NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1720410365|ref|XP_030109769|]
View 

ubiquitin carboxyl-terminal hydrolase 45 isoform X3 [Mus musculus]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 13671465)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
192-388 2.14e-36

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.


The actual alignment was detected with superfamily member cd02667:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 279  Bit Score: 138.29  E-value: 2.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 192 GITNLGNTCFFNAVIQNLAQTYILFELMNEikedgtkfkislssapqleplvvelsspgpltsalflflhsmkeaekgpl 271
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE-------------------------------------------------- 30
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 272 SPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTeetkriqasilkafnnpttktaddetrkkvkaygkegvkmnFI 351
Cdd:cd02667    31 TPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLRT-----------------------------------------FI 69
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1720410365 352 DRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEE 388
Cdd:cd02667    70 DSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDE 106
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
587-720 3.37e-31

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.


The actual alignment was detected with superfamily member cd02667:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 279  Bit Score: 123.27  E-value: 3.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 587 CFSEGKHTRLHSAqnaFQTLS-QSYVTTSKECSVQSCLYQFTSMELLMGNNKLLCEDCTEkrrkchketssaekkaggvy 665
Cdd:cd02667    83 CESCGTVSLVYEP---FLDLSlPRSDEIKSECSIESCLKQFTEVEILEGNNKFACENCTK-------------------- 139
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720410365 666 tnARKQLLISAVPAILILHLKRFHQAGL-SLRKVNRHVDFPLTLDLAPFCAATCKV 720
Cdd:cd02667   140 --AKKQYLISKLPPVLVIHLKRFQQPRSaNLRKVSRHVSFPEILDLAPFCDPKCNS 193
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
192-713 7.25e-17

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


The actual alignment was detected with superfamily member COG5560:

Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 84.93  E-value: 7.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 192 GITNLGNTCFFNAVIQNLAQTYilfELMNEIKEDGTKFKISLSSapqlePLVVElsspGPLTSALFLFLHSMKEAEKGPL 271
Cdd:COG5560   267 GLRNLGNTCYMNSALQCLMHTW---ELRDYFLSDEYEESINEEN-----PLGMH----GSVASAYADLIKQLYDGNLHAF 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 272 SPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRtEETKRIQasILKAFNNPTTKTADDETRKKV-KAYGKEGVKMN- 349
Cdd:COG5560   335 TPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLH-EDLNRII--KKPYTSKPDLSPGDDVVVKKKaKECWWEHLKRNd 411
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 350 -FIDRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEERV-SKPVLLGKMSKCRSLQETDQDHNKGTVTVGNAHQPRA 427
Cdd:COG5560   412 sIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVwKHTIVVFPESGRRQPLKIELDASSTIRGLKKLVDAEY 491
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 428 SRKHSSPNDKNQLSHDR---------KHLRKWPSEEEKTVVTHPKNDNLEAspPASTLSTEA-----------SLNESLT 487
Cdd:COG5560   492 GKLGCFEIKVMCIYYGGnynmlepadKVLLQDIPQTDFVYLYETNDNGIEV--PVVHLRIEKgykskrlfgdpFLQLNVL 569
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 488 D-GSERDASLESSVDADSEASepeiASKQPVLLRSRGDSCGHAEQHP--HLPLASELPQAKEthggeeemaeaiaelhls 564
Cdd:COG5560   570 IkASIYDKLVKEFEELLVLVE----MKKTDVDLVSEQVRLLREESSPssWLKLETEIDTKRE------------------ 627
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 565 gtvtgnrDFHREKQPLNVPNNLCFsegkhTRLHSAQNAFQTLSQSYVTTSKEC-------SVQSCLYQFTSMELLMGNNK 637
Cdd:COG5560   628 -------EQVEEEGQMNFNDAVVI-----SCEWEEKRYLSLFSYDPLWTIREIgaaertiTLQDCLNEFSKPEQLGLSDS 695
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720410365 638 LLCEDCTEKRRkchketssaekkaggvytnARKQLLISAVPAILILHLKRFHQAGLSLRKVNRHVDFPLT-LDLAPF 713
Cdd:COG5560   696 WYCPGCKEFRQ-------------------ASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDdLDLSGV 753
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
62-132 6.88e-15

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 69.60  E-value: 6.88e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720410365  62 CSECLKERRfcdgqpvlpadVWLCLKCGLQGCGKNSESqHSLRHFKSSGtesHCVVISLSTWVIWCYECNE 132
Cdd:pfam02148   1 CSLCGNTSN-----------LWLCLTCGHVGCGRYQNS-HALEHYEETG---HPLAVNLSTLTVYCYPCDD 56
 
Name Accession Description Interval E-value
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-388 2.14e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 138.29  E-value: 2.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 192 GITNLGNTCFFNAVIQNLAQTYILFELMNEikedgtkfkislssapqleplvvelsspgpltsalflflhsmkeaekgpl 271
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE-------------------------------------------------- 30
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 272 SPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTeetkriqasilkafnnpttktaddetrkkvkaygkegvkmnFI 351
Cdd:cd02667    31 TPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLRT-----------------------------------------FI 69
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1720410365 352 DRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEE 388
Cdd:cd02667    70 DSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDE 106
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
587-720 3.37e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 123.27  E-value: 3.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 587 CFSEGKHTRLHSAqnaFQTLS-QSYVTTSKECSVQSCLYQFTSMELLMGNNKLLCEDCTEkrrkchketssaekkaggvy 665
Cdd:cd02667    83 CESCGTVSLVYEP---FLDLSlPRSDEIKSECSIESCLKQFTEVEILEGNNKFACENCTK-------------------- 139
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720410365 666 tnARKQLLISAVPAILILHLKRFHQAGL-SLRKVNRHVDFPLTLDLAPFCAATCKV 720
Cdd:cd02667   140 --AKKQYLISKLPPVLVIHLKRFQQPRSaNLRKVSRHVSFPEILDLAPFCDPKCNS 193
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
192-432 8.03e-22

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 96.74  E-value: 8.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 192 GITNLGNTCFFNAVIQNLAQTYILFELMNEIKEDGTKFKISLSSApqleplvvelsspgpLTSALFLFLHSMKEAEKG-P 270
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------------LLCALRDLFKALQKNSKSsS 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 271 LSPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTEEtkriqasilkafnNPTTKTADDetrkkvkaygkegvkmNF 350
Cdd:pfam00443  67 VSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDL-------------NGNHSTENE----------------SL 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 351 IDRIFIGELTSTVMCEECANISTMKDPFIDISLPIIE-ERVSKPVLLGKMSKCRSLQETDQDHNKGTVTVGNAHQpRASR 429
Cdd:pfam00443 118 ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGdSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQ-DAIK 196

                  ...
gi 1720410365 430 KHS 432
Cdd:pfam00443 197 QLK 199
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
192-713 7.25e-17

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 84.93  E-value: 7.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 192 GITNLGNTCFFNAVIQNLAQTYilfELMNEIKEDGTKFKISLSSapqlePLVVElsspGPLTSALFLFLHSMKEAEKGPL 271
Cdd:COG5560   267 GLRNLGNTCYMNSALQCLMHTW---ELRDYFLSDEYEESINEEN-----PLGMH----GSVASAYADLIKQLYDGNLHAF 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 272 SPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRtEETKRIQasILKAFNNPTTKTADDETRKKV-KAYGKEGVKMN- 349
Cdd:COG5560   335 TPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLH-EDLNRII--KKPYTSKPDLSPGDDVVVKKKaKECWWEHLKRNd 411
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 350 -FIDRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEERV-SKPVLLGKMSKCRSLQETDQDHNKGTVTVGNAHQPRA 427
Cdd:COG5560   412 sIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVwKHTIVVFPESGRRQPLKIELDASSTIRGLKKLVDAEY 491
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 428 SRKHSSPNDKNQLSHDR---------KHLRKWPSEEEKTVVTHPKNDNLEAspPASTLSTEA-----------SLNESLT 487
Cdd:COG5560   492 GKLGCFEIKVMCIYYGGnynmlepadKVLLQDIPQTDFVYLYETNDNGIEV--PVVHLRIEKgykskrlfgdpFLQLNVL 569
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 488 D-GSERDASLESSVDADSEASepeiASKQPVLLRSRGDSCGHAEQHP--HLPLASELPQAKEthggeeemaeaiaelhls 564
Cdd:COG5560   570 IkASIYDKLVKEFEELLVLVE----MKKTDVDLVSEQVRLLREESSPssWLKLETEIDTKRE------------------ 627
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 565 gtvtgnrDFHREKQPLNVPNNLCFsegkhTRLHSAQNAFQTLSQSYVTTSKEC-------SVQSCLYQFTSMELLMGNNK 637
Cdd:COG5560   628 -------EQVEEEGQMNFNDAVVI-----SCEWEEKRYLSLFSYDPLWTIREIgaaertiTLQDCLNEFSKPEQLGLSDS 695
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720410365 638 LLCEDCTEKRRkchketssaekkaggvytnARKQLLISAVPAILILHLKRFHQAGLSLRKVNRHVDFPLT-LDLAPF 713
Cdd:COG5560   696 WYCPGCKEFRQ-------------------ASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDdLDLSGV 753
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
62-132 6.88e-15

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 69.60  E-value: 6.88e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720410365  62 CSECLKERRfcdgqpvlpadVWLCLKCGLQGCGKNSESqHSLRHFKSSGtesHCVVISLSTWVIWCYECNE 132
Cdd:pfam02148   1 CSLCGNTSN-----------LWLCLTCGHVGCGRYQNS-HALEHYEETG---HPLAVNLSTLTVYCYPCDD 56
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
612-715 2.79e-11

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 65.16  E-value: 2.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 612 TTSKECSVQSCLYQFTSMELLMGNNKLLCEDCtekrrKCHKETSsaekkaggvytnarKQLLISAVPAILILHLKRFHQA 691
Cdd:pfam00443 157 AELKTASLQICFLQFSKLEELDDEEKYYCDKC-----GCKQDAI--------------KQLKISRLPPVLIIHLKRFSYN 217
                          90       100
                  ....*....|....*....|....
gi 1720410365 692 GLSLRKVNRHVDFPLTLDLAPFCA 715
Cdd:pfam00443 218 RSTWEKLNTEVEFPLELDLSRYLA 241
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
62-122 2.42e-06

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 45.05  E-value: 2.42e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720410365   62 CSECLkerrfcdgqpvLPADVWLCLKCGLQGCGkNSESQHSLRHFKSSGtesHCVVISLST 122
Cdd:smart00290   2 CSVCG-----------TIENLWLCLTCGQVGCG-RYQNGHALEHFEETG---HPLVVKLGT 47
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
618-713 9.66e-04

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 42.55  E-value: 9.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365  618 SVQSCLYQFTSMELLMGNNKLLCEDctekrrkcHKetssaekkaggvYTNARKQLLISAVPAILILHLKRFHQAGLS--L 695
Cdd:COG5077    339 NLQESFRRYIQVETLDGDNRYNAEK--------HG------------LQDAKKGVIFESLPPVLHLQLKRFEYDFERdmM 398
                           90
                   ....*....|....*...
gi 1720410365  696 RKVNRHVDFPLTLDLAPF 713
Cdd:COG5077    399 VKINDRYEFPLEIDLLPF 416
 
Name Accession Description Interval E-value
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-388 2.14e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 138.29  E-value: 2.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 192 GITNLGNTCFFNAVIQNLAQTYILFELMNEikedgtkfkislssapqleplvvelsspgpltsalflflhsmkeaekgpl 271
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE-------------------------------------------------- 30
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 272 SPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTeetkriqasilkafnnpttktaddetrkkvkaygkegvkmnFI 351
Cdd:cd02667    31 TPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDGLRT-----------------------------------------FI 69
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1720410365 352 DRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEE 388
Cdd:cd02667    70 DSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDE 106
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
587-720 3.37e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 123.27  E-value: 3.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 587 CFSEGKHTRLHSAqnaFQTLS-QSYVTTSKECSVQSCLYQFTSMELLMGNNKLLCEDCTEkrrkchketssaekkaggvy 665
Cdd:cd02667    83 CESCGTVSLVYEP---FLDLSlPRSDEIKSECSIESCLKQFTEVEILEGNNKFACENCTK-------------------- 139
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720410365 666 tnARKQLLISAVPAILILHLKRFHQAGL-SLRKVNRHVDFPLTLDLAPFCAATCKV 720
Cdd:cd02667   140 --AKKQYLISKLPPVLVIHLKRFQQPRSaNLRKVSRHVSFPEILDLAPFCDPKCNS 193
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
192-432 8.03e-22

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 96.74  E-value: 8.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 192 GITNLGNTCFFNAVIQNLAQTYILFELMNEIKEDGTKFKISLSSApqleplvvelsspgpLTSALFLFLHSMKEAEKG-P 270
Cdd:pfam00443   2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---------------LLCALRDLFKALQKNSKSsS 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 271 LSPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTEEtkriqasilkafnNPTTKTADDetrkkvkaygkegvkmNF 350
Cdd:pfam00443  67 VSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDL-------------NGNHSTENE----------------SL 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 351 IDRIFIGELTSTVMCEECANISTMKDPFIDISLPIIE-ERVSKPVLLGKMSKCRSLQETDQDHNKGTVTVGNAHQpRASR 429
Cdd:pfam00443 118 ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGdSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQ-DAIK 196

                  ...
gi 1720410365 430 KHS 432
Cdd:pfam00443 197 QLK 199
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
192-713 7.25e-17

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 84.93  E-value: 7.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 192 GITNLGNTCFFNAVIQNLAQTYilfELMNEIKEDGTKFKISLSSapqlePLVVElsspGPLTSALFLFLHSMKEAEKGPL 271
Cdd:COG5560   267 GLRNLGNTCYMNSALQCLMHTW---ELRDYFLSDEYEESINEEN-----PLGMH----GSVASAYADLIKQLYDGNLHAF 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 272 SPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRtEETKRIQasILKAFNNPTTKTADDETRKKV-KAYGKEGVKMN- 349
Cdd:COG5560   335 TPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLH-EDLNRII--KKPYTSKPDLSPGDDVVVKKKaKECWWEHLKRNd 411
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 350 -FIDRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEERV-SKPVLLGKMSKCRSLQETDQDHNKGTVTVGNAHQPRA 427
Cdd:COG5560   412 sIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVwKHTIVVFPESGRRQPLKIELDASSTIRGLKKLVDAEY 491
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 428 SRKHSSPNDKNQLSHDR---------KHLRKWPSEEEKTVVTHPKNDNLEAspPASTLSTEA-----------SLNESLT 487
Cdd:COG5560   492 GKLGCFEIKVMCIYYGGnynmlepadKVLLQDIPQTDFVYLYETNDNGIEV--PVVHLRIEKgykskrlfgdpFLQLNVL 569
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 488 D-GSERDASLESSVDADSEASepeiASKQPVLLRSRGDSCGHAEQHP--HLPLASELPQAKEthggeeemaeaiaelhls 564
Cdd:COG5560   570 IkASIYDKLVKEFEELLVLVE----MKKTDVDLVSEQVRLLREESSPssWLKLETEIDTKRE------------------ 627
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 565 gtvtgnrDFHREKQPLNVPNNLCFsegkhTRLHSAQNAFQTLSQSYVTTSKEC-------SVQSCLYQFTSMELLMGNNK 637
Cdd:COG5560   628 -------EQVEEEGQMNFNDAVVI-----SCEWEEKRYLSLFSYDPLWTIREIgaaertiTLQDCLNEFSKPEQLGLSDS 695
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720410365 638 LLCEDCTEKRRkchketssaekkaggvytnARKQLLISAVPAILILHLKRFHQAGLSLRKVNRHVDFPLT-LDLAPF 713
Cdd:COG5560   696 WYCPGCKEFRQ-------------------ASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDdLDLSGV 753
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
618-713 1.15e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 78.47  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 618 SVQSCLYQFTSMELLMGNNKLLCEDCTEKrrkchketssaekkaggvyTNARKQLLISAVPAILILHLKRFhqAGLSLRK 697
Cdd:cd02661   163 SLEDALEQFTKPEQLDGENKYKCERCKKK-------------------VKASKQLTIHRAPNVLTIHLKRF--SNFRGGK 221
                          90
                  ....*....|....*.
gi 1720410365 698 VNRHVDFPLTLDLAPF 713
Cdd:cd02661   222 INKQISFPETLDLSPY 237
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
62-132 6.88e-15

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 69.60  E-value: 6.88e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720410365  62 CSECLKERRfcdgqpvlpadVWLCLKCGLQGCGKNSESqHSLRHFKSSGtesHCVVISLSTWVIWCYECNE 132
Cdd:pfam02148   1 CSLCGNTSN-----------LWLCLTCGHVGCGRYQNS-HALEHYEETG---HPLAVNLSTLTVYCYPCDD 56
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
611-719 1.43e-14

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: 74.06  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 611 VTTSKECSVQSCLYQFTSMELLMGNNKLLCEdctekrrkchketssaekkaGGVYTNARKQLLISAVPAILILHLKRFHQ 690
Cdd:cd02257    93 VKGLPQVSLEDCLEKFFKEEILEGDNCYKCE--------------------KKKKQEATKRLKIKKLPPVLIIHLKRFSF 152
                          90       100       110
                  ....*....|....*....|....*....|
gi 1720410365 691 AGL-SLRKVNRHVDFPLTLDLAPFCAATCK 719
Cdd:cd02257   153 NEDgTKEKLNTKVSFPLELDLSPYLSEGEK 182
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
615-720 8.34e-14

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 71.55  E-value: 8.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 615 KECSVQSCLYQFTSMELLMGNNKLLCEDCTEKRrkchketssaekkaggvytNARKQLLISAVPAILILHLKRFHQAGLS 694
Cdd:cd02674    82 PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKR-------------------KATKKLTISRLPKVLIIHLKRFSFSRGS 142
                          90       100
                  ....*....|....*....|....*..
gi 1720410365 695 LRKVNRHVDFPLT-LDLAPFCAATCKV 720
Cdd:cd02674   143 TRKLTTPVTFPLNdLDLTPYVDTRSFT 169
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
191-393 3.33e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 71.25  E-value: 3.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 191 KGITNLGNTCFFNAVIQNLAQTYILFE-LMNEIKEDGTKFKISLSSAP-QLEPLVVELSSPGpltsalflflhsmkeaEK 268
Cdd:cd02660     1 RGLINLGATCFMNVILQALLHNPLLRNyFLSDRHSCTCLSCSPNSCLScAMDEIFQEFYYSG----------------DR 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 269 GPLSPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTEETKRiqasilkafnnpttktaddetrkkVKAYGKEGVKM 348
Cdd:cd02660    65 SPYGPINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGD------------------------KNEANDESHCN 120
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720410365 349 NFIDRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEERVSKP 393
Cdd:cd02660   121 CIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSW 165
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
188-392 9.38e-12

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: 66.84  E-value: 9.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 188 PSVKGITNLGNTCFFNAVIQNLaqtyilfELMNEIKEdGTKFKISL-SSAPQLEplvvelsspgpltsALFLFLHSMKEA 266
Cdd:cd02671    22 LPFVGLNNLGNTCYLNSVLQVL-------YFCPGFKH-GLKHLVSLiSSVEQLQ--------------SSFLLNPEKYND 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 267 EKGPLSPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRteetkriqasilkafnnpttktaddetrkkvkaygkegv 346
Cdd:cd02671    80 ELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQ--------------------------------------- 120
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1720410365 347 kmNFIDRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEERVSK 392
Cdd:cd02671   121 --ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSK 164
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
618-714 1.02e-11

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 66.90  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 618 SVQSCLYQFTSMELLMGNNKLLCEDCTEKRRkchketssaekkaggvytnARKQLLISAVPAILILHLKRFHQAGLSLR- 696
Cdd:cd02659   152 NLEESLDAYVQGETLEGDNKYFCEKCGKKVD-------------------AEKGVCFKKLPPVLTLQLKRFEFDFETMMr 212
                          90
                  ....*....|....*....
gi 1720410365 697 -KVNRHVDFPLTLDLAPFC 714
Cdd:cd02659   213 iKINDRFEFPLELDMEPYT 231
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
620-716 1.93e-11

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 65.86  E-value: 1.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 620 QSCLYQFTSMELLmGNNKLLCEDCtekrrkchketssaekkagGVYTNARKQLLISAVPAILILHLKRF-HQAGLSLRKV 698
Cdd:cd02660   179 SDCLDRFTRPEKL-GDFAYKCSGC-------------------GSTQEATKQLSIKKLPPVLCFQLKRFeHSLNKTSRKI 238
                          90
                  ....*....|....*...
gi 1720410365 699 NRHVDFPLTLDLAPFCAA 716
Cdd:cd02660   239 DTYVQFPLELNMTPYTSS 256
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
612-715 2.79e-11

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 65.16  E-value: 2.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 612 TTSKECSVQSCLYQFTSMELLMGNNKLLCEDCtekrrKCHKETSsaekkaggvytnarKQLLISAVPAILILHLKRFHQA 691
Cdd:pfam00443 157 AELKTASLQICFLQFSKLEELDDEEKYYCDKC-----GCKQDAI--------------KQLKISRLPPVLIIHLKRFSYN 217
                          90       100
                  ....*....|....*....|....
gi 1720410365 692 GLSLRKVNRHVDFPLTLDLAPFCA 715
Cdd:pfam00443 218 RSTWEKLNTEVEFPLELDLSRYLA 241
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-407 7.55e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 60.79  E-value: 7.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 192 GITNLGNTCFFNAVIQNLAQTYILfelmneikedgtkfkislssapqleplvvelsspgpltSALFLFLHSMKEAEK--G 269
Cdd:cd02663     1 GLENFGNTCYCNSVLQALYFENLL--------------------------------------TCLKDLFESISEQKKrtG 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 270 PLSPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLdavrteetkriqasilkafnNPTTKTADDEtRKKVKAYGKEGVKM- 348
Cdd:cd02663    43 VISPKKFITRLKRENELFDNYMHQDAHEFLNFLL--------------------NEIAEILDAE-RKAEKANRKLNNNNn 101
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720410365 349 -----NFIDRIFIGELTSTVMCEECANISTMKDPFIDISLPiIEERVSKPVLLGKMS--------------KCRSLQE 407
Cdd:cd02663   102 aepqpTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSID-VEQNTSITSCLRQFSatetlcgrnkfycdECCSLQE 178
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
192-385 7.85e-10

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: 60.19  E-value: 7.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 192 GITNLGNTCFFNAVIQNLAqtyilfelmneikedgtkfkislssapqleplvvelsspgpltsalflflhsmkeaekgpl 271
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALF------------------------------------------------------------- 19
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 272 spkvlfnqlcqkaprfkgFQQQDSQELLHHLLDAVRTEETKRIQASILKAFNNpttktaddetrkkvkaygkegvkmNFI 351
Cdd:cd02257    20 ------------------SEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLK------------------------SLI 57
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1720410365 352 DRIFIGELTSTVMCEECANISTMKDPFIDISLPI 385
Cdd:cd02257    58 HDLFGGKLESTIVCLECGHESVSTEPELFLSLPL 91
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-406 1.01e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 60.58  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 192 GITNLGNTCFFNAVIQNLAQT-YILFELMNEIKEDGtkfkislssAPQLEPLVVELSspgpltsaLFLFLHSMKEAEKGP 270
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAkDFRRQVLSLNLPRL---------GDSQSVMKKLQL--------LQAHLMHTQRRAEAP 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 271 lsPKVLFNQlcQKAPRFKGFQQQDSQELLHHLLDAVRTeetkriqasilkafnnpttktaddetrkkvkaygkegvkmnF 350
Cdd:cd02664    64 --PDYFLEA--SRPPWFTPGSQQDCSEYLRYLLDRLHT-----------------------------------------L 98
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720410365 351 IDRIFIGELTSTVMCEECANISTMKD--PFIDISLP----IIEERVSKPVLLGK----MSKCRSLQ 406
Cdd:cd02664    99 IEKMFGGKLSTTIRCLNCNSTSARTErfRDLDLSFPsvqdLLNYFLSPEKLTGDnqyyCEKCASLQ 164
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-376 1.06e-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 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: 60.42  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 192 GITNLGNTCFFNAVIQNLaqtyilfELMNEIKEDGTKFKISLSSAPQleplvvelsSPGPLTSALFLFLHSMKEAEKgPL 271
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCL-------RSVPELRDALKNYNPARRGANQ---------SSDNLTNALRDLFDTMDKKQE-PV 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 272 SPKVLFNQLCQKAPRFK------GFQQQDSQELLhhlldavrteetkriqASILKAFNNpttktaddetrkkvkAYGKEG 345
Cdd:cd02657    64 PPIEFLQLLRMAFPQFAekqnqgGYAQQDAEECW----------------SQLLSVLSQ---------------KLPGAG 112
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1720410365 346 VKMNFIDRIFIGELTSTVMCEECANISTMKD 376
Cdd:cd02657   113 SKGSFIDQLFGIELETKMKCTESPDEEEVST 143
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-385 1.55e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 59.98  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 192 GITNLGNTCFFNAVIQNLAQT-----YIL-FELMNEIKEDGtkFKISlssapqleplvvelsspgpltSALFLFLHSMKE 265
Cdd:cd02661     3 GLQNLGNTCFLNSVLQCLTHTpplanYLLsREHSKDCCNEG--FCMM---------------------CALEAHVERALA 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 266 AEKGPLSPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAvrteetkrIQASILKAFNNpttktaDDETRKKVKAYgkeg 345
Cdd:cd02661    60 SSGPGSAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDA--------MQKACLDRFKK------LKAVDPSSQET---- 121
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720410365 346 vkmNFIDRIFIGELTSTVMCEECANISTMKDPFIDISLPI 385
Cdd:cd02661   122 ---TLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDI 158
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-407 2.45e-09

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 59.58  E-value: 2.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 192 GITNLGNTCFFNAVIQNLAQT----YILFELMNEIKEDGTKfkiSLSSAPQLeplvvelsspgpltsaLFLFLHSMKEAE 267
Cdd:cd02659     4 GLKNQGATCYMNSLLQQLYMTpefrNAVYSIPPTEDDDDNK---SVPLALQR----------------LFLFLQLSESPV 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 268 KGPlSPKVLFNQLCQKAprFKGFQQQDSQELLHHLLDAVRTeetkriqasilkafnnpttktaddetrkKVKAYGKEGVk 347
Cdd:cd02659    65 KTT-ELTDKTRSFGWDS--LNTFEQHDVQEFFRVLFDKLEE----------------------------KLKGTGQEGL- 112
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 348 mnfIDRIFIGELTSTVMCEECANISTMKDPFIDISLPIieervskpvllgkmSKCRSLQE 407
Cdd:cd02659   113 ---IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAV--------------KGKKNLEE 155
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
615-710 9.46e-09

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 57.32  E-value: 9.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 615 KECSVQSCLYQFTSMELLMGNNKLLCEDCtekrrKCHKEtssaekkaggvytnARKQLLISAVPAILILHLKRFHQAGls 694
Cdd:cd02663   145 QNTSITSCLRQFSATETLCGRNKFYCDEC-----CSLQE--------------AEKRMKIKKLPKILALHLKRFKYDE-- 203
                          90       100
                  ....*....|....*....|..
gi 1720410365 695 lrKVNRH------VDFPLTLDL 710
Cdd:cd02663   204 --QLNRYiklfyrVVFPLELRL 223
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
618-715 2.10e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 53.58  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 618 SVQSCLYQFTSMELLMGNNKLLCEDCTEKRrkchketssaekkaggvytNARKQLLISAVPAILILHLKR--FHQAGLSL 695
Cdd:cd02668   157 TLEECIDEFLKEEQLTGDNQYFCESCNSKT-------------------DATRRIRLTTLPPTLNFQLLRfvFDRKTGAK 217
                          90       100
                  ....*....|....*....|
gi 1720410365 696 RKVNRHVDFPLTLDLAPFCA 715
Cdd:cd02668   218 KKLNASISFPEILDMGEYLA 237
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-393 2.02e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 49.59  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 192 GITNLGNTCFFNAVIQNLAQtyilfelmneikedgtkfkislssapqleplvvelsspgpltsalflflhsmkeaekgpl 271
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 272 spkvlfnqlcqkaprfkgfQQQDSQELLHHLLDAVRteetkriqasilkafnnpttktaddetrkkvkaygkegvkmNFI 351
Cdd:cd02674    21 -------------------DQQDAQEFLLFLLDGLH-----------------------------------------SII 40
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720410365 352 DRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEERVSKP 393
Cdd:cd02674    41 VDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAP 82
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
62-122 2.42e-06

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 45.05  E-value: 2.42e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720410365   62 CSECLkerrfcdgqpvLPADVWLCLKCGLQGCGkNSESQHSLRHFKSSGtesHCVVISLST 122
Cdd:smart00290   2 CSVCG-----------TIENLWLCLTCGQVGCG-RYQNGHALEHFEETG---HPLVVKLGT 47
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
625-710 9.17e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 48.35  E-value: 9.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 625 QFTSMELLMGNNKLLCEDCTEkrrkchketssaekkaggvYTNARKQLLISAVPAILILHLKRFHQAGLS------LRKV 698
Cdd:cd02671   188 QFASVERIVGEDKYFCENCHH-------------------YTEAERSLLFDKLPEVITIHLKCFAANGSEfdcyggLSKV 248
                          90
                  ....*....|..
gi 1720410365 699 NRHVDFPLTLDL 710
Cdd:cd02671   249 NTPLLTPLKLSL 260
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-385 1.92e-04

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 44.33  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 192 GITNLGNTCFFNAVIQnlaqtyILFelMN-EIKEDGTKFKISLSSAPQLEPLVVELSSPGPLTSALFLFLHsMKEAEKGP 270
Cdd:cd02668     1 GLKNLGATCYVNSFLQ------LWF--MNlEFRKAVYECNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQ-LQFGNRSV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 271 LSPKVLFNQLcqkapRFKGFQQQDSQELLHHLLDAvrteetkrIQASILKAFNNpttktaddetrkKVKaygkegvkmNF 350
Cdd:cd02668    72 VDPSGFVKAL-----GLDTGQQQDAQEFSKLFLSL--------LEAKLSKSKNP------------DLK---------NI 117
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1720410365 351 IDRIFIGELTSTVMCEECANISTMKDPFIDISLPI 385
Cdd:cd02668   118 VQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL 152
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
653-718 2.70e-04

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 43.47  E-value: 2.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720410365 653 ETSSAEKKAGGVYTnarKQLLISAVPAILILHLKRFHQAGLSLR--KVNRHVDFPLTLDLAPFCAATC 718
Cdd:cd02657   175 EKHSPTLGRDAIYT---KTSRISRLPKYLTVQFVRFFWKRDIQKkaKILRKVKFPFELDLYELCTPSG 239
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
617-710 4.40e-04

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 42.86  E-value: 4.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 617 CSVQSCLYQFTSMELLMGNNKLLCEDCtekRRKChketssaekkaggvytNARKQLLISAVPAILILHLKRFH--QAGLS 694
Cdd:cd02664   134 PSVQDLLNYFLSPEKLTGDNQYYCEKC---ASLQ----------------DAEKEMKVTGAPEYLILTLLRFSydQKTHV 194
                          90
                  ....*....|....*.
gi 1720410365 695 LRKVNRHVDFPLTLDL 710
Cdd:cd02664   195 REKIMDNVSINEVLSL 210
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
618-713 9.66e-04

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 42.55  E-value: 9.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365  618 SVQSCLYQFTSMELLMGNNKLLCEDctekrrkcHKetssaekkaggvYTNARKQLLISAVPAILILHLKRFHQAGLS--L 695
Cdd:COG5077    339 NLQESFRRYIQVETLDGDNRYNAEK--------HG------------LQDAKKGVIFESLPPVLHLQLKRFEYDFERdmM 398
                           90
                   ....*....|....*...
gi 1720410365  696 RKVNRHVDFPLTLDLAPF 713
Cdd:COG5077    399 VKINDRYEFPLEIDLLPF 416
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
192-309 2.71e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 39.85  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410365 192 GITNLGNTCFFNAVIQnlaqtyILFELMNEIKEDGTKFKISLSSAPQLEplvVELSSPGPLTsalflfLHSMKEAEKGP- 270
Cdd:cd02665     1 GLKNVGNTCWFSAVIQ------SLFSQQQDVSEFTHLLLDWLEDAFQAA---AEAISPGEKS------KNPMVQLFYGTf 65
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1720410365 271 LSPKVLFNQLCQKAPRFKGFQ-QQDSQELLHHLLDAVRTE 309
Cdd:cd02665    66 LTEGVLEGKPFCNCETFGQYPlQVNGYGNLHECLEAAMFE 105
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH