKEKVCNKINKANADVELDK 351
Cdd:COG5533   140 QEFIDNMEE---LVDDETGVK-AKENEELEVQAKQEYEVSFVKLPK 181
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
30-81 1.78e-09

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 53.91  E-value: 1.78e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907149175   30 CQDCKvRGPNLWACLEnrCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRV 81
Cdd:smart00290   2 CSVCG-TIENLWLCLT--CGQVGCGRYQNGHALEHFEETGHPLVVKLGTQRV 50
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
557-679 4.68e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 57.92  E-value: 4.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 557 CEKCKKlRNGVKFCKVQKFPEILCIHLKRFRhelmFSTKISTHvsfplegldlqpfLAKDSPA------QIVTYDLLSVI 630
Cdd:cd02673   129 CSSCKC-ESAISSERIMTFPECLSINLKRYK----LRIATSDY-------------LKKNEEImkkycgTDAKYSLVAVI 190
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907149175 631 CHHG-TASSGHYIAYCRNNLN-NLWYEFDDQSVTEVSESTVQNA---EAYVLFY 679
Cdd:cd02673   191 CHLGeSPYDGHYIAYTKELYNgSSWLYCSDDEIRPVSKNDVSTNarsSGYLIFY 244
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
574-679 3.23e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 55.26  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 574 KFPEILCIHLKRFRHELMFSTKISTHVSFPLEgldlqpflakdspAQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLW 653
Cdd:cd02665   127 ELPPVLTFELSRFEFNQGRPEKIHDKLEFPQI-------------IQQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEW 193
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1907149175 654 YEFDDQSVTEVSESTVQ--------NAEAYVLFY 679
Cdd:cd02665   194 EKYNDISVTESSWEEVErdsfgggrNPSAYCLMY 227
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
519-680 6.00e-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: 54.46  E-value: 6.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 519 RFVVSCVPSWFWGPVVTLQDCLAAFFardelkgdnmyscekckklRNGVkfckVQKFPEILCIHLKRFRHELMFSTKIST 598
Cdd:cd02670    65 RLLQIPVPDDDDGGGITLEQCLEQYF-------------------NNSV----FAKAPSCLIICLKRYGKTEGKAQKMFK 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 599 HVsFPLEGLDLQPFLAKDSPA-------QIVTYD--------------LLSVICHHGTA-SSGHYIAYCRNN-------- 648
Cdd:cd02670   122 KI-LIPDEIDIPDFVADDPRAcskcqleCRVCYDdkdfsptcgkfklsLCSAVCHRGTSlETGHYVAFVRYGsysltetd 200
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1907149175 649 ---LNNLWYEFDD-------QSVTEVSESTVQnAEAYVLFYR 680
Cdd:cd02670   201 neaYNAQWVFFDDmadrdgvSNGFNIPAARLL-EDPYMLFYQ 241
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
557-679 2.35e-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: 239137 [Multi-domain]  Cd Length: 268  Bit Score: 52.90  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 557 CEKCKKLRNGVKFCKVQKFPEI----LCIHLKRF-------RHELMFSTKISTHVSFPLEglDLQPFLAKDSPAQIVTYD 625
Cdd:cd02672   137 CDTCCKYQPLEQTTSIRHLPDIlllvLVINLSVTngefddiNVVLPSGKVMQNKVSPKAI--DHDKLVKNRGQESIYKYE 214
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907149175 626 LLSVICH-HGTASSGHY----IAYCRNNLNNLWYEFDDQSVTEVSEStvqnaeAYVLFY 679
Cdd:cd02672   215 LVGYVCEiNDSSRGQHNvvfvIKVNEESTHGRWYLFNDFLVTPVSEL------AYILLY 267
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
557-661 4.96e-07

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 52.27  E-value: 4.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149175 557 CEKCKKLRNGVKFCKVQKFPEILCIHLKRFRHElmFSTKISTHVSFPLEgLDLQPFLAKDSPAQIVTYDLLSVICH-HGT 635
Cdd:pfam13423 196 CEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKTPGWLPPE-IGLTLSDDLQGDNEIVKYELRGVVVHiGDS 272
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907149175 636 ASSGHYIAYCRNNLNNL-------WYEFDDQSV 661
Cdd:pfam13423 273 GTSGHLVSFVKVADSELedptesqWYLFNDFLV 305
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
154-184 8.57e-03

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: 39.40  E-value: 8.57e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907149175 154 TGLKNIGNTCYMNAALQALSNCPPLTQFFLD 184
Cdd:cd02666     2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLN 32
 
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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