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Conserved domains on  [gi|1867163780|ref|NP_001372109|]
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ubiquitin carboxyl-terminal hydrolase 36 isoform 5 [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase family protein( domain architecture ID 913)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1-202 5.08e-115

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


The actual alignment was detected with superfamily member cd02661:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 304  Bit Score: 353.50  E-value: 5.08e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780   1 MQKACLNGCAKL---DRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSG 77
Cdd:cd02661   100 MQKACLDRFKKLkavDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDG 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  78 ENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQNNGDPVMYGLYAVLVHSGY 157
Cdd:cd02661   180 ENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQPNDGPLKYKLYAVLVHSGF 259
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1867163780 158 SCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYL 202
Cdd:cd02661   260 SPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
PHA03247 super family cl33720
large tegument protein UL36; Provisional
287-621 1.96e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  287 PPKLPSGSPSPKLSQTPTHMPTILDDPGKKVKKPAPPQHFSPRTAQGL-------------------------------- 334
Cdd:PHA03247  2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLgraaqassppqrprrraarptvgsltsladpp 2702
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  335 -----PGTSNSNSSRSGSQRQGSWDSRDVVLSTSPKLLATATANGHGLKGNDESAGLDRRGSSSSSPEHSASSDSTKAPQ 409
Cdd:PHA03247  2703 pppptPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  410 TPRSGAAHLCDSQETNCStaghsktPPSGADSKTVKLKSPVLSNTTTEPASTMSPPPAKKLALSAKKASTL--------W 481
Cdd:PHA03247  2783 LTRPAVASLSESRESLPS-------PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPppslplggS 2855
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  482 RATGNDLRPPPPSPSSdLTHPMKTSHPvvastwPVHRARAVSPAPQSSSRLQPPFSPHPtllssTPKPPGTSEPRscssi 561
Cdd:PHA03247  2856 VAPGGDVRRRPPSRSP-AAKPAAPARP------PVRRLARPAVSRSTESFALPPDQPER-----PPQPQAPPPPQ----- 2918
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1867163780  562 stalPQVNEDLVSLPHQLPEASEPPQSPSEKRKKTF-VGEPQRLGSETRLPQHIREATAAP 621
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 ...
1-202 5.08e-115

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: 353.50  E-value: 5.08e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780   1 MQKACLNGCAKL---DRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSG 77
Cdd:cd02661   100 MQKACLDRFKKLkavDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDG 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  78 ENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQNNGDPVMYGLYAVLVHSGY 157
Cdd:cd02661   180 ENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQPNDGPLKYKLYAVLVHSGF 259
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1867163780 158 SCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYL 202
Cdd:cd02661   260 SPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
19-201 3.88e-46

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 168.00  E-value: 3.88e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  19 TTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVR------ALELFVKADVLSGENAYMCAKCKKKVPA 92
Cdd:pfam00443 115 ESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDA 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  93 SKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEFLNIRPYMSQNN----GDPVMYGLYAVLVHSGySCHAGHYYC 166
Cdd:pfam00443 195 IKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELDLSRYLAEELkpktNNLQDYRLVAVVVHSG-SLSSGHYIA 273
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1867163780 167 YVKA-SNGQWYQMNDSLV-HSSNVKVVLNQQAYVLFY 201
Cdd:pfam00443 274 YIKAyENNRWYKFDDEKVtEVDEETAVLSSSAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
14-235 7.55e-18

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 89.16  E-value: 7.55e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780   14 RQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKcKKKVPAS 93
Cdd:COG5077    292 RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAK 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780   94 KRFTIHRTSNVLTLSLKRF-ANFSGG---KITKDVGYPEFLNIRPYMSQN-----NGDPVmYGLYAVLVHSGySCHAGHY 164
Cdd:COG5077    371 KGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEIDLLPFLDRDadkseNSDAV-YVLYGVLVHSG-DLHEGHY 448
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  165 YCYVKAS-NGQWYQMNDSLVHSSNVKVVLNQ----------------------QAYVLFYLRipgsKKSPEGLISrtgss 221
Cdd:COG5077    449 YALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdhsgikrfmSAYMLVYLR----KSMLDDLLN----- 519
                          250
                   ....*....|....
gi 1867163780  222 slPGRPSVIPDHSK 235
Cdd:COG5077    520 --PVAAVDIPPHVE 531
PHA03247 PHA03247
large tegument protein UL36; Provisional
287-621 1.96e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  287 PPKLPSGSPSPKLSQTPTHMPTILDDPGKKVKKPAPPQHFSPRTAQGL-------------------------------- 334
Cdd:PHA03247  2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLgraaqassppqrprrraarptvgsltsladpp 2702
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  335 -----PGTSNSNSSRSGSQRQGSWDSRDVVLSTSPKLLATATANGHGLKGNDESAGLDRRGSSSSSPEHSASSDSTKAPQ 409
Cdd:PHA03247  2703 pppptPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  410 TPRSGAAHLCDSQETNCStaghsktPPSGADSKTVKLKSPVLSNTTTEPASTMSPPPAKKLALSAKKASTL--------W 481
Cdd:PHA03247  2783 LTRPAVASLSESRESLPS-------PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPppslplggS 2855
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  482 RATGNDLRPPPPSPSSdLTHPMKTSHPvvastwPVHRARAVSPAPQSSSRLQPPFSPHPtllssTPKPPGTSEPRscssi 561
Cdd:PHA03247  2856 VAPGGDVRRRPPSRSP-AAKPAAPARP------PVRRLARPAVSRSTESFALPPDQPER-----PPQPQAPPPPQ----- 2918
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1867163780  562 stalPQVNEDLVSLPHQLPEASEPPQSPSEKRKKTF-VGEPQRLGSETRLPQHIREATAAP 621
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 ...
1-202 5.08e-115

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: 353.50  E-value: 5.08e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780   1 MQKACLNGCAKL---DRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSG 77
Cdd:cd02661   100 MQKACLDRFKKLkavDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDG 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  78 ENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQNNGDPVMYGLYAVLVHSGY 157
Cdd:cd02661   180 ENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQPNDGPLKYKLYAVLVHSGF 259
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1867163780 158 SCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYL 202
Cdd:cd02661   260 SPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1-201 1.01e-51

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: 181.91  E-value: 1.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780   1 MQKACLNGCAKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDP--YLDVALEIRQAA--NIVRALELFVKADVLS 76
Cdd:cd02257    36 LHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPelFLSLPLPVKGLPqvSLEDCLEKFFKEEILE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  77 GENAYMCaKCKKKVPASKRFTIHRTSNVLTLSLKRFA---NFSGGKITKDVGYPEFLNIRPYMSQNNGD------PVMYG 147
Cdd:cd02257   116 GDNCYKC-EKKKKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYLSEGEKDsdsdngSYKYE 194
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780 148 LYAVLVHSGYSCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVL-----NQQAYVLFY 201
Cdd:cd02257   195 LVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFY 254
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
22-201 1.31e-46

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 169.86  E-value: 1.31e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  22 VHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRA---------------LELFVKADVLsGENAYMCAKC 86
Cdd:cd02660   123 IHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWAlgesgvsgtptlsdcLDRFTRPEKL-GDFAYKCSGC 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  87 KKKVPASKRFTIHRTSNVLTLSLKRFANFSGG---KITKDVGYPEFLNIRPYMSQNNGDPVM---------YGLYAVLVH 154
Cdd:cd02660   202 GSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKIDTYVQFPLELNMTPYTSSSIGDTQDsnsldpdytYDLFAVVVH 281
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1867163780 155 SGySCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFY 201
Cdd:cd02660   282 KG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
19-201 3.88e-46

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 168.00  E-value: 3.88e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  19 TTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVR------ALELFVKADVLSGENAYMCAKCKKKVPA 92
Cdd:pfam00443 115 ESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDA 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  93 SKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEFLNIRPYMSQNN----GDPVMYGLYAVLVHSGySCHAGHYYC 166
Cdd:pfam00443 195 IKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELDLSRYLAEELkpktNNLQDYRLVAVVVHSG-SLSSGHYIA 273
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1867163780 167 YVKA-SNGQWYQMNDSLV-HSSNVKVVLNQQAYVLFY 201
Cdd:pfam00443 274 YIKAyENNRWYKFDDEKVtEVDEETAVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
21-201 1.80e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 151.67  E-value: 1.80e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  21 LVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRA------LELFVKADVLSGENAYMCAKCKKKVPASK 94
Cdd:cd02674    39 IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAPKvtledcLRLFTKEETLDGDNAWKCPKCKKKRKATK 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  95 RFTIHRTSNVLTLSLKRFaNFSGG---KITKDVGYP-EFLNIRPY-MSQNNGDPVMYGLYAVLVHSGySCHAGHYYCYVK 169
Cdd:cd02674   119 KLTISRLPKVLIIHLKRF-SFSRGstrKLTTPVTFPlNDLDLTPYvDTRSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCK 196
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1867163780 170 -ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFY 201
Cdd:cd02674   197 nNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
20-201 5.06e-40

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: 149.46  E-value: 5.06e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  20 TLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVAL----EIRQAANIVRALELFVKADVLSGENAYMCAKCKKkvpASKR 95
Cdd:cd02667    67 TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSECSIESCLKQFTEVEILEGNNKFACENCTK---AKKQ 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  96 FTIHRTSNVLTLSLKRF-----ANFSggKITKDVGYPEFLNIRPYMSQNN-----GDPVMYGLYAVLVHSGySCHAGHYY 165
Cdd:cd02667   144 YLISKLPPVLVIHLKRFqqprsANLR--KVSRHVSFPEILDLAPFCDPKCnssedKSSVLYRLYGVVEHSG-TMRSGHYV 220
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1867163780 166 CYVKASN----------------------GQWYQMNDSLVHSSNVKVVLNQQAYVLFY 201
Cdd:cd02667   221 AYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-204 2.76e-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: 145.86  E-value: 2.76e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780   1 MQKACLNGCAKLDRQTQATT---LVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSG 77
Cdd:cd02659    89 VQEFFRVLFDKLEEKLKGTGqegLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEG 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  78 ENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFaNF-----SGGKITKDVGYPEFLNIRPYMSQNNG----------- 141
Cdd:cd02659   169 DNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRF-EFdfetmMRIKINDRFEFPLELDMEPYTEKGLAkkegdsekkds 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780 142 DPVMYGLYAVLVHSGySCHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQ----------------------AYV 198
Cdd:cd02659   248 ESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECfggeetqktydsgprafkrttnAYM 326

                  ....*.
gi 1867163780 199 LFYLRI 204
Cdd:cd02659   327 LFYERK 332
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
18-201 1.78e-29

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 119.34  E-value: 1.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  18 ATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFT 97
Cdd:cd02663   105 QPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMK 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  98 IHRTSNVLTLSLKRFA-NFSGGKITK---DVGYPEFLNIRPYMSQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKaSNG 173
Cdd:cd02663   185 IKKLPKILALHLKRFKyDEQLNRYIKlfyRVVFPLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVK-SHG 263
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1867163780 174 QWYQMND---SLVHSSNVKVVLNQ-----QAYVLFY 201
Cdd:cd02663   264 GWLLFDDetvEKIDENAVEEFFGDspnqaTAYVLFY 299
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
18-183 4.58e-26

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: 110.20  E-value: 4.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  18 ATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFT 97
Cdd:cd02668   114 LKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIR 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  98 IHRTSNVLTLSLKRFA----NFSGGKITKDVGYPEFLNIRPY-MSQNNGDPVmYGLYAVLVHSGYSCHAGHYYCYVK-AS 171
Cdd:cd02668   194 LTTLPPTLNFQLLRFVfdrkTGAKKKLNASISFPEILDMGEYlAESDEGSYV-YELSGVLIHQGVSAYSGHYIAHIKdEQ 272
                         170
                  ....*....|..
gi 1867163780 172 NGQWYQMNDSLV 183
Cdd:cd02668   273 TGEWYKFNDEDV 284
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
8-201 1.51e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 108.73  E-value: 1.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780   8 GCAKLDRqtqATTLVHQIFGGYLRSRVKCSVCKSVSDTYD--PYLDVALeirqaANIVRALELFVKADVLSGENAYMCAK 85
Cdd:cd02664    88 LRYLLDR---LHTLIEKMFGGKLSTTIRCLNCNSTSARTErfRDLDLSF-----PSVQDLLNYFLSPEKLTGDNQYYCEK 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  86 CKKKVPASKRFTIHRTSNVLTLSLKRFA-NFSGG---KITKDVGYPEFLNI--------------RPYMSQNNGD----- 142
Cdd:cd02664   160 CASLQDAEKEMKVTGAPEYLILTLLRFSyDQKTHvreKIMDNVSINEVLSLpvrveskssespleKKEEESGDDGelvtr 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780 143 PVMYGLYAVLVHSGYSCHAGHYYCYV---------------------KASNGQWYQMNDSLVHSSNVKVVLN-------Q 194
Cdd:cd02664   240 QVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNWYLFNDSRVTFSSFESVQNvtsrfpkD 319

                  ....*..
gi 1867163780 195 QAYVLFY 201
Cdd:cd02664   320 TPYILFY 326
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
14-235 7.55e-18

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 89.16  E-value: 7.55e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780   14 RQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKcKKKVPAS 93
Cdd:COG5077    292 RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAK 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780   94 KRFTIHRTSNVLTLSLKRF-ANFSGG---KITKDVGYPEFLNIRPYMSQN-----NGDPVmYGLYAVLVHSGySCHAGHY 164
Cdd:COG5077    371 KGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEIDLLPFLDRDadkseNSDAV-YVLYGVLVHSG-DLHEGHY 448
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  165 YCYVKAS-NGQWYQMNDSLVHSSNVKVVLNQ----------------------QAYVLFYLRipgsKKSPEGLISrtgss 221
Cdd:COG5077    449 YALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdhsgikrfmSAYMLVYLR----KSMLDDLLN----- 519
                          250
                   ....*....|....
gi 1867163780  222 slPGRPSVIPDHSK 235
Cdd:COG5077    520 --PVAAVDIPPHVE 531
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
66-203 8.01e-17

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 85.32  E-value: 8.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  66 LELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEF-LNIRPYMSQNNGD 142
Cdd:COG5560   681 LNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSsvRSFRDKIDDLVEYPIDdLDLSGVEYMVDDP 760
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1867163780 143 PVMYGLYAVLVHSGYScHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYLR 203
Cdd:COG5560   761 RLIYDLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
21-201 8.65e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 70.69  E-value: 8.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  21 LVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQA-------------------ANIVRALELFVKADVLSGENAY 81
Cdd:cd02671   122 LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESelskseesseispdpktemKTLKWAISQFASVERIVGEDKY 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  82 MCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFS------GG--KITKDVGYPEFLNIRPYMSQNNGDpvMYGLYAVLV 153
Cdd:cd02671   202 FCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGsefdcyGGlsKVNTPLLTPLKLSLEEWSTKPKND--VYRLFAVVM 279
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1867163780 154 HSGYSCHAGHYYCYVKasngqWYQMNDSLVHSSNVKVVLN---------QQAYVLFY 201
Cdd:cd02671   280 HSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKDFLEalspntsstSTPYLLFY 331
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
16-183 1.47e-12

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 69.61  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  16 TQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEI-RQAANIVRALELFVKADVL----SGENAY--MCAKCKK 88
Cdd:pfam13423 122 SPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDLIYpRKPSSNNKKPPNQTFSSILksslERETTTkaWCEKCKR 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  89 KVPASKRFTIHRTSNVLTLSLKRFaNFSGGKITKDVGY-PEFLNIRPYM-SQNNGDPVMYGLYAVLVHSGYSCHAGHYYC 166
Cdd:pfam13423 202 YQPLESRRTVRNLPPVLSLNAALT-NEEWRQLWKTPGWlPPEIGLTLSDdLQGDNEIVKYELRGVVVHIGDSGTSGHLVS 280
                         170       180
                  ....*....|....*....|....*
gi 1867163780 167 YVKASN--------GQWYQMNDSLV 183
Cdd:pfam13423 281 FVKVADseledpteSQWYLFNDFLV 305
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
97-204 1.65e-12

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 69.06  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  97 TIHRTSNVLTLSLKRFANFSGG-KITKDVGYPEFLNIRPYMSQNNGDPVMYGLYAVLVHSGySCHAGHYYCYVKaSNGQW 175
Cdd:COG5533   175 SFVKLPKILTIQLKRFANLGGNqKIDTEVDEKFELPVKHDQILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKW 252
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1867163780 176 YQMNDSLVHSSNVKVVLN---QQAYVLFYLRI 204
Cdd:COG5533   253 EKANDSDVTPVSEEEAINekaKNAYLYFYERI 284
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
25-201 2.30e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 68.89  E-value: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  25 IFGGYLRSRVKCSVCKSVSDTYDP--YLDVALEIRQAANIVRALELFVKADV-------LSGE-NAYMCAKCKKKVPASK 94
Cdd:cd02658   129 LFKFMIEDRLECLSCKKVKYTSELseILSLPVPKDEATEKEEGELVYEPVPLedclkayFAPEtIEDFCSTCKEKTTATK 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  95 RFTIHRTSNVLTLSLKRFANFSGG---KITKDVGYPEFLnirpymsqnngDPVMYGLYAVLVHSGYSCHAGHYYCYVK-- 169
Cdd:cd02658   209 TTGFKTFPDYLVINMKRFQLLENWvpkKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKke 277
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1867163780 170 -ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFY 201
Cdd:cd02658   278 iDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
26-201 3.55e-10

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 61.23  E-value: 3.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  26 FGGYLRSRVKCSVCKSVS-DTYDPYLDVALEIRQA-----ANIVRALELFVKADVLSGenaYMCAKCKKKVPASKRftih 99
Cdd:cd02662    56 FDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQssgsgTTLEHCLDDFLSTEIIDD---YKCDRCQTVIVRLPQ---- 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780 100 rtsnVLTLSLKRFAnFSG-GKITKD---VGYPEFLNirpymsqnngdPVMYGLYAVLVHSGySCHAGHYYCYVKAS---- 171
Cdd:cd02662   129 ----ILCIHLSRSV-FDGrGTSTKNsckVSFPERLP-----------KVLYRLRAVVVHYG-SHSSGHYVCYRRKPlfsk 191
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1867163780 172 -----------------NGQWYQMNDSLV-HSSNVKVVLNQQAYVLFY 201
Cdd:cd02662   192 dkepgsfvrmregpsstSHPWWRISDTTVkEVSESEVLEQKSAYMLFY 239
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
93-183 3.54e-06

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 50.02  E-value: 3.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  93 SKRFTIHRTSNVLTLSLKRF-----ANfSGGKITKDVGYPEFLNIRPYMSqNNGdpvMYGLYAVLVHSGYSCHAGHYYCY 167
Cdd:cd02657   188 TKTSRISRLPKYLTVQFVRFfwkrdIQ-KKAKILRKVKFPFELDLYELCT-PSG---YYELVAVITHQGRSADSGHYVAW 262
                          90
                  ....*....|....*..
gi 1867163780 168 VKASN-GQWYQMNDSLV 183
Cdd:cd02657   263 VRRKNdGKWIKFDDDKV 279
PHA03247 PHA03247
large tegument protein UL36; Provisional
287-621 1.96e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  287 PPKLPSGSPSPKLSQTPTHMPTILDDPGKKVKKPAPPQHFSPRTAQGL-------------------------------- 334
Cdd:PHA03247  2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLgraaqassppqrprrraarptvgsltsladpp 2702
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  335 -----PGTSNSNSSRSGSQRQGSWDSRDVVLSTSPKLLATATANGHGLKGNDESAGLDRRGSSSSSPEHSASSDSTKAPQ 409
Cdd:PHA03247  2703 pppptPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  410 TPRSGAAHLCDSQETNCStaghsktPPSGADSKTVKLKSPVLSNTTTEPASTMSPPPAKKLALSAKKASTL--------W 481
Cdd:PHA03247  2783 LTRPAVASLSESRESLPS-------PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPppslplggS 2855
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  482 RATGNDLRPPPPSPSSdLTHPMKTSHPvvastwPVHRARAVSPAPQSSSRLQPPFSPHPtllssTPKPPGTSEPRscssi 561
Cdd:PHA03247  2856 VAPGGDVRRRPPSRSP-AAKPAAPARP------PVRRLARPAVSRSTESFALPPDQPER-----PPQPQAPPPPQ----- 2918
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1867163780  562 stalPQVNEDLVSLPHQLPEASEPPQSPSEKRKKTF-VGEPQRLGSETRLPQHIREATAAP 621
Cdd:PHA03247  2919 ----PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAgAGEPSGAVPQPWLGALVPGRVAVP 2975
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
75-201 1.47e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 44.44  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  75 LSGENAYMCAKCKK--KVPASKRF----TIHRTSNVLTLSLKRFANFS-------------GGKITKDVGYPEFLNI--- 132
Cdd:cd02673    76 YTIESSYVCIGCSFeeNVSDVGNFldvsMIDNKLDIDELLISNFKTWSpiekdcssckcesAISSERIMTFPECLSInlk 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780 133 ---------------RPYMSQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKAS--NGQWYQMNDSLVH---SSNVKVVL 192
Cdd:cd02673   156 ryklriatsdylkknEEIMKKYCGTDAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEIRpvsKNDVSTNA 235

                  ....*....
gi 1867163780 193 NQQAYVLFY 201
Cdd:cd02673   236 RSSGYLIFY 244
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
104-202 1.88e-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: 43.70  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780 104 VLTLSLKRFA--NFSGGKITKDVGYPEFLNIRPYMsqnngdpvmygLYAVLVHSGySCHAGHYYCYV-KASNGQWYQMND 180
Cdd:cd02665   131 VLTFELSRFEfnQGRPEKIHDKLEFPQIIQQVPYE-----------LHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYND 198
                          90       100       110
                  ....*....|....*....|....*....|
gi 1867163780 181 -SLVHSSNVKVV-------LNQQAYVLFYL 202
Cdd:cd02665   199 iSVTESSWEEVErdsfgggRNPSAYCLMYI 228
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
91-194 2.49e-03

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 41.15  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163780  91 PASKRFTIHRTSNVLTLSLKRF--ANFSGGKITKDVGYP-EFLNIRPYMSQNNGD---PVMYGLYAVLVHSGYSCHAGHY 164
Cdd:cd02669   322 DSLKRYLISRLPKYLIFHIKRFskNNFFKEKNPTIVNFPiKNLDLSDYVHFDKPSlnlSTKYNLVANIVHEGTPQEDGTW 401
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1867163780 165 YCYV-KASNGQWYQMNDslvhsSNVKVVLNQ 194
Cdd:cd02669   402 RVQLrHKSTNKWFEIQD-----LNVKEVLPQ 427
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
20-56 5.28e-03

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 40.64  E-value: 5.28e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1867163780  20 TLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEI 56
Cdd:COG5560   412 SIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
 
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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