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Conserved domains on  [gi|1867163782|ref|NP_001372108|]
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ubiquitin carboxyl-terminal hydrolase 36 isoform 4 [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 ...
21-211 1.03e-110

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: 342.72  E-value: 1.03e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  21 LDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVP 100
Cdd:cd02661   114 VDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVK 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782 101 ASKRFTIHRTSNVLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKAS 180
Cdd:cd02661   194 ASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSS 273
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1867163782 181 NGQWYQMNDSLVHSSNVKVVLNQQAYVLFYL 211
Cdd:cd02661   274 NGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
PHA03247 super family cl33720
large tegument protein UL36; Provisional
296-630 2.39e-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: 48.40  E-value: 2.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  296 PPKLPSGSPSPKLSQTPTHMPTILDDPGKKVKKPAPPQHFSPRTAQGL-------------------------------- 343
Cdd:PHA03247  2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLgraaqassppqrprrraarptvgsltsladpp 2702
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  344 -----PGTSNSNSSRSGSQRQGSWDSRDVVLSTSPKLLATATANGHGLKGNDESAGLDRRGSSSSSPEHSASSDSTKAPQ 418
Cdd:PHA03247  2703 pppptPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  419 TPRSGAAHLCDSQETNCStaghsktPPSGADSKTVKLKSPVLSNTTTEPASTMSPPPAKKLALSAKKASTL--------W 490
Cdd:PHA03247  2783 LTRPAVASLSESRESLPS-------PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPppslplggS 2855
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  491 RATGNDLRPPPPSPSSdLTHPMKTSHPvvastwPVHRARAVSPAPQSSSRLQPPFSPHPtllssTPKPPGTSEPRscssi 570
Cdd:PHA03247  2856 VAPGGDVRRRPPSRSP-AAKPAAPARP------PVRRLARPAVSRSTESFALPPDQPER-----PPQPQAPPPPQ----- 2918
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1867163782  571 stalPQVNEDLVSLPHQLPEASEPPQSPSEKRKKTF-VGEPQRLGSETRLPQHIREATAAP 630
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 ...
21-211 1.03e-110

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: 342.72  E-value: 1.03e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  21 LDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVP 100
Cdd:cd02661   114 VDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVK 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782 101 ASKRFTIHRTSNVLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKAS 180
Cdd:cd02661   194 ASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSS 273
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1867163782 181 NGQWYQMNDSLVHSSNVKVVLNQQAYVLFYL 211
Cdd:cd02661   274 NGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
28-210 4.00e-46

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 168.00  E-value: 4.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  28 TTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVR------ALELFVKADVLSGENAYMCAKCKKKVPA 101
Cdd:pfam00443 115 ESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDA 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782 102 SKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEFLNIRPYMSQNN----GDPVMYGLYAVLVHSGySCHAGHYYC 175
Cdd:pfam00443 195 IKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELDLSRYLAEELkpktNNLQDYRLVAVVVHSG-SLSSGHYIA 273
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1867163782 176 YVKA-SNGQWYQMNDSLV-HSSNVKVVLNQQAYVLFY 210
Cdd:pfam00443 274 YIKAyENNRWYKFDDEKVtEVDEETAVLSSSAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
23-244 7.68e-18

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 89.16  E-value: 7.68e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782   23 RQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKcKKKVPAS 102
Cdd:COG5077    292 RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAK 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  103 KRFTIHRTSNVLTLSLKRF-ANFSGG---KITKDVGYPEFLNIRPYMSQN-----NGDPVmYGLYAVLVHSGySCHAGHY 173
Cdd:COG5077    371 KGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEIDLLPFLDRDadkseNSDAV-YVLYGVLVHSG-DLHEGHY 448
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  174 YCYVKAS-NGQWYQMNDSLVHSSNVKVVLNQ----------------------QAYVLFYLRipgsKKSPEGLISrtgss 230
Cdd:COG5077    449 YALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdhsgikrfmSAYMLVYLR----KSMLDDLLN----- 519
                          250
                   ....*....|....
gi 1867163782  231 slPGRPSVIPDHSK 244
Cdd:COG5077    520 --PVAAVDIPPHVE 531
PHA03247 PHA03247
large tegument protein UL36; Provisional
296-630 2.39e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 2.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  296 PPKLPSGSPSPKLSQTPTHMPTILDDPGKKVKKPAPPQHFSPRTAQGL-------------------------------- 343
Cdd:PHA03247  2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLgraaqassppqrprrraarptvgsltsladpp 2702
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  344 -----PGTSNSNSSRSGSQRQGSWDSRDVVLSTSPKLLATATANGHGLKGNDESAGLDRRGSSSSSPEHSASSDSTKAPQ 418
Cdd:PHA03247  2703 pppptPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  419 TPRSGAAHLCDSQETNCStaghsktPPSGADSKTVKLKSPVLSNTTTEPASTMSPPPAKKLALSAKKASTL--------W 490
Cdd:PHA03247  2783 LTRPAVASLSESRESLPS-------PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPppslplggS 2855
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  491 RATGNDLRPPPPSPSSdLTHPMKTSHPvvastwPVHRARAVSPAPQSSSRLQPPFSPHPtllssTPKPPGTSEPRscssi 570
Cdd:PHA03247  2856 VAPGGDVRRRPPSRSP-AAKPAAPARP------PVRRLARPAVSRSTESFALPPDQPER-----PPQPQAPPPPQ----- 2918
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1867163782  571 stalPQVNEDLVSLPHQLPEASEPPQSPSEKRKKTF-VGEPQRLGSETRLPQHIREATAAP 630
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 ...
21-211 1.03e-110

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: 342.72  E-value: 1.03e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  21 LDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVP 100
Cdd:cd02661   114 VDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVK 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782 101 ASKRFTIHRTSNVLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKAS 180
Cdd:cd02661   194 ASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSS 273
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1867163782 181 NGQWYQMNDSLVHSSNVKVVLNQQAYVLFYL 211
Cdd:cd02661   274 NGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
25-210 2.51e-50

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: 178.06  E-value: 2.51e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  25 TQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDP--YLDVALEIRQAA--NIVRALELFVKADVLSGENAYMCaKCKKKVP 100
Cdd:cd02257    51 SSLKSLIHDLFGGKLESTIVCLECGHESVSTEPelFLSLPLPVKGLPqvSLEDCLEKFFKEEILEGDNCYKC-EKKKKQE 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782 101 ASKRFTIHRTSNVLTLSLKRFA---NFSGGKITKDVGYPEFLNIRPYMSQNNGD------PVMYGLYAVLVHSGYSCHAG 171
Cdd:cd02257   130 ATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYLSEGEKDsdsdngSYKYELVAVVVHSGTSADSG 209
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1867163782 172 HYYCYVK-ASNGQWYQMNDSLVHSSNVKVVL-----NQQAYVLFY 210
Cdd:cd02257   210 HYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFY 254
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
31-210 7.24e-47

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: 170.63  E-value: 7.24e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  31 VHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRA---------------LELFVKADVLsGENAYMCAKC 95
Cdd:cd02660   123 IHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWAlgesgvsgtptlsdcLDRFTRPEKL-GDFAYKCSGC 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  96 KKKVPASKRFTIHRTSNVLTLSLKRFANFSGG---KITKDVGYPEFLNIRPYMSQNNGDPVM---------YGLYAVLVH 163
Cdd:cd02660   202 GSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKIDTYVQFPLELNMTPYTSSSIGDTQDsnsldpdytYDLFAVVVH 281
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1867163782 164 SGySCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFY 210
Cdd:cd02660   282 KG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQAYLLFY 327
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
28-210 4.00e-46

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 168.00  E-value: 4.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  28 TTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVR------ALELFVKADVLSGENAYMCAKCKKKVPA 101
Cdd:pfam00443 115 ESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELKtaslqiCFLQFSKLEELDDEEKYYCDKCGCKQDA 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782 102 SKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEFLNIRPYMSQNN----GDPVMYGLYAVLVHSGySCHAGHYYC 175
Cdd:pfam00443 195 IKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELDLSRYLAEELkpktNNLQDYRLVAVVVHSG-SLSSGHYIA 273
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1867163782 176 YVKA-SNGQWYQMNDSLV-HSSNVKVVLNQQAYVLFY 210
Cdd:pfam00443 274 YIKAyENNRWYKFDDEKVtEVDEETAVLSSSAYILFY 310
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
30-210 1.84e-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: 1.84e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  30 LVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRA------LELFVKADVLSGENAYMCAKCKKKVPASK 103
Cdd:cd02674    39 IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAPKvtledcLRLFTKEETLDGDNAWKCPKCKKKRKATK 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782 104 RFTIHRTSNVLTLSLKRFaNFSGG---KITKDVGYP-EFLNIRPY-MSQNNGDPVMYGLYAVLVHSGySCHAGHYYCYVK 178
Cdd:cd02674   119 KLTISRLPKVLIIHLKRF-SFSRGstrKLTTPVTFPlNDLDLTPYvDTRSFTGPFKYDLYAVVNHYG-SLNGGHYTAYCK 196
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1867163782 179 -ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFY 210
Cdd:cd02674   197 nNETNDWYKFDDSRVTKVSESSVVSSSAYILFY 229
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
29-210 5.14e-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: 5.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  29 TLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVAL----EIRQAANIVRALELFVKADVLSGENAYMCAKCKKkvpASKR 104
Cdd:cd02667    67 TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSECSIESCLKQFTEVEILEGNNKFACENCTK---AKKQ 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782 105 FTIHRTSNVLTLSLKRF-----ANFSggKITKDVGYPEFLNIRPYMSQNN-----GDPVMYGLYAVLVHSGySCHAGHYY 174
Cdd:cd02667   144 YLISKLPPVLVIHLKRFqqprsANLR--KVSRHVSFPEILDLAPFCDPKCnssedKSSVLYRLYGVVEHSG-TMRSGHYV 220
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1867163782 175 CYVKASN----------------------GQWYQMNDSLVHSSNVKVVLNQQAYVLFY 210
Cdd:cd02667   221 AYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
30-213 7.50e-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: 144.71  E-value: 7.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  30 LVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFTIHR 109
Cdd:cd02659   112 LIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKK 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782 110 TSNVLTLSLKRFaNF-----SGGKITKDVGYPEFLNIRPYMSQNNG-----------DPVMYGLYAVLVHSGySCHAGHY 173
Cdd:cd02659   192 LPPVLTLQLKRF-EFdfetmMRIKINDRFEFPLELDMEPYTEKGLAkkegdsekkdsESYIYELHGVLVHSG-DAHGGHY 269
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1867163782 174 YCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQ----------------------AYVLFYLRI 213
Cdd:cd02659   270 YSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECfggeetqktydsgprafkrttnAYMLFYERK 332
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
27-210 1.80e-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: 1.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  27 ATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFT 106
Cdd:cd02663   105 QPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMK 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782 107 IHRTSNVLTLSLKRFA-NFSGGKITK---DVGYPEFLNIRPYMSQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKaSNG 182
Cdd:cd02663   185 IKKLPKILALHLKRFKyDEQLNRYIKlfyRVVFPLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVK-SHG 263
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1867163782 183 QWYQMND---SLVHSSNVKVVLNQ-----QAYVLFY 210
Cdd:cd02663   264 GWLLFDDetvEKIDENAVEEFFGDspnqaTAYVLFY 299
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
27-192 4.64e-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: 4.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  27 ATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFT 106
Cdd:cd02668   114 LKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIR 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782 107 IHRTSNVLTLSLKRFA----NFSGGKITKDVGYPEFLNIRPY-MSQNNGDPVmYGLYAVLVHSGYSCHAGHYYCYVK-AS 180
Cdd:cd02668   194 LTTLPPTLNFQLLRFVfdrkTGAKKKLNASISFPEILDMGEYlAESDEGSYV-YELSGVLIHQGVSAYSGHYIAHIKdEQ 272
                         170
                  ....*....|..
gi 1867163782 181 NGQWYQMNDSLV 192
Cdd:cd02668   273 TGEWYKFNDEDV 284
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
29-210 1.92e-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: 108.35  E-value: 1.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  29 TLVHQIFGGYLRSRVKCSVCKSVSDTYD--PYLDVALeirqaANIVRALELFVKADVLSGENAYMCAKCKKKVPASKRFT 106
Cdd:cd02664    97 TLIEKMFGGKLSTTIRCLNCNSTSARTErfRDLDLSF-----PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMK 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782 107 IHRTSNVLTLSLKRFA-NFSGG---KITKDVGYPEFLNI--------------RPYMSQNNGD-----PVMYGLYAVLVH 163
Cdd:cd02664   172 VTGAPEYLILTLLRFSyDQKTHvreKIMDNVSINEVLSLpvrveskssespleKKEEESGDDGelvtrQVHYRLYAVVVH 251
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1867163782 164 SGYSCHAGHYYCYV---------------------KASNGQWYQMNDSLVHSSNVKVVLN-------QQAYVLFY 210
Cdd:cd02664   252 SGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNWYLFNDSRVTFSSFESVQNvtsrfpkDTPYILFY 326
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
23-244 7.68e-18

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 89.16  E-value: 7.68e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782   23 RQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQAANIVRALELFVKADVLSGENAYMCAKcKKKVPAS 102
Cdd:COG5077    292 RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAK 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  103 KRFTIHRTSNVLTLSLKRF-ANFSGG---KITKDVGYPEFLNIRPYMSQN-----NGDPVmYGLYAVLVHSGySCHAGHY 173
Cdd:COG5077    371 KGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEIDLLPFLDRDadkseNSDAV-YVLYGVLVHSG-DLHEGHY 448
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  174 YCYVKAS-NGQWYQMNDSLVHSSNVKVVLNQ----------------------QAYVLFYLRipgsKKSPEGLISrtgss 230
Cdd:COG5077    449 YALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdhsgikrfmSAYMLVYLR----KSMLDDLLN----- 519
                          250
                   ....*....|....
gi 1867163782  231 slPGRPSVIPDHSK 244
Cdd:COG5077    520 --PVAAVDIPPHVE 531
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
75-212 8.14e-17

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 85.32  E-value: 8.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  75 LELFVKADVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFA--NFSGGKITKDVGYPEF-LNIRPYMSQNNGD 151
Cdd:COG5560   681 LNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSsvRSFRDKIDDLVEYPIDdLDLSGVEYMVDDP 760
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1867163782 152 PVMYGLYAVLVHSGYScHAGHYYCYVK-ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYLR 212
Cdd:COG5560   761 RLIYDLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
30-210 7.37e-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: 7.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  30 LVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEIRQA-------------------ANIVRALELFVKADVLSGENAY 90
Cdd:cd02671   122 LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESelskseesseispdpktemKTLKWAISQFASVERIVGEDKY 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  91 MCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFS------GG--KITKDVGYPEFLNIRPYMSQNNGDpvMYGLYAVLV 162
Cdd:cd02671   202 FCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGsefdcyGGlsKVNTPLLTPLKLSLEEWSTKPKND--VYRLFAVVM 279
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1867163782 163 HSGYSCHAGHYYCYVKasngqWYQMNDSLVHSSNVKVVLN---------QQAYVLFY 210
Cdd:cd02671   280 HSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKDFLEalspntsstSTPYLLFY 331
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
25-192 1.49e-12

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 69.61  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  25 TQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEI-RQAANIVRALELFVKADVL----SGENAY--MCAKCKK 97
Cdd:pfam13423 122 SPAESPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDLIYpRKPSSNNKKPPNQTFSSILksslERETTTkaWCEKCKR 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  98 KVPASKRFTIHRTSNVLTLSLKRFaNFSGGKITKDVGY-PEFLNIRPYM-SQNNGDPVMYGLYAVLVHSGYSCHAGHYYC 175
Cdd:pfam13423 202 YQPLESRRTVRNLPPVLSLNAALT-NEEWRQLWKTPGWlPPEIGLTLSDdLQGDNEIVKYELRGVVVHIGDSGTSGHLVS 280
                         170       180
                  ....*....|....*....|....*
gi 1867163782 176 YVKASN--------GQWYQMNDSLV 192
Cdd:pfam13423 281 FVKVADseledpteSQWYLFNDFLV 305
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
106-213 1.67e-12

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 69.06  E-value: 1.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782 106 TIHRTSNVLTLSLKRFANFSGG-KITKDVGYPEFLNIRPYMSQNNGDPVMYGLYAVLVHSGySCHAGHYYCYVKaSNGQW 184
Cdd:COG5533   175 SFVKLPKILTIQLKRFANLGGNqKIDTEVDEKFELPVKHDQILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKW 252
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1867163782 185 YQMNDSLVHSSNVKVVLN---QQAYVLFYLRI 213
Cdd:COG5533   253 EKANDSDVTPVSEEEAINekaKNAYLYFYERI 284
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
34-210 2.33e-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: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  34 IFGGYLRSRVKCSVCKSVSDTYDP--YLDVALEIRQAANIVRALELFVKADV-------LSGE-NAYMCAKCKKKVPASK 103
Cdd:cd02658   129 LFKFMIEDRLECLSCKKVKYTSELseILSLPVPKDEATEKEEGELVYEPVPLedclkayFAPEtIEDFCSTCKEKTTATK 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782 104 RFTIHRTSNVLTLSLKRFANFSGG---KITKDVGYPEFLnirpymsqnngDPVMYGLYAVLVHSGYSCHAGHYYCYVK-- 178
Cdd:cd02658   209 TTGFKTFPDYLVINMKRFQLLENWvpkKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKke 277
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1867163782 179 -ASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFY 210
Cdd:cd02658   278 iDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
20-210 8.97e-11

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 63.15  E-value: 8.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  20 WLDR---QTQATTLVHQI-----------FGGYLRSRVKCSVCKSVS-DTYDPYLDVALEIRQA-----ANIVRALELFV 79
Cdd:cd02662    27 YLEEfleQQDAHELFQVLletleqllkfpFDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQssgsgTTLEHCLDDFL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  80 KADVLSGenaYMCAKCKKKVPASKRftihrtsnVLTLSLKRFAnFSG-GKITKD---VGYPEFLNirpymsqnngdPVMY 155
Cdd:cd02662   107 STEIIDD---YKCDRCQTVIVRLPQ--------ILCIHLSRSV-FDGrGTSTKNsckVSFPERLP-----------KVLY 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1867163782 156 GLYAVLVHSGySCHAGHYYCYVKAS---------------------NGQWYQMNDSLV-HSSNVKVVLNQQAYVLFY 210
Cdd:cd02662   164 RLRAVVVHYG-SHSSGHYVCYRRKPlfskdkepgsfvrmregpsstSHPWWRISDTTVkEVSESEVLEQKSAYMLFY 239
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
102-192 3.58e-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: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782 102 SKRFTIHRTSNVLTLSLKRF-----ANfSGGKITKDVGYPEFLNIRPYMSqNNGdpvMYGLYAVLVHSGYSCHAGHYYCY 176
Cdd:cd02657   188 TKTSRISRLPKYLTVQFVRFfwkrdIQ-KKAKILRKVKFPFELDLYELCT-PSG---YYELVAVITHQGRSADSGHYVAW 262
                          90
                  ....*....|....*..
gi 1867163782 177 VKASN-GQWYQMNDSLV 192
Cdd:cd02657   263 VRRKNdGKWIKFDDDKV 279
PHA03247 PHA03247
large tegument protein UL36; Provisional
296-630 2.39e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 2.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  296 PPKLPSGSPSPKLSQTPTHMPTILDDPGKKVKKPAPPQHFSPRTAQGL-------------------------------- 343
Cdd:PHA03247  2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLgraaqassppqrprrraarptvgsltsladpp 2702
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  344 -----PGTSNSNSSRSGSQRQGSWDSRDVVLSTSPKLLATATANGHGLKGNDESAGLDRRGSSSSSPEHSASSDSTKAPQ 418
Cdd:PHA03247  2703 pppptPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  419 TPRSGAAHLCDSQETNCStaghsktPPSGADSKTVKLKSPVLSNTTTEPASTMSPPPAKKLALSAKKASTL--------W 490
Cdd:PHA03247  2783 LTRPAVASLSESRESLPS-------PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPppslplggS 2855
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  491 RATGNDLRPPPPSPSSdLTHPMKTSHPvvastwPVHRARAVSPAPQSSSRLQPPFSPHPtllssTPKPPGTSEPRscssi 570
Cdd:PHA03247  2856 VAPGGDVRRRPPSRSP-AAKPAAPARP------PVRRLARPAVSRSTESFALPPDQPER-----PPQPQAPPPPQ----- 2918
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1867163782  571 stalPQVNEDLVSLPHQLPEASEPPQSPSEKRKKTF-VGEPQRLGSETRLPQHIREATAAP 630
Cdd:PHA03247  2919 ----PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAgAGEPSGAVPQPWLGALVPGRVAVP 2975
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
84-210 1.49e-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: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782  84 LSGENAYMCAKCKK--KVPASKRF----TIHRTSNVLTLSLKRFANFS-------------GGKITKDVGYPEFLNI--- 141
Cdd:cd02673    76 YTIESSYVCIGCSFeeNVSDVGNFldvsMIDNKLDIDELLISNFKTWSpiekdcssckcesAISSERIMTFPECLSInlk 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782 142 ---------------RPYMSQNNGDPVMYGLYAVLVHSGYSCHAGHYYCYVKAS--NGQWYQMNDSLVH---SSNVKVVL 201
Cdd:cd02673   156 ryklriatsdylkknEEIMKKYCGTDAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEIRpvsKNDVSTNA 235

                  ....*....
gi 1867163782 202 NQQAYVLFY 210
Cdd:cd02673   236 RSSGYLIFY 244
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
113-211 1.91e-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: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782 113 VLTLSLKRFA--NFSGGKITKDVGYPEFLNIRPYMsqnngdpvmygLYAVLVHSGySCHAGHYYCYV-KASNGQWYQMND 189
Cdd:cd02665   131 VLTFELSRFEfnQGRPEKIHDKLEFPQIIQQVPYE-----------LHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYND 198
                          90       100       110
                  ....*....|....*....|....*....|
gi 1867163782 190 -SLVHSSNVKVV-------LNQQAYVLFYL 211
Cdd:cd02665   199 iSVTESSWEEVErdsfgggRNPSAYCLMYI 228
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
100-203 2.52e-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: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867163782 100 PASKRFTIHRTSNVLTLSLKRF--ANFSGGKITKDVGYP-EFLNIRPYMSQNNGD---PVMYGLYAVLVHSGYSCHAGHY 173
Cdd:cd02669   322 DSLKRYLISRLPKYLIFHIKRFskNNFFKEKNPTIVNFPiKNLDLSDYVHFDKPSlnlSTKYNLVANIVHEGTPQEDGTW 401
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1867163782 174 YCYV-KASNGQWYQMNDslvhsSNVKVVLNQ 203
Cdd:cd02669   402 RVQLrHKSTNKWFEIQD-----LNVKEVLPQ 427
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
29-65 5.35e-03

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 40.64  E-value: 5.35e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1867163782  29 TLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDVALEI 65
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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