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Conserved domains on  [gi|1046904076|ref|XP_017451900|]
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ubiquitin carboxyl-terminal hydrolase 49 isoform X1 [Rattus norvegicus]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 12031653)

ubiquitin carboxyl-terminal hydrolase catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin on target proteins; belongs to the peptidase C19 family

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
250-651 7.19e-71

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 232.72  E-value: 7.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 250 TGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSTSehlfpqatngkaqipsrpasstaagfsvrsdraqgfepqgfcw 329
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSE------------------------------------------- 37
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 330 ssgasisrsleliqnKEPSSKHISLCHELHTLFRVMWSGKW-ALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKV 408
Cdd:pfam00443  38 ---------------DSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGL 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 409 QQELESEGSTRRILIpfsqrkltkqvlkvVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFPERYHCVEkgfvplnq 488
Cdd:pfam00443 103 HEDLNGNHSTENESL--------------ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELK-------- 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 489 tECLLTEMLAKFTETEALEGRI-YACDQCNSKRrksnpkplvlsEARKQLMIYRLPQVLRLHLKRFRWSgRNHREKIGVH 567
Cdd:pfam00443 161 -TASLQICFLQFSKLEELDDEEkYYCDKCGCKQ-----------DAIKQLKISRLPPVLIIHLKRFSYN-RSTWEKLNTE 227
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 568 VVFDQVLTMEPYCCGDmLSSLDKDTFAYDLSAVVMHHGkGFGSGHYTAYCYNTEGGFWVHCNDSKLDVCSVE-EVCKTQA 646
Cdd:pfam00443 228 VEFPLELDLSRYLAEE-LKPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEEtAVLSSSA 305

                  ....*
gi 1046904076 647 YILFY 651
Cdd:pfam00443 306 YILFY 310
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
26-87 4.58e-23

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 92.71  E-value: 4.58e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046904076  26 CLECATTESAWACLKCSHVACGRYIEDHALKHFEETGHPLAMEVRDLYVFCYLCKDYVLNDN 87
Cdd:pfam02148   1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
250-651 7.19e-71

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 232.72  E-value: 7.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 250 TGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSTSehlfpqatngkaqipsrpasstaagfsvrsdraqgfepqgfcw 329
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSE------------------------------------------- 37
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 330 ssgasisrsleliqnKEPSSKHISLCHELHTLFRVMWSGKW-ALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKV 408
Cdd:pfam00443  38 ---------------DSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGL 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 409 QQELESEGSTRRILIpfsqrkltkqvlkvVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFPERYHCVEkgfvplnq 488
Cdd:pfam00443 103 HEDLNGNHSTENESL--------------ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELK-------- 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 489 tECLLTEMLAKFTETEALEGRI-YACDQCNSKRrksnpkplvlsEARKQLMIYRLPQVLRLHLKRFRWSgRNHREKIGVH 567
Cdd:pfam00443 161 -TASLQICFLQFSKLEELDDEEkYYCDKCGCKQ-----------DAIKQLKISRLPPVLIIHLKRFSYN-RSTWEKLNTE 227
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 568 VVFDQVLTMEPYCCGDmLSSLDKDTFAYDLSAVVMHHGkGFGSGHYTAYCYNTEGGFWVHCNDSKLDVCSVE-EVCKTQA 646
Cdd:pfam00443 228 VEFPLELDLSRYLAEE-LKPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEEtAVLSSSA 305

                  ....*
gi 1046904076 647 YILFY 651
Cdd:pfam00443 306 YILFY 310
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
251-652 2.24e-62

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 210.69  E-value: 2.24e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLnldpstsehlfpqatngkaqipsrpasstaagfsvrSDRAQGFepqgfcws 330
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFL------------------------------------SDRHSCT-------- 37
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 331 sgasisrsleliqNKEPSSKHiSLCHELHTLFRVMW-SGKWALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKVQ 409
Cdd:cd02660    38 -------------CLSCSPNS-CLSCAMDEIFQEFYySGDRSPYGPINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLH 103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 410 QElesegSTRRILIPFSqrklTKQVLKVVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFPERYHCVEKGFVPLNQT 489
Cdd:cd02660   104 TH-----YGGDKNEAND----ESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGESGVSG 174
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 490 ECLLTEMLAKFTETEALEGRIYACDQCNSKrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFRWSGRNHREKIGVHVV 569
Cdd:cd02660   175 TPTLSDCLDRFTRPEKLGDFAYKCSGCGST-----------QEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQ 243
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 570 FDQVLTMEPYC----CGDMLSSLDKDTFAYDLSAVVMHHGKgFGSGHYTAYCYNtEGGFWVHCNDSKLDVCSVEEVCKTQ 645
Cdd:cd02660   244 FPLELNMTPYTsssiGDTQDSNSLDPDYTYDLFAVVVHKGT-LDTGHYTAYCRQ-GDGQWFKFDDAMITRVSEEEVLKSQ 321

                  ....*..
gi 1046904076 646 AYILFYT 652
Cdd:cd02660   322 AYLLFYH 328
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
26-87 4.58e-23

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 92.71  E-value: 4.58e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046904076  26 CLECATTESAWACLKCSHVACGRYIEDHALKHFEETGHPLAMEVRDLYVFCYLCKDYVLNDN 87
Cdd:pfam02148   1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
248-655 1.48e-21

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 99.96  E-value: 1.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 248 GVTGLRNLGNTCYMNSILQVLSHLQKFRECFLnldpstsehlfpqatngkaqipsrpasstaagfsvrSDraqGFEPQgf 327
Cdd:COG5560   264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFL------------------------------------SD---EYEES-- 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 328 cwssgasisrslelIQNKEPSSKHISLCHELHTLFRVMWSGKWALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLC----- 402
Cdd:COG5560   303 --------------INEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAflldg 368
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 403 --ELLHKVQQELESEGSTRRILIPFSQRKLTKQVLK--------VVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSL-- 470
Cdd:COG5560   369 lhEDLNRIIKKPYTSKPDLSPGDDVVVKKKAKECWWehlkrndsIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLpl 448
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 471 --------------------------------------------------------------------------EFPERY 476
Cdd:COG5560   449 pvsmvwkhtivvfpesgrrqplkieldasstirglkklvdaeygklgcfeikvmciyyggnynmlepadkvllqDIPQTD 528
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 477 HCVEKG----------------------------FVPLN----------------------------------QTECLLT 494
Cdd:COG5560   529 FVYLYEtndngievpvvhlriekgykskrlfgdpFLQLNvlikasiydklvkefeellvlvemkktdvdlvseQVRLLRE 608
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 495 EM----------------------------------------------------------------------LAKFTETE 504
Cdd:COG5560   609 ESspsswlkleteidtkreeqveeegqmnfndavvisceweekrylslfsydplwtireigaaertitlqdcLNEFSKPE 688
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 505 AL--EGRIYaCDQCNSKRrksnpkplvlsEARKQLMIYRLPQVLRLHLKRFRwSGRNHREKIGVHVVF---DQVLTMepy 579
Cdd:COG5560   689 QLglSDSWY-CPGCKEFR-----------QASKQMELWRLPMILIIHLKRFS-SVRSFRDKIDDLVEYpidDLDLSG--- 752
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046904076 580 ccgdMLSSLDKDTFAYDLSAVVMHHGkGFGSGHYTAYCYNTEGGFWVHCNDSKLDVCSVEEVCKTQAYILFYTRRT 655
Cdd:COG5560   753 ----VEYMVDDPRLIYDLYAVDNHYG-GLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
26-72 1.11e-14

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 68.55  E-value: 1.11e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1046904076   26 CLECATTESAWACLKCSHVACGRYIEDHALKHFEETGHPLAMEVRDL 72
Cdd:smart00290   2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQ 48
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
250-651 7.19e-71

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 232.72  E-value: 7.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 250 TGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSTSehlfpqatngkaqipsrpasstaagfsvrsdraqgfepqgfcw 329
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSE------------------------------------------- 37
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 330 ssgasisrsleliqnKEPSSKHISLCHELHTLFRVMWSGKW-ALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKV 408
Cdd:pfam00443  38 ---------------DSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGL 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 409 QQELESEGSTRRILIpfsqrkltkqvlkvVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFPERYHCVEkgfvplnq 488
Cdd:pfam00443 103 HEDLNGNHSTENESL--------------ITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELK-------- 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 489 tECLLTEMLAKFTETEALEGRI-YACDQCNSKRrksnpkplvlsEARKQLMIYRLPQVLRLHLKRFRWSgRNHREKIGVH 567
Cdd:pfam00443 161 -TASLQICFLQFSKLEELDDEEkYYCDKCGCKQ-----------DAIKQLKISRLPPVLIIHLKRFSYN-RSTWEKLNTE 227
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 568 VVFDQVLTMEPYCCGDmLSSLDKDTFAYDLSAVVMHHGkGFGSGHYTAYCYNTEGGFWVHCNDSKLDVCSVE-EVCKTQA 646
Cdd:pfam00443 228 VEFPLELDLSRYLAEE-LKPKTNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEEtAVLSSSA 305

                  ....*
gi 1046904076 647 YILFY 651
Cdd:pfam00443 306 YILFY 310
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
251-652 2.24e-62

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 210.69  E-value: 2.24e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLnldpstsehlfpqatngkaqipsrpasstaagfsvrSDRAQGFepqgfcws 330
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFL------------------------------------SDRHSCT-------- 37
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 331 sgasisrsleliqNKEPSSKHiSLCHELHTLFRVMW-SGKWALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKVQ 409
Cdd:cd02660    38 -------------CLSCSPNS-CLSCAMDEIFQEFYySGDRSPYGPINLLYLSWKHSRNLAGYSQQDAHEFFQFLLDQLH 103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 410 QElesegSTRRILIPFSqrklTKQVLKVVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFPERYHCVEKGFVPLNQT 489
Cdd:cd02660   104 TH-----YGGDKNEAND----ESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGESGVSG 174
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 490 ECLLTEMLAKFTETEALEGRIYACDQCNSKrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFRWSGRNHREKIGVHVV 569
Cdd:cd02660   175 TPTLSDCLDRFTRPEKLGDFAYKCSGCGST-----------QEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYVQ 243
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 570 FDQVLTMEPYC----CGDMLSSLDKDTFAYDLSAVVMHHGKgFGSGHYTAYCYNtEGGFWVHCNDSKLDVCSVEEVCKTQ 645
Cdd:cd02660   244 FPLELNMTPYTsssiGDTQDSNSLDPDYTYDLFAVVVHKGT-LDTGHYTAYCRQ-GDGQWFKFDDAMITRVSEEEVLKSQ 321

                  ....*..
gi 1046904076 646 AYILFYT 652
Cdd:cd02660   322 AYLLFYH 328
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
392-651 2.56e-58

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: 197.32  E-value: 2.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 392 YDQQDAQEFLCELLHKVQQELESEGSTRRILipfsqrkltKQVLKVVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLE 471
Cdd:cd02257    20 SEQQDAHEFLLFLLDKLHEELKKSSKRTSDS---------SSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 472 FPERyhcvekgfvplNQTECLLTEMLAKFTETEALEGriYACDQCNSKRrksnpkplvLSEARKQLMIYRLPQVLRLHLK 551
Cdd:cd02257    91 LPVK-----------GLPQVSLEDCLEKFFKEEILEG--DNCYKCEKKK---------KQEATKRLKIKKLPPVLIIHLK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 552 RFRWSGRNHREKIGVHVVFDQVLTMEPYC-CGDMLSSLDKDTFAYDLSAVVMHHGKGFGSGHYTAYCYNTEGGFWVHCND 630
Cdd:cd02257   149 RFSFNEDGTKEKLNTKVSFPLELDLSPYLsEGEKDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKDPSDGKWYKFND 228
                         250       260
                  ....*....|....*....|....*.
gi 1046904076 631 SKLDVCSVEEV-----CKTQAYILFY 651
Cdd:cd02257   229 DKVTEVSEEEVlefgsLSSSAYILFY 254
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
250-651 1.99e-48

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: 172.46  E-value: 1.99e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 250 TGLRNLGNTCYMNSILQVLSHlqkfrecflnldpstsehlfpqatngkaqipSRPAsstaAGFSVRSDRAQGFEPQGFCw 329
Cdd:cd02661     2 AGLQNLGNTCFLNSVLQCLTH-------------------------------TPPL----ANYLLSREHSKDCCNEGFC- 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 330 ssgasISRSLEliqnkepssKHISlchelhtlfRVMWSGKWALVSPF--AMLHSVWsliPAFRGYDQQDAQEFLCELLHK 407
Cdd:cd02661    46 -----MMCALE---------AHVE---------RALASSGPGSAPRIfsSNLKQIS---KHFRIGRQEDAHEFLRYLLDA 99
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 408 VQqelesegstRRILIPFSQRKLTKQVLK---VVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEfperyhcVEKGfv 484
Cdd:cd02661   100 MQ---------KACLDRFKKLKAVDPSSQettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLD-------IKGA-- 161
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 485 plnQTeclLTEMLAKFTETEALEGR-IYACDQCNSKrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFrwsGRNHREK 563
Cdd:cd02661   162 ---DS---LEDALEQFTKPEQLDGEnKYKCERCKKK-----------VKASKQLTIHRAPNVLTIHLKRF---SNFRGGK 221
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 564 IGVHVVFDQVLTMEPYccgdmLSSLDKDTFAYDLSAVVMHHGKGFGSGHYTAYCyNTEGGFWVHCNDSKLDVCSVEEVCK 643
Cdd:cd02661   222 INKQISFPETLDLSPY-----MSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYV-KSSNGKWYNMDDSKVSPVSIETVLS 295

                  ....*...
gi 1046904076 644 TQAYILFY 651
Cdd:cd02661   296 QKAYILFY 303
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
352-651 5.53e-45

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: 162.17  E-value: 5.53e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 352 ISLCHELHTLFrvmwsgkwaLVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKvqqelesegstrriLIPFsqrklt 431
Cdd:cd02667    18 LSQTPALRELL---------SETPKELFSQVCRKAPQFKGYQQQDSHELLRYLLDG--------------LRTF------ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 432 kqvlkvVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFPEryhcvekgfvpLNQTECLLTEMLAKFTETEALEGR-I 510
Cdd:cd02667    69 ------IDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSD-----------EIKSECSIESCLKQFTEVEILEGNnK 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 511 YACDQCnskrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFRWSGRNHREKIGVHVVFDQVLTMEPYCCGDMLSSLDK 590
Cdd:cd02667   132 FACENC--------------TKAKKQYLISKLPPVLVIHLKRFQQPRSANLRKVSRHVSFPEILDLAPFCDPKCNSSEDK 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 591 DTFAYDLSAVVMHHGkGFGSGHYTAYCY------------------NTEG---GFWVHCNDSKLDVCSVEEVCKTQAYIL 649
Cdd:cd02667   198 SSVLYRLYGVVEHSG-TMRSGHYVAYVKvrppqqrlsdltkskpaaDEAGpgsGQWYYISDSDVREVSLEEVLKSEAYLL 276

                  ..
gi 1046904076 650 FY 651
Cdd:cd02667   277 FY 278
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
393-652 5.81e-45

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: 160.15  E-value: 5.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 393 DQQDAQEFLCELLhkvqQELESegstrrilipfsqrkltkqvlkVVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEF 472
Cdd:cd02674    21 DQQDAQEFLLFLL----DGLHS----------------------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 473 PERYHcvekgfvplNQTECLLTEMLAKFTETEALEGRIYA-CDQCNSKRRksnpkplvlseARKQLMIYRLPQVLRLHLK 551
Cdd:cd02674    75 PSGSG---------DAPKVTLEDCLRLFTKEETLDGDNAWkCPKCKKKRK-----------ATKKLTISRLPKVLIIHLK 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 552 RFRWSGRNhREKIGVHVVFD-QVLTMEPYCcgdmLSSLDKDTFAYDLSAVVMHHGKGFGsGHYTAYCYNTEGGFWVHCND 630
Cdd:cd02674   135 RFSFSRGS-TRKLTTPVTFPlNDLDLTPYV----DTRSFTGPFKYDLYAVVNHYGSLNG-GHYTAYCKNNETNDWYKFDD 208
                         250       260
                  ....*....|....*....|..
gi 1046904076 631 SKLDVCSVEEVCKTQAYILFYT 652
Cdd:cd02674   209 SRVTKVSESSVVSSSAYILFYE 230
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
251-652 2.18e-38

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: 144.87  E-value: 2.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLdPSTsehlfpQATNGKAQIPSRPasstaagfsvrsdraqgFEPQGfcws 330
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEC-NST------EDAELKNMPPDKP-----------------HEPQT---- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 331 sgasisrsleliqnkepsskhisLCHELHTLFRVMWSGKWALVSPFAmlhsvwsLIPAFR--GYDQQDAQEFLCELLHKV 408
Cdd:cd02668    53 -----------------------IIDQLQLIFAQLQFGNRSVVDPSG-------FVKALGldTGQQQDAQEFSKLFLSLL 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 409 QQELESEgstrrilipfsqrkLTKQVLKVVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEfperyhcvekgfvpLNQ 488
Cdd:cd02668   103 EAKLSKS--------------KNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQ--------------LKG 154
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 489 TECLlTEMLAKFTETEALEG-RIYACDQCNSKRRksnpkplvlseARKQLMIYRLPQVLRLHLKRF---RWSGrnHREKI 564
Cdd:cd02668   155 HKTL-EECIDEFLKEEQLTGdNQYFCESCNSKTD-----------ATRRIRLTTLPPTLNFQLLRFvfdRKTG--AKKKL 220
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 565 GVHVVFDQVLTMEPYCCGDmlsslDKDTFAYDLSAVVMHHGKGFGSGHYTAYCYNTEGGFWVHCNDSKLD---------- 634
Cdd:cd02668   221 NASISFPEILDMGEYLAES-----DEGSYVYELSGVLIHQGVSAYSGHYIAHIKDEQTGEWYKFNDEDVEempgkplklg 295
                         410       420
                  ....*....|....*....|....*....
gi 1046904076 635 -----------VCSVEEVCKTQAYILFYT 652
Cdd:cd02668   296 nsedpakprksEIKKGTHSSRTAYMLVYK 324
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
251-653 2.45e-38

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: 145.09  E-value: 2.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPstsehlfpqatngkaqipsrpasstaagfsvrsdrAQGFEPQgfcws 330
Cdd:cd02659     4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPP-----------------------------------TEDDDDN----- 43
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 331 sgASISRSLELIQNKEPSSKHISLCHELHTLFRVMWsgkWALVSPFamlhsvwslipafrgyDQQDAQEFLCELLHKVQQ 410
Cdd:cd02659    44 --KSVPLALQRLFLFLQLSESPVKTTELTDKTRSFG---WDSLNTF----------------EQHDVQEFFRVLFDKLEE 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 411 ELESEGstrrilipfsQRKLtkqvlkvVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFperyhcveKGFVPlnqte 490
Cdd:cd02659   103 KLKGTG----------QEGL-------IKNLFGGKLVNYIICKECPHESEREEYFLDLQVAV--------KGKKN----- 152
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 491 clLTEMLAKFTETEALEG-RIYACDQCNSKRRksnpkplvlseARKQLMIYRLPQVLRLHLKRFRWSG-RNHREKIGVHV 568
Cdd:cd02659   153 --LEESLDAYVQGETLEGdNKYFCEKCGKKVD-----------AEKGVCFKKLPPVLTLQLKRFEFDFeTMMRIKINDRF 219
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 569 VFDQVLTMEPYC------CGDMLSSLDKDTFAYDLSAVVMHHGkGFGSGHYTAYCYNTEGGFWVHCNDSKLDVCSVEEVC 642
Cdd:cd02659   220 EFPLELDMEPYTekglakKEGDSEKKDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAE 298
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1046904076 643 K----------------------TQAYILFYTR 653
Cdd:cd02659   299 EecfggeetqktydsgprafkrtTNAYMLFYER 331
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
358-652 2.01e-35

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 135.90  E-value: 2.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 358 LHTLFRVMWSGK--WALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKVQQELESEGSTRRILIPFSQRKLTKQVL 435
Cdd:cd02663    27 LKDLFESISEQKkrTGVISPKKFITRLKRENELFDNYMHQDAHEFLNFLLNEIAEILDAERKAEKANRKLNNNNNAEPQP 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 436 KVVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFPEryhcvekgfvplnqtECLLTEMLAKFTETEALEGR-IYACD 514
Cdd:cd02663   107 TWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQ---------------NTSITSCLRQFSATETLCGRnKFYCD 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 515 QCNSKRrksnpkplvlsEARKQLMIYRLPQVLRLHLKRFRWSGRNHR-EKIGVHVVFDqvLTMEPYCCGDMLSSLDKdtf 593
Cdd:cd02663   172 ECCSLQ-----------EAEKRMKIKKLPKILALHLKRFKYDEQLNRyIKLFYRVVFP--LELRLFNTTDDAENPDR--- 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046904076 594 AYDLSAVVMHHGKGFGSGHYTAYCYNTegGFWVHCND---SKLDVCSVEEV-----CKTQAYILFYT 652
Cdd:cd02663   236 LYELVAVVVHIGGGPNHGHYVSIVKSH--GGWLLFDDetvEKIDENAVEEFfgdspNQATAYVLFYQ 300
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
251-651 1.01e-25

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: 108.19  E-value: 1.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPStsehlfpqatngkaqipSRPASSTAAGFSVrsdraqgfepqgfcws 330
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPA-----------------RRGANQSSDNLTN---------------- 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 331 sgasisrsleliqnkepsskhislchELHTLFRVMwSGKWALVSPFAMLHSVWSLIPAF------RGYDQQDAQEFLCEL 404
Cdd:cd02657    48 --------------------------ALRDLFDTM-DKKQEPVPPIEFLQLLRMAFPQFaekqnqGGYAQQDAEECWSQL 100
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 405 LHKVQQELESEGSTRRilipfsqrkltkqvlkVVNTIFHGQLLSQVTCV-SCNYKSNTIEPFWDLSLefperyHCVEKGF 483
Cdd:cd02657   101 LSVLSQKLPGAGSKGS----------------FIDQLFGIELETKMKCTeSPDEEEVSTESEYKLQC------HISITTE 158
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 484 VplnqtECLLTEMLAKFTETEALEGRIYACDQCNSKRRKsnpkplvlsearkqlmIYRLPQVLRLHLKRFRWSGR-NHRE 562
Cdd:cd02657   159 V-----NYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSR----------------ISRLPKYLTVQFVRFFWKRDiQKKA 217
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 563 KIGVHVVFDQVLTMEPYCCGdmlSSLdkdtfaYDLSAVVMHHGKGFGSGHYTAYCYNTEGGFWVHCNDSKLDVCSVEEVC 642
Cdd:cd02657   218 KILRKVKFPFELDLYELCTP---SGY------YELVAVITHQGRSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDIL 288
                         410
                  ....*....|....*.
gi 1046904076 643 KTQ-------AYILFY 651
Cdd:cd02657   289 KLSgggdwhiAYILLY 304
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
246-651 1.74e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 104.97  E-value: 1.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 246 APGVTGLRNLGNTCYMNSILQVLSHLQKFREcflNLdpstsEHLFpqatngkaqipsrpasstaagfsvrsdraqgfepq 325
Cdd:cd02671    21 LLPFVGLNNLGNTCYLNSVLQVLYFCPGFKH---GL-----KHLV----------------------------------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 326 gfcwSSGASISrsleliqnkepssKHISLCHELHTLFrvmwSGKWALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELL 405
Cdd:cd02671    58 ----SLISSVE-------------QLQSSFLLNPEKY----NDELANQAPRRLLNALREVNPMYEGYLQHDAQEVLQCIL 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 406 HKVQQELESegstrrilipfsqrkltkqvlkvvntIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFPERYHCVEKGFVP 485
Cdd:cd02671   117 GNIQELVEK--------------------------DFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESSE 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 486 LNQTECLLTEMLAKFTETEALEGRI-----YACDQCNSkrrksnpkplvLSEARKQLMIYRLPQVLRLHLKRFRWSGRNH 560
Cdd:cd02671   171 ISPDPKTEMKTLKWAISQFASVERIvgedkYFCENCHH-----------YTEAERSLLFDKLPEVITIHLKCFAANGSEF 239
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 561 REKIGVHVVFDQVLTMEPYCCGDMLSSLDKDTfaYDLSAVVMHHGKGFGSGHYTAYCYnteggfWVHCNDSK-------- 632
Cdd:cd02671   240 DCYGGLSKVNTPLLTPLKLSLEEWSTKPKNDV--YRLFAVVMHSGATISSGHYTAYVR------WLLFDDSEvkvteekd 311
                         410       420
                  ....*....|....*....|
gi 1046904076 633 -LDVCSVEEVCKTQAYILFY 651
Cdd:cd02671   312 fLEALSPNTSSTSTPYLLFY 331
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
251-651 2.89e-23

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 101.41  E-value: 2.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPstsehlfpQATNGkaqipsrpasstaagfsvrsdraqgfepqgfcws 330
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNL--------PRLGD---------------------------------- 38
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 331 sgasisrsleliQNKEPSSKHISLCHELHTLFRvmwsgkwALVSPFAMLHSVWSliPAFRGYDQQDAQEFLCELLHKVQQ 410
Cdd:cd02664    39 ------------SQSVMKKLQLLQAHLMHTQRR-------AEAPPDYFLEASRP--PWFTPGSQQDCSEYLRYLLDRLHT 97
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 411 elesegstrrilipfsqrkltkqvlkVVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFPeryhcvekgfvplnqte 490
Cdd:cd02664    98 --------------------------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFP----------------- 134
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 491 cLLTEMLAKFTETEALEG-RIYACDQCNSkrrksnpkplvLSEARKQLMIYRLPQVLRLHLKRFRWSGRNH-REKIGVHV 568
Cdd:cd02664   135 -SVQDLLNYFLSPEKLTGdNQYYCEKCAS-----------LQDAEKEMKVTGAPEYLILTLLRFSYDQKTHvREKIMDNV 202
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 569 VFDQVLTM----------EPYCCGDMLSSLDKD----TFAYDLSAVVMHHGKGFGSGHYtaYCY---------------- 618
Cdd:cd02664   203 SINEVLSLpvrvesksseSPLEKKEEESGDDGElvtrQVHYRLYAVVVHSGYSSESGHY--FTYardqtdadstgqecpe 280
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1046904076 619 ------NTEGGFWVHCNDSKLDVCSVEEV-------CKTQAYILFY 651
Cdd:cd02664   281 pkdaeeNDESKNWYLFNDSRVTFSSFESVqnvtsrfPKDTPYILFY 326
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
26-87 4.58e-23

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 92.71  E-value: 4.58e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046904076  26 CLECATTESAWACLKCSHVACGRYIEDHALKHFEETGHPLAMEVRDLYVFCYLCKDYVLNDN 87
Cdd:pfam02148   1 CSLCGNTSNLWLCLTCGHVGCGRYQNSHALEHYEETGHPLAVNLSTLTVYCYPCDDYVHDPS 62
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
251-651 2.39e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 98.16  E-value: 2.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 251 GLRNLGNTCYMNSILQVLSHLQKFRECFLNLdpstsEHLFPQAtngkaqiPSRPASStaagfsvrsdraqgFEPQ----- 325
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDL-----ENKFPSD-------VVDPAND--------------LNCQlikla 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 326 -GFCwsSGASiSRSLELIQNKEPSSKHISlchelhtlfrvmwsgkwalvsPFaMLHSvwsLI----PAFRGYDQQDAQEF 400
Cdd:cd02658    55 dGLL--SGRY-SKPASLKSENDPYQVGIK---------------------PS-MFKA---LIgkghPEFSTMRQQDALEF 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 401 LCELLHKVQQELESEGSTRrilipfsqrkltkqvlkvVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFPER----Y 476
Cdd:cd02658   107 LLHLIDKLDRESFKNLGLN------------------PNDLFKFMIEDRLECLSCKKVKYTSELSEILSLPVPKDeateK 168
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 477 HCVEKGFVPLNQTEClltemLAKFTETEALEgriYACDQCNSKrrksnpkplvlSEARKQLMIYRLPQVLRLHLKRFR-- 554
Cdd:cd02658   169 EEGELVYEPVPLEDC-----LKAYFAPETIE---DFCSTCKEK-----------TTATKTTGFKTFPDYLVINMKRFQll 229
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 555 --WSGRnhreKIGVHVVFDQVLTMEPyccgdmlssldkdtfaYDLSAVVMHHGKGFGSGHYTAYCY--NTEGGFWVHCND 630
Cdd:cd02658   230 enWVPK----KLDVPIDVPEELGPGK----------------YELIAFISHKGTSVHSGHYVAHIKkeIDGEGKWVLFND 289
                         410       420
                  ....*....|....*....|.
gi 1046904076 631 SKLDVCSVEEVCKTQAYILFY 651
Cdd:cd02658   290 EKVVASQDPPEMKKLGYIYFY 310
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
383-651 7.57e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 95.13  E-value: 7.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 383 WSLIPAFRGY-----DQQDAQEFLCELLHKVQQELESegstrriliPFsqrkltkqvlkvvntifHGQLLSQVTCVSCNY 457
Cdd:cd02662    18 LASLPSLIEYleeflEQQDAHELFQVLLETLEQLLKF---------PF-----------------DGLLASRIVCLQCGE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 458 KSN-TIEPFWDLSLEFPERyhcvekgfvpLNQTECLLTEMLAKFTETEALEGriYACDQCnskrrksnpkplvlsearkQ 536
Cdd:cd02662    72 SSKvRYESFTMLSLPVPNQ----------SSGSGTTLEHCLDDFLSTEIIDD--YKCDRC-------------------Q 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 537 LMIYRLPQVLRLHLKRFRWSGRNHREKIGVHVVFDQVLTmepyccgdmlssldkdTFAYDLSAVVMHHGkGFGSGHYTAY 616
Cdd:cd02662   121 TVIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERLP----------------KVLYRLRAVVVHYG-SHSSGHYVCY 183
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046904076 617 --------------------CYNTEGGFWVHCNDSKLDVCSVEEVCKT-QAYILFY 651
Cdd:cd02662   184 rrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVLEQkSAYMLFY 239
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
248-655 1.48e-21

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 99.96  E-value: 1.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 248 GVTGLRNLGNTCYMNSILQVLSHLQKFRECFLnldpstsehlfpqatngkaqipsrpasstaagfsvrSDraqGFEPQgf 327
Cdd:COG5560   264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFL------------------------------------SD---EYEES-- 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 328 cwssgasisrslelIQNKEPSSKHISLCHELHTLFRVMWSGKWALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLC----- 402
Cdd:COG5560   303 --------------INEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAflldg 368
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 403 --ELLHKVQQELESEGSTRRILIPFSQRKLTKQVLK--------VVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSL-- 470
Cdd:COG5560   369 lhEDLNRIIKKPYTSKPDLSPGDDVVVKKKAKECWWehlkrndsIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLpl 448
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 471 --------------------------------------------------------------------------EFPERY 476
Cdd:COG5560   449 pvsmvwkhtivvfpesgrrqplkieldasstirglkklvdaeygklgcfeikvmciyyggnynmlepadkvllqDIPQTD 528
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 477 HCVEKG----------------------------FVPLN----------------------------------QTECLLT 494
Cdd:COG5560   529 FVYLYEtndngievpvvhlriekgykskrlfgdpFLQLNvlikasiydklvkefeellvlvemkktdvdlvseQVRLLRE 608
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 495 EM----------------------------------------------------------------------LAKFTETE 504
Cdd:COG5560   609 ESspsswlkleteidtkreeqveeegqmnfndavvisceweekrylslfsydplwtireigaaertitlqdcLNEFSKPE 688
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 505 AL--EGRIYaCDQCNSKRrksnpkplvlsEARKQLMIYRLPQVLRLHLKRFRwSGRNHREKIGVHVVF---DQVLTMepy 579
Cdd:COG5560   689 QLglSDSWY-CPGCKEFR-----------QASKQMELWRLPMILIIHLKRFS-SVRSFRDKIDDLVEYpidDLDLSG--- 752
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046904076 580 ccgdMLSSLDKDTFAYDLSAVVMHHGkGFGSGHYTAYCYNTEGGFWVHCNDSKLDVCSVEEVCKTQAYILFYTRRT 655
Cdd:COG5560   753 ----VEYMVDDPRLIYDLYAVDNHYG-GLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
251-653 2.16e-19

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 89.09  E-value: 2.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 251 GLRNLGNTCYMNSILQVLShlqkfrecfLNLdPSTSEHLFPQATNGKAQIpsrpasstaagfSVRSDRaqgFEPQGFCws 330
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILA---------LYL-PKLDELLDDLSKELKVLK------------NVIRKP---EPDLNQE-- 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 331 sgasisrsleliqnkepsskhislchELHTLFRVMWSGKwalvspfamLHSVWSLIPAfrgYDQQDAQEFLCELLHKVQQ 410
Cdd:COG5533    54 --------------------------EALKLFTALWSSK---------EHKVGWIPPM---GSQEDAHELLGKLLDELKL 95
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 411 ELESEGsTRRILIPFSqrkltkqvlkvvntifhgqllsqvtcvscNYKSNTIEPFWDLSLEFPERyhcveKGFVPLNQTE 490
Cdd:COG5533    96 DLVNSF-TIRIFKTTK-----------------------------DKKKTSTGDWFDIIIELPDQ-----TWVNNLKTLQ 140
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 491 CLLTEMLAKFTetealegriyacDQCNSKRrKSNPKPLVLSEARKQLMIYRLPQVLRLHLKRFRWSGRNHR------EKI 564
Cdd:COG5533   141 EFIDNMEELVD------------DETGVKA-KENEELEVQAKQEYEVSFVKLPKILTIQLKRFANLGGNQKidtevdEKF 207
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 565 GVHVVFDQVLTMEPyccgdmlssldkdTFAYDLSAVVMHHGkGFGSGHYTAYCynTEGGFWVHCNDSKLDVCSVEEVCKT 644
Cdd:COG5533   208 ELPVKHDQILNIVK-------------ETYYDLVGFVLHQG-SLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEEAINE 271
                         410
                  ....*....|..
gi 1046904076 645 ---QAYILFYTR 653
Cdd:COG5533   272 kakNAYLYFYER 283
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
248-641 4.54e-16

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 82.61  E-value: 4.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076  248 GVTGLRNLGNTCYMNSILQVLSHLQKFRECFLNL-----DPSTSEHLFPQATNGKAQIPSRPASSTAAgfsVRSdraqgf 322
Cdd:COG5077    192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIptdhpRGRDSVALALQRLFYNLQTGEEPVDTTEL---TRS------ 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076  323 epqgFCWSSGASISrsleliqnkepsskhislchelhtlfrvmwsgkwalvspfamlhsvwslipafrgydQQDAQEFlc 402
Cdd:COG5077    263 ----FGWDSDDSFM---------------------------------------------------------QHDIQEF-- 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076  403 ellhkvqqelesegstRRILIPFSQRKLTKQVLK-VVNTIFHGQLLSQVTCVSCNYKSNTIEPFWDLSLEFperyhcveK 481
Cdd:COG5077    280 ----------------NRVLQDNLEKSMRGTVVEnALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNV--------K 335
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076  482 GFVPLNqteclltEMLAKFTETEALEG-RIYACDQCNskrrksnpkplvLSEARKQLMIYRLPQVLRLHLKRFRWS-GRN 559
Cdd:COG5077    336 GMKNLQ-------ESFRRYIQVETLDGdNRYNAEKHG------------LQDAKKGVIFESLPPVLHLQLKRFEYDfERD 396
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076  560 HREKIGVHVVFDQVLTMEPYCCGDMLSSLDKDtFAYDLSAVVMHHGKgFGSGHYTAYCYNTEGGFWVHCNDSKLDVCSVE 639
Cdd:COG5077    397 MMVKINDRYEFPLEIDLLPFLDRDADKSENSD-AVYVLYGVLVHSGD-LHEGHYYALLKPEKDGRWYKFDDTRVTRATEK 474

                   ..
gi 1046904076  640 EV 641
Cdd:COG5077    475 EV 476
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
26-72 1.11e-14

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 68.55  E-value: 1.11e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1046904076   26 CLECATTESAWACLKCSHVACGRYIEDHALKHFEETGHPLAMEVRDL 72
Cdd:smart00290   2 CSVCGTIENLWLCLTCGQVGCGRYQNGHALEHFEETGHPLVVKLGTQ 48
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
250-641 2.03e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 72.14  E-value: 2.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 250 TGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSTSEhlfpqATNGKAQIPSRPasstaagfsvrsdraqgfepqgfcw 329
Cdd:cd02666     2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAE-----LASDYPTERRIG------------------------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 330 ssGASISRSLELIQNKepsskhisLCHELHTLFRVMWSGKWALVSPFAMLhsvwslipAFRGYDQQDAQEflceLLHKVQ 409
Cdd:cd02666    52 --GREVSRSELQRSNQ--------FVYELRSLFNDLIHSNTRSVTPSKEL--------AYLALRQQDVTE----CIDNVL 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 410 QELESEGSTRRILIPFSQRKLTKQVLKVVNTIFHGQLLSQVT-CVSCNYKSNTIEPFWDLSLEFPeryhCVEKGFVPLNQ 488
Cdd:cd02666   110 FQLEVALEPISNAFAGPDTEDDKEQSDLIKRLFSGKTKQQLVpESMGNQPSVRTKTERFLSLLVD----VGKKGREIVVL 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 489 TE-CLLTEMLAKFTETEALEG-RIYACDQCN----------SKRRKSNPKPL-VLSEARKQLMIYRLPQVLRLhlkrfRW 555
Cdd:cd02666   186 LEpKDLYDALDRYFDYDSLTKlPQRSQVQAQlaqplqreliSMDRYELPSSIdDIDELIREAIQSESSLVRQA-----QN 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 556 SGRNHREKIgvhvvfdqvltmepyccgdmlSSLDKD--TFAYDLSAVVMHHGKGfGSGHYTAYCYNTEGGFWVHCNDSKL 633
Cdd:cd02666   261 ELAELKHEI---------------------EKQFDDlkSYGYRLHAVFIHRGEA-SSGHYWVYIKDFEENVWRKYNDETV 318

                  ....*...
gi 1046904076 634 DVCSVEEV 641
Cdd:cd02666   319 TVVPASEV 326
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
247-651 2.66e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 72.35  E-value: 2.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 247 PGVTGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDpstsehlfpqatngkaqipsrpasstaagfsvrsdraqgfepqg 326
Cdd:cd02669   117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYE-------------------------------------------- 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 327 fcwssgasisrSLELIQNKEPSskhisLCHELHTLFRVMWSGKW--ALVSPFAMLH--SVWSLIPaFRGYDQQDAQEFLC 402
Cdd:cd02669   153 -----------NYENIKDRKSE-----LVKRLSELIRKIWNPRNfkGHVSPHELLQavSKVSKKK-FSITEQSDPVEFLS 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 403 ELLHKVQQELE-SEGSTRRILIPFSQRKLTKQVLKVVNTIFHGQLLSQVTCVSCNYKSNTIePFWDLSLEFPERyhcvek 481
Cdd:cd02669   216 WLLNTLHKDLGgSKKPNSSIIHDCFQGKVQIETQKIKPHAEEEGSKDKFFKDSRVKKTSVS-PFLLLTLDLPPP------ 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 482 gfvPLNQTE--------CLLTEMLAKFTETEALEgriyacdqcnskrrksnpkplvLSEARKQLMIYRLPQVLRLHLKRF 553
Cdd:cd02669   289 ---PLFKDGneeniipqVPLKQLLKKYDGKTETE----------------------LKDSLKRYLISRLPKYLIFHIKRF 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 554 RwsgRNH--REKIGVHVVFDQVLTMEPYCCGDMLSSLDKDTfAYDLSAVVMHHGKGFGSGHYTAYCYNTEGGFWVHCNDS 631
Cdd:cd02669   344 S---KNNffKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLST-KYNLVANIVHEGTPQEDGTWRVQLRHKSTNKWFEIQDL 419
                         410       420
                  ....*....|....*....|
gi 1046904076 632 KLDVCSVEEVCKTQAYILFY 651
Cdd:cd02669   420 NVKEVLPQLIFLSESYIQIW 439
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
379-651 3.03e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 67.17  E-value: 3.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 379 LHSVWSLIPAFRGYDQQDAQEFLCELLHKVQQELESEgSTRRILIPFSQRKLTK-QVLKV-VNTIFhgqllsqvTCVSCN 456
Cdd:cd02673    18 LSSIGKINTEFDNDDQQDAHEFLLTLLEAIDDIMQVN-RTNVPPSNIEIKRLNPlEAFKYtIESSY--------VCIGCS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 457 YKSNTIEPFWDLSLEFPERYHCVEKgfvplnqtecLLTEMLAKFTETEALegriyaCDQCNSKRRKSNPKplvlsearkq 536
Cdd:cd02673    89 FEENVSDVGNFLDVSMIDNKLDIDE----------LLISNFKTWSPIEKD------CSSCKCESAISSER---------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 537 lmIYRLPQVLRLHLKRFRWsgrnhREKIGVHVVfDQVLTMEPYCcgdmlSSLDKdtfaYDLSAVVMHHGKGFGSGHYTAY 616
Cdd:cd02673   143 --IMTFPECLSINLKRYKL-----RIATSDYLK-KNEEIMKKYC-----GTDAK----YSLVAVICHLGESPYDGHYIAY 205
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1046904076 617 CYN-TEGGFWVHCNDSKLDVCSVEEVCK---TQAYILFY 651
Cdd:cd02673   206 TKElYNGSSWLYCSDDEIRPVSKNDVSTnarSSGYLIFY 244
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
542-651 2.20e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 43.32  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046904076 542 LPQVLRLHLKRFRWsGRNHREKIGVHVVFDQVLTMEPYccgdmlssldkdtfayDLSAVVMHHGKGfGSGHYTAYCYNTE 621
Cdd:cd02665   128 LPPVLTFELSRFEF-NQGRPEKIHDKLEFPQIIQQVPY----------------ELHAVLVHEGQA-NAGHYWAYIYKQS 189
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1046904076 622 GGFWVHCNDSKLDVCSVEEVCK--------TQAYILFY 651
Cdd:cd02665   190 RQEWEKYNDISVTESSWEEVERdsfgggrnPSAYCLMY 227
 
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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