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Conserved domains on  [gi|767995416|ref|XP_011523368|]
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ubiquitin carboxyl-terminal hydrolase 36 isoform X1 [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase family protein( domain architecture ID 10119183)

ubiquitin carboxyl-terminal hydrolase family protein is a C19 family peptidase that may deubiquitinate polyubiquitinated target proteins

CATH:  3.90.70.10
EC:  3.4.19.12
Gene Ontology:  GO:0016579|GO:0004843
MEROPS:  C19
PubMed:  7845226|11517925
SCOP:  4003158

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
121-421 7.82e-179

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: 524.92  E-value: 7.82e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  121 GAGLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSCHQGSFCMLCVMQNHIVQAFANSGNAIKPVSFIRDLKKIARH 200
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  201 FRFGNQEDAHEFLRYTIDAMQKACLNGCAKL---DRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQ 277
Cdd:cd02661    81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  278 AANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQ 357
Cdd:cd02661   161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767995416  358 NNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYL 421
Cdd:cd02661   241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
PHA03247 super family cl33720
large tegument protein UL36; Provisional
506-840 9.27e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 9.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  506 PPKLPSGSPSPKLSQTPTHMPTILDDPGKKVKKPAPPQHFSPRTAQGL-------------------------------- 553
Cdd:PHA03247 2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLgraaqassppqrprrraarptvgsltsladpp 2702
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  554 -----PGTSNSNSSRSGSQRQGSWDSRDVVLSTSPKLLATATANGHGLKGNDESAGLDRRGSSSSSPEHSASSDSTKAPQ 628
Cdd:PHA03247 2703 pppptPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  629 TPRSGAAHLCDSQETncstaghSKTPPSGADSKTVKLKSPVLSNTTTEPASTMSPPPAKKLALSAKKASTL--------W 700
Cdd:PHA03247 2783 LTRPAVASLSESRES-------LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPppslplggS 2855
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  701 RATGNDLRPPPPSPSSdLTHPMKTSHPvvastwPVHRARAVSPAPQSSSRLQPPFSPHPtllssTPKPPGTSEPRscssi 780
Cdd:PHA03247 2856 VAPGGDVRRRPPSRSP-AAKPAAPARP------PVRRLARPAVSRSTESFALPPDQPER-----PPQPQAPPPPQ----- 2918
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767995416  781 stalPQVNEDLVSLPHQLPEASEPPQSPSEKRKKTF-VGEPQRLGSETRLPQHIREATAAP 840
Cdd:PHA03247 2919 ----PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAgAGEPSGAVPQPWLGALVPGRVAVP 2975
 
Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
121-421 7.82e-179

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: 524.92  E-value: 7.82e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  121 GAGLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSCHQGSFCMLCVMQNHIVQAFANSGNAIKPVSFIRDLKKIARH 200
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  201 FRFGNQEDAHEFLRYTIDAMQKACLNGCAKL---DRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQ 277
Cdd:cd02661    81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  278 AANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQ 357
Cdd:cd02661   161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767995416  358 NNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYL 421
Cdd:cd02661   241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
122-420 9.92e-78

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 258.14  E-value: 9.92e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416   122 AGLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSC--HQGSFCMLCVMQNHIVQAFANS-GNAIKPVSFIRDLKKIA 198
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDsrYNKDINLLCALRDLFKALQKNSkSSSVSPKMFKKSLGKLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416   199 RHFRFGNQEDAHEFLRYTIDAMQKAClngcaKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQA 278
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416   279 ANIVR------ALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEFLN 350
Cdd:pfam00443  156 SAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELD 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767995416   351 IRPYMSQNN----GDPVMYGLYAVLVHSGySCHAGHYYCYVKA-SNGQWYQMNDSLV-HSSNVKVVLNQQAYVLFY 420
Cdd:pfam00443  236 LSRYLAEELkpktNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVtEVDEETAVLSSSAYILFY 310
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
123-423 6.92e-27

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 111.82  E-value: 6.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  123 GLHNLGNTCFLNATIQCLT-YTPPLANYL--LSKEharschqgsfcmLCVMQNHIVQAFA--NSGNAIKPVSFIRDLK-- 195
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlYLPKLDELLddLSKE------------LKVLKNVIRKPEPdlNQEEALKLFTALWSSKeh 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  196 KIARHFRFGNQEDAHEFLRYTIDAMqkaclngcaKLDRQTQATTLVHQIFGGYLRSRVkcsvcKSVSDTYdpyldVALEI 275
Cdd:COG5533    69 KVGWIPPMGSQEDAHELLGKLLDEL---------KLDLVNSFTIRIFKTTKDKKKTST-----GDWFDII-----IELPD 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  276 RQAANIVRALELFVKAD---------VLSGENAYMCAKCKKKVPASKRftihRTSNVLTLSLKRFANFSGG-KITKDVGY 345
Cdd:COG5533   130 QTWVNNLKTLQEFIDNMeelvddetgVKAKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANLGGNqKIDTEVDE 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  346 PEFLNIRPYMSQNNGDPVMYGLYAVLVHSGySCHAGHYYCYVKaSNGQWYQMNDSLVHSSNVKVVLN---QQAYVLFYLR 422
Cdd:COG5533   206 KFELPVKHDQILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283

                  .
gi 767995416  423 I 423
Cdd:COG5533   284 I 284
PHA03247 PHA03247
large tegument protein UL36; Provisional
506-840 9.27e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 9.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  506 PPKLPSGSPSPKLSQTPTHMPTILDDPGKKVKKPAPPQHFSPRTAQGL-------------------------------- 553
Cdd:PHA03247 2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLgraaqassppqrprrraarptvgsltsladpp 2702
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  554 -----PGTSNSNSSRSGSQRQGSWDSRDVVLSTSPKLLATATANGHGLKGNDESAGLDRRGSSSSSPEHSASSDSTKAPQ 628
Cdd:PHA03247 2703 pppptPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  629 TPRSGAAHLCDSQETncstaghSKTPPSGADSKTVKLKSPVLSNTTTEPASTMSPPPAKKLALSAKKASTL--------W 700
Cdd:PHA03247 2783 LTRPAVASLSESRES-------LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPppslplggS 2855
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  701 RATGNDLRPPPPSPSSdLTHPMKTSHPvvastwPVHRARAVSPAPQSSSRLQPPFSPHPtllssTPKPPGTSEPRscssi 780
Cdd:PHA03247 2856 VAPGGDVRRRPPSRSP-AAKPAAPARP------PVRRLARPAVSRSTESFALPPDQPER-----PPQPQAPPPPQ----- 2918
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767995416  781 stalPQVNEDLVSLPHQLPEASEPPQSPSEKRKKTF-VGEPQRLGSETRLPQHIREATAAP 840
Cdd:PHA03247 2919 ----PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAgAGEPSGAVPQPWLGALVPGRVAVP 2975
 
Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
121-421 7.82e-179

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: 524.92  E-value: 7.82e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  121 GAGLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSCHQGSFCMLCVMQNHIVQAFANSGNAIKPVSFIRDLKKIARH 200
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  201 FRFGNQEDAHEFLRYTIDAMQKACLNGCAKL---DRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQ 277
Cdd:cd02661    81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  278 AANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQ 357
Cdd:cd02661   161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767995416  358 NNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYL 421
Cdd:cd02661   241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
122-420 9.92e-78

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 258.14  E-value: 9.92e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416   122 AGLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSC--HQGSFCMLCVMQNHIVQAFANS-GNAIKPVSFIRDLKKIA 198
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDsrYNKDINLLCALRDLFKALQKNSkSSSVSPKMFKKSLGKLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416   199 RHFRFGNQEDAHEFLRYTIDAMQKAClngcaKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQA 278
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416   279 ANIVR------ALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEFLN 350
Cdd:pfam00443  156 SAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELD 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767995416   351 IRPYMSQNN----GDPVMYGLYAVLVHSGySCHAGHYYCYVKA-SNGQWYQMNDSLV-HSSNVKVVLNQQAYVLFY 420
Cdd:pfam00443  236 LSRYLAEELkpktNNLQDYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVtEVDEETAVLSSSAYILFY 310
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
123-420 2.62e-72

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: 243.82  E-value: 2.62e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  123 GLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSCH--QGSFCMLCVMQNhIVQAFANSGNAiKPVSFIRDLK---KI 197
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLscSPNSCLSCAMDE-IFQEFYYSGDR-SPYGPINLLYlswKH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  198 ARHFRFGNQEDAHEFLRYTIDAMQKACLNGCAKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQ 277
Cdd:cd02660    80 SRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  278 AANIVRA---------------LELFVKADVLsGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSGG---KI 339
Cdd:cd02660   160 KSTPSWAlgesgvsgtptlsdcLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  340 TKDVGYPEFLNIRPYMSQNNGDPVM---------YGLYAVLVHSGySCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVV 410
Cdd:cd02660   239 DTYVQFPLELNMTPYTSSSIGDTQDsnsldpdytYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEV 317
                         330
                  ....*....|
gi 767995416  411 LNQQAYVLFY 420
Cdd:cd02660   318 LKSQAYLLFY 327
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
123-420 5.74e-66

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: 223.13  E-value: 5.74e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  123 GLHNLGNTCFLNATIQCLtytpplanyllskeharschqgsfcmlcvmqnhivqafansgnaikpvsfirdlkkiarhfr 202
Cdd:cd02257     1 GLNNLGNTCYLNSVLQAL-------------------------------------------------------------- 18
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  203 FGNQEDAHEFLRYTIDAMQKACLNGCAKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDP--YLDVALEIRQAA- 279
Cdd:cd02257    19 FSEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPelFLSLPLPVKGLPq 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  280 -NIVRALELFVKADVLSGENAYMCaKCKKKVPASKRFTIHRTSNVLTLSLKRFA---NFSGGKITKDVGYPEFLNIRPYM 355
Cdd:cd02257    99 vSLEDCLEKFFKEEILEGDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYL 177
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767995416  356 SQNNGD------PVMYGLYAVLVHSGYSCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVL-----NQQAYVLFY 420
Cdd:cd02257   178 SEGEKDsdsdngSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFY 254
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
123-420 7.11e-55

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: 192.60  E-value: 7.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  123 GLHNLGNTCFLNATIQCLTYTPPLANyLLSKeharschqgsfcmlcvmqnhivqafansgnaiKPVSFIRDLKKIARHFR 202
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRE-LLSE--------------------------------TPKELFSQVCRKAPQFK 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  203 FGNQEDAHEFLRYTIDAMQkaclngcakldrqtqatTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVAL----EIRQA 278
Cdd:cd02667    48 GYQQQDSHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSE 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  279 ANIVRALELFVKADVLSGENAYMCAKCKKkvpASKRFTIHRTSNVLTLSLKRF-----ANFSggKITKDVGYPEFLNIRP 353
Cdd:cd02667   111 CSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqqprsANLR--KVSRHVSFPEILDLAP 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  354 YMSQNN-----GDPVMYGLYAVLVHSGySCHAGHYYCYVKASN----------------------GQWYQMNDSLVHSSN 406
Cdd:cd02667   186 FCDPKCnssedKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVS 264
                         330
                  ....*....|....
gi 767995416  407 VKVVLNQQAYVLFY 420
Cdd:cd02667   265 LEEVLKSEAYLLFY 278
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
123-420 6.27e-51

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: 179.41  E-value: 6.27e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  123 GLHNLGNTCFLNATIQCLtytpplanyllskeharschqgsfcmlcvmqnhivqafansgnaikpvsfirdlkkiarhfr 202
Cdd:cd02674     1 GLRNLGNTCYMNSILQCL-------------------------------------------------------------- 18
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  203 FGNQEDAHEFLRYTIDamqkaclngcaKLDRqtqattLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIV 282
Cdd:cd02674    19 SADQQDAQEFLLFLLD-----------GLHS------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDA 81
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  283 RA------LELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFaNFSGG---KITKDVGYP-EFLNIR 352
Cdd:cd02674    82 PKvtledcLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF-SFSRGstrKLTTPVTFPlNDLDLT 160
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  353 PY-MSQNNGDPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFY 420
Cdd:cd02674   161 PYvDTRSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
123-423 1.38e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 176.29  E-value: 1.38e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  123 GLHNLGNTCFLNATIQCLTYTPPLANYLLS---KEHARSCHQGsfcmLCVMQnhiVQaFANSGNAIKPVSFIRDLKKIar 199
Cdd:cd02659     4 GLKNQGATCYMNSLLQQLYMTPEFRNAVYSippTEDDDDNKSV----PLALQ---RL-FLFLQLSESPVKTTELTDKT-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  200 hFRFG-------NQEDAHEFLRYTIDAMQKaclngcaKLdRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVA 272
Cdd:cd02659    74 -RSFGwdslntfEQHDVQEFFRVLFDKLEE-------KL-KGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQ 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  273 LEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFaNF-----SGGKITKDVGYPE 347
Cdd:cd02659   145 VAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRF-EFdfetmMRIKINDRFEFPL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  348 FLNIRPYMSQNNG-----------DPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQ- 414
Cdd:cd02659   224 ELDMEPYTEKGLAkkegdsekkdsESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECf 302
                         330       340       350
                  ....*....|....*....|....*....|
gi 767995416  415 ---------------------AYVLFYLRI 423
Cdd:cd02659   303 ggeetqktydsgprafkrttnAYMLFYERK 332
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
123-420 4.95e-41

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: 153.23  E-value: 4.95e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  123 GLHNLGNTCFLNATIQCLTYtpplaNYLLSkeharsCHQGSFCmlCVMQNHivqafaNSGNAIKPVSFIRDLKKIARHFR 202
Cdd:cd02663     1 GLENFGNTCYCNSVLQALYF-----ENLLT------CLKDLFE--SISEQK------KRTGVISPKKFITRLKRENELFD 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  203 FGNQEDAHEFLRYTI----DAMQKACLNGCAKLDRQ-----TQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVAL 273
Cdd:cd02663    62 NYMHQDAHEFLNFLLneiaEILDAERKAEKANRKLNnnnnaEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  274 EIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA-NFSGGKITK---DVGYPEFL 349
Cdd:cd02663   142 DVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKyDEQLNRYIKlfyRVVFPLEL 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767995416  350 NIRPYMSQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKaSNGQWYQMND---SLVHSSNVKVVLNQ-----QAYVLFY 420
Cdd:cd02663   222 RLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDetvEKIDENAVEEFFGDspnqaTAYVLFY 299
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
123-402 3.89e-37

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 142.94  E-value: 3.89e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  123 GLHNLGNTCFLNATIQCLTYTPPLANYLLSkeharschqgsfcmlCVMQNHIVQAFANSGNAIKPVSFIRDLKKIARHFR 202
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE---------------CNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQ 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  203 FGN-------------------QEDAHEFLRYTIDAMQkaclngcAKLDRQT--QATTLVHQIFGGYLRSRVKCSVCKSV 261
Cdd:cd02668    66 FGNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLE-------AKLSKSKnpDLKNIVQDLFRGEYSYVTQCSKCGRE 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  262 SDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA----NFSGG 337
Cdd:cd02668   139 SSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVfdrkTGAKK 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767995416  338 KITKDVGYPEFLNIRPY-MSQNNGDPVmYGLYAVLVHSGYSCHAGHYYCYVK-ASNGQWYQMNDSLV 402
Cdd:cd02668   219 KLNASISFPEILDMGEYlAESDEGSYV-YELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDV 284
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
123-420 1.76e-34

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: 135.31  E-value: 1.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  123 GLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSCHQGSfcMLCVMQNHIVQAFANSGNAIKPVS-FIRDLKkiARHF 201
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQS--VMKKLQLLQAHLMHTQRRAEAPPDyFLEASR--PPWF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  202 RFGNQEDAHEFLRYTIDamqkaclngcaKLDrqtqatTLVHQIFGGYLRSRVKCSVCKSVSDTYD--PYLDVALeirqaA 279
Cdd:cd02664    77 TPGSQQDCSEYLRYLLD-----------RLH------TLIEKMFGGKLSTTIRCLNCNSTSARTErfRDLDLSF-----P 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  280 NIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA-NFSGG---KITKDVGYPEFLNI---- 351
Cdd:cd02664   135 SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSyDQKTHvreKIMDNVSINEVLSLpvrv 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  352 ----------RPYMSQNNGD-----PVMYGLYAVLVHSGYSCHAGHYYCYV---------------------KASNGQWY 395
Cdd:cd02664   215 eskssespleKKEEESGDDGelvtrQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNWY 294
                         330       340       350
                  ....*....|....*....|....*....|..
gi 767995416  396 QMNDSLVHSSNVKVVLN-------QQAYVLFY 420
Cdd:cd02664   295 LFNDSRVTFSSFESVQNvtsrfpkDTPYILFY 326
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
123-423 6.92e-27

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 111.82  E-value: 6.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  123 GLHNLGNTCFLNATIQCLT-YTPPLANYL--LSKEharschqgsfcmLCVMQNHIVQAFA--NSGNAIKPVSFIRDLK-- 195
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlYLPKLDELLddLSKE------------LKVLKNVIRKPEPdlNQEEALKLFTALWSSKeh 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  196 KIARHFRFGNQEDAHEFLRYTIDAMqkaclngcaKLDRQTQATTLVHQIFGGYLRSRVkcsvcKSVSDTYdpyldVALEI 275
Cdd:COG5533    69 KVGWIPPMGSQEDAHELLGKLLDEL---------KLDLVNSFTIRIFKTTKDKKKTST-----GDWFDII-----IELPD 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  276 RQAANIVRALELFVKAD---------VLSGENAYMCAKCKKKVPASKRftihRTSNVLTLSLKRFANFSGG-KITKDVGY 345
Cdd:COG5533   130 QTWVNNLKTLQEFIDNMeelvddetgVKAKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANLGGNqKIDTEVDE 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  346 PEFLNIRPYMSQNNGDPVMYGLYAVLVHSGySCHAGHYYCYVKaSNGQWYQMNDSLVHSSNVKVVLN---QQAYVLFYLR 422
Cdd:COG5533   206 KFELPVKHDQILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPVSEEEAINekaKNAYLYFYER 283

                  .
gi 767995416  423 I 423
Cdd:COG5533   284 I 284
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
123-420 1.49e-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 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: 108.56  E-value: 1.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  123 GLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSC----------------HQGSFCMLCVMQNHIVQAFANSGNAIK 186
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSdvvdpandlncqliklADGLLSGRYSKPASLKSENDPYQVGIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  187 PVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAClngcaKLDRQTQATTLvhqiFGGYLRSRVKCSVCKSVSDTYD 266
Cdd:cd02658    81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRES-----FKNLGLNPNDL----FKFMIEDRLECLSCKKVKYTSE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  267 P--YLDVALEIRQAANIVRALELFVKADV-------LSGE-NAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSG 336
Cdd:cd02658   152 LseILSLPVPKDEATEKEEGELVYEPVPLedclkayFAPEtIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLEN 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  337 G---KITKDVGYPEFLnirpymsqnngDPVMYGLYAVLVHSGYSCHAGHYYCYVK---ASNGQWYQMNDSLVHSSNVKVV 410
Cdd:cd02658   232 WvpkKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVVASQDPPE 300
                         330
                  ....*....|
gi 767995416  411 LNQQAYVLFY 420
Cdd:cd02658   301 MKKLGYIYFY 310
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
122-420 2.70e-24

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 105.36  E-value: 2.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  122 AGLHNLGNTCFLNATIQCLTYTPPLAN---YLLSKEHARSCHQGSFcmlcvMQNHivQAFANSGNAIKPVSFIRDLKKIA 198
Cdd:cd02671    25 VGLNNLGNTCYLNSVLQVLYFCPGFKHglkHLVSLISSVEQLQSSF-----LLNP--EKYNDELANQAPRRLLNALREVN 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  199 RHFRFGNQEDAHEFLRYTIDAMQKaclngcakldrqtqattLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQA 278
Cdd:cd02671    98 PMYEGYLQHDAQEVLQCILGNIQE-----------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQES 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  279 -------------------ANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFS---- 335
Cdd:cd02671   161 elskseesseispdpktemKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGsefd 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  336 --GG--KITKDVGYPEFLNIRPYMSQNNGDpvMYGLYAVLVHSGYSCHAGHYYCYVKasngqWYQMNDSLVHSSNVKVVL 411
Cdd:cd02671   241 cyGGlsKVNTPLLTPLKLSLEEWSTKPKND--VYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKDFL 313
                         330
                  ....*....|....*...
gi 767995416  412 N---------QQAYVLFY 420
Cdd:cd02671   314 EalspntsstSTPYLLFY 331
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
123-454 2.94e-23

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 107.26  E-value: 2.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  123 GLHNLGNTCFLNATIQCLTYTPPLAN--YLLSKEHARschqGSFCMLCVMQnhivQAFANSGNAIKPV-------SFIRD 193
Cdd:COG5077   195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPR----GRDSVALALQ----RLFYNLQTGEEPVdtteltrSFGWD 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  194 lkkIARHFrfgNQEDAHEFLRYTIDAMQKAClngcakldRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVAL 273
Cdd:COG5077   267 ---SDDSF---MQHDIQEFNRVLQDNLEKSM--------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL 332
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  274 EIRQAANIVRALELFVKADVLSGENAYMCAKcKKKVPASKRFTIHRTSNVLTLSLKRF-ANFSGG---KITKDVGYPEFL 349
Cdd:COG5077   333 NVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEI 411
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  350 NIRPYMSQN-----NGDPVmYGLYAVLVHSGySCHAGHYYCYVKAS-NGQWYQMNDSLVHSSNVKVVLNQ---------- 413
Cdd:COG5077   412 DLLPFLDRDadkseNSDAV-YVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykd 489
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767995416  414 ------------QAYVLFYLRipgsKKSPEGLISrtgssslPGRPSVIPDHSK 454
Cdd:COG5077   490 kirdhsgikrfmSAYMLVYLR----KSMLDDLLN-------PVAAVDIPPHVE 531
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
122-402 5.05e-19

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 89.25  E-value: 5.05e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416   122 AGLHNLGNTCFLNATIQCLTYTPPLANYLLSkeHARSCHQGSFCMLCVM------------QNhiVQAfANsgnaikpvs 189
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCELgflfdmlekakgKN--CQA-SN--------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416   190 FIRDLKKIARHFRFGNQEDAHE-------------FLRYTIDAMQKaclNGCAKLDRQTQATTLVHQIFGGYLRSRVKCS 256
Cdd:pfam13423   67 FLRALSSIPEASALGLLDEDREtnsaislssliqsFNRFLLDQLSS---EENSTPPNPSPAESPLEQLFGIDAETTIRCS 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416   257 VCKSVSDTYDPYLDVALEI-RQAANIVRALELFVKADVL----SGENAY--MCAKCKKKVPASKRFTIHRTSNVLTLSLK 329
Cdd:pfam13423  144 NCGHESVRESSTHVLDLIYpRKPSSNNKKPPNQTFSSILksslERETTTkaWCEKCKRYQPLESRRTVRNLPPVLSLNAA 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416   330 RFaNFSGGKITKDVGY-PEFLNIRPYM-SQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASN--------GQWYQMND 399
Cdd:pfam13423  224 LT-NEEWRQLWKTPGWlPPEIGLTLSDdLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKVADseledpteSQWYLFND 302

                   ...
gi 767995416   400 SLV 402
Cdd:pfam13423  303 FLV 305
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
123-402 6.11e-19

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: 88.93  E-value: 6.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  123 GLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHARSCHQGSFCMLCVMQNHIVQAFANSGNAIKPVSFIRDLKKIARHF- 201
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQFa 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  202 ---RFGN--QEDAHEFLRYTIDAMQkaclngcAKLDRQTQATTLVHQIFGGYLRSRVKC---SVCKSVSDTYDPYLDVAL 273
Cdd:cd02657    81 ekqNQGGyaQQDAEECWSQLLSVLS-------QKLPGAGSKGSFIDQLFGIELETKMKCtesPDEEEVSTESEYKLQCHI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  274 EIRQaanIVRALELFVKADvLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRF-----ANfSGGKITKDVGYPEF 348
Cdd:cd02657   154 SITT---EVNYLQDGLKKG-LEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFfwkrdIQ-KKAKILRKVKFPFE 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767995416  349 LNIRPYMSqNNGdpvMYGLYAVLVHSGYSCHAGHYYCYVKASN-GQWYQMNDSLV 402
Cdd:cd02657   229 LDLYELCT-PSG---YYELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDDKV 279
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
123-420 1.97e-17

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 82.80  E-value: 1.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  123 GLHNLGNTCFLNATIQCLTytpplanyllskeharSChqgsfcmlcvmqnhivqafansgnaikpVSFIRDLKkiarhfR 202
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALA----------------SL----------------------------PSLIEYLE------E 30
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  203 FGNQEDAHEFLRYTIDAMQKACLNgcakldrqtqattlvhqIFGGYLRSRVKCSVCKSVS-DTYDPYLDVALEIRQA--- 278
Cdd:cd02662    31 FLEQQDAHELFQVLLETLEQLLKF-----------------PFDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQssg 93
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  279 --ANIVRALELFVKADVLSGenaYMCAKCKKKVPASKRftihrtsnVLTLSLKRFAnFSG-GKITKD---VGYPEFLNir 352
Cdd:cd02662    94 sgTTLEHCLDDFLSTEIIDD---YKCDRCQTVIVRLPQ--------ILCIHLSRSV-FDGrGTSTKNsckVSFPERLP-- 159
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  353 pymsqnngdPVMYGLYAVLVHSGySCHAGHYYCYVKAS---------------------NGQWYQMNDSLV-HSSNVKVV 410
Cdd:cd02662   160 ---------KVLYRLRAVVVHYG-SHSSGHYVCYRRKPlfskdkepgsfvrmregpsstSHPWWRISDTTVkEVSESEVL 229
                         330
                  ....*....|
gi 767995416  411 LNQQAYVLFY 420
Cdd:cd02662   230 EQKSAYMLFY 239
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
123-275 1.11e-16

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 85.32  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  123 GLHNLGNTCFLNATIQCLTYTPPLANYLLSKEHA----RSCHQGsfcmlcvMQNHIVQAFAN------SGN--AIKPVSF 190
Cdd:COG5560   267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEesinEENPLG-------MHGSVASAYADlikqlyDGNlhAFTPSGF 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  191 IRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKAcLNGCA-------------------KLDRQT------QATTLVHQIF 245
Cdd:COG5560   340 KKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHED-LNRIIkkpytskpdlspgddvvvkKKAKECwwehlkRNDSIITDLF 418
                         170       180       190
                  ....*....|....*....|....*....|
gi 767995416  246 GGYLRSRVKCSVCKSVSDTYDPYLDVALEI 275
Cdd:COG5560   419 QGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
285-422 1.12e-16

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 85.32  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  285 LELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEF-LNIRPYMSQNNGD 361
Cdd:COG5560   681 LNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSsvRSFRDKIDDLVEYPIDdLDLSGVEYMVDDP 760
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767995416  362 PVMYGLYAVLVHSGYScHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYLR 422
Cdd:COG5560   761 RLIYDLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
123-413 1.22e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 71.20  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  123 GLHNLGNTCFLNATIQCLTYTPPLANYLLSKE----HARSCHQgsfcmlcvmqnhIVQAFA-------NSgNAIK----P 187
Cdd:cd02669   121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYEnyenIKDRKSE------------LVKRLSelirkiwNP-RNFKghvsP 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  188 VSFIRDLKKI-ARHFRFGNQEDAHEFLRYTIDAMqKACLNGCAKldrqtQATTLVHQIFGGYLR---------------- 250
Cdd:cd02669   188 HELLQAVSKVsKKKFSITEQSDPVEFLSWLLNTL-HKDLGGSKK-----PNSSIIHDCFQGKVQietqkikphaeeegsk 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  251 -SRVKCSVCKSVSDTYDPYLDVALEIR------QAANIVRALELFvkaDVLSGENAYMCAKCKKKVpasKRFTIHRTSNV 323
Cdd:cd02669   262 dKFFKDSRVKKTSVSPFLLLTLDLPPPplfkdgNEENIIPQVPLK---QLLKKYDGKTETELKDSL---KRYLISRLPKY 335
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  324 LTLSLKRF--ANFSGGKITKDVGYP-EFLNIRPYMSQNNGD---PVMYGLYAVLVHSGYSCHAGHYYCYV-KASNGQWYQ 396
Cdd:cd02669   336 LIFHIKRFskNNFFKEKNPTIVNFPiKNLDLSDYVHFDKPSlnlSTKYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFE 415
                         330
                  ....*....|....*..
gi 767995416  397 MNDslvhsSNVKVVLNQ 413
Cdd:cd02669   416 IQD-----LNVKEVLPQ 427
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
124-420 2.81e-09

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


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 59.08  E-value: 2.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  124 LHNLGNTCFLNATIQCLTYTpplanyllskeharschqgsfcmlcvmqNHIVQAFANSgnaikpvsfirdlkkiarhfrf 203
Cdd:cd02673     2 LVNTGNSCYFNSTMQALSSI----------------------------GKINTEFDND---------------------- 31
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  204 gNQEDAHEFLRYTI----DAMQKACLNGCAKLDRQTQATTLvhQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQaa 279
Cdd:cd02673    32 -DQQDAHEFLLTLLeaidDIMQVNRTNVPPSNIEIKRLNPL--EAFKYTIESSYVCIGCSFEENVSDVGNFLDVSMID-- 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  280 NIVRALELFVKADVLSGENAYMCAKCKKKVpASKRFTIHRTSNVLTLSLKRF-ANFSGGKITKDvgypEFLNIRPYMSQn 358
Cdd:cd02673   107 NKLDIDELLISNFKTWSPIEKDCSSCKCES-AISSERIMTFPECLSINLKRYkLRIATSDYLKK----NEEIMKKYCGT- 180
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767995416  359 ngdPVMYGLYAVLVHSGYSCHAGHYYCYVKAS--NGQWYQMNDSLVH---SSNVKVVLNQQAYVLFY 420
Cdd:cd02673   181 ---DAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEIRpvsKNDVSTNARSSGYLIFY 244
PHA03247 PHA03247
large tegument protein UL36; Provisional
506-840 9.27e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 9.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  506 PPKLPSGSPSPKLSQTPTHMPTILDDPGKKVKKPAPPQHFSPRTAQGL-------------------------------- 553
Cdd:PHA03247 2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLgraaqassppqrprrraarptvgsltsladpp 2702
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  554 -----PGTSNSNSSRSGSQRQGSWDSRDVVLSTSPKLLATATANGHGLKGNDESAGLDRRGSSSSSPEHSASSDSTKAPQ 628
Cdd:PHA03247 2703 pppptPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  629 TPRSGAAHLCDSQETncstaghSKTPPSGADSKTVKLKSPVLSNTTTEPASTMSPPPAKKLALSAKKASTL--------W 700
Cdd:PHA03247 2783 LTRPAVASLSESRES-------LPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPppslplggS 2855
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  701 RATGNDLRPPPPSPSSdLTHPMKTSHPvvastwPVHRARAVSPAPQSSSRLQPPFSPHPtllssTPKPPGTSEPRscssi 780
Cdd:PHA03247 2856 VAPGGDVRRRPPSRSP-AAKPAAPARP------PVRRLARPAVSRSTESFALPPDQPER-----PPQPQAPPPPQ----- 2918
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767995416  781 stalPQVNEDLVSLPHQLPEASEPPQSPSEKRKKTF-VGEPQRLGSETRLPQHIREATAAP 840
Cdd:PHA03247 2919 ----PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAgAGEPSGAVPQPWLGALVPGRVAVP 2975
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
123-421 2.62e-05

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: 46.78  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  123 GLHNLGNTCFLNATIQCLtytpplanyllskeharschqgsfcmlcvmqnhivqafansgnaikpvsfirdlkkiarhfr 202
Cdd:cd02665     1 GLKNVGNTCWFSAVIQSL-------------------------------------------------------------- 18
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  203 FGNQEDAHEFLRYTIDAMQKA-------------CLNGCAKLDRQTQATTLVHqiFGGYLRsrvKCSVCKSVSDTYDPY- 268
Cdd:cd02665    19 FSQQQDVSEFTHLLLDWLEDAfqaaaeaispgekSKNPMVQLFYGTFLTEGVL--EGKPFC---NCETFGQYPLQVNGYg 93
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  269 -LDVALEirqAANI-VRALELFVKADVLSG-ENAYMcakckkKVPAskrftihrtsnVLTLSLKRFA--NFSGGKITKDV 343
Cdd:cd02665    94 nLHECLE---AAMFeGEVELLPSDHSVKSGqERWFT------ELPP-----------VLTFELSRFEfnQGRPEKIHDKL 153
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995416  344 GYPEFLNIRPYMsqnngdpvmygLYAVLVHSGySCHAGHYYCYV-KASNGQWYQMND-SLVHSSNVKVV-------LNQQ 414
Cdd:cd02665   154 EFPQIIQQVPYE-----------LHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYNDiSVTESSWEEVErdsfgggRNPS 221

                  ....*..
gi 767995416  415 AYVLFYL 421
Cdd:cd02665   222 AYCLMYI 228
 
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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