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Conserved domains on  [gi|1820480215|ref|NP_001243823|]
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ubiquitin carboxyl-terminal hydrolase 17-like protein 15 [Homo sapiens]

Protein Classification

Peptidase_C19E and HABP4_PAI-RBP1 domain-containing protein( domain architecture ID 10119189)

Peptidase_C19E and HABP4_PAI-RBP1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 79-373 1.79e-156

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: 449.03  E-value: 1.79e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  79 GAGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMQAHITRALHNPGHVIQP------SQALAAG 152
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPrifssnLKQISKH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 153 FHRGKQEDAHEFLMFTVDAMKKACLPGHKQ---VDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQA 229
Cdd:cd02661    81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKlkaVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 230 AQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKIDKNVQYPECLDMKLYMSQ 309
Cdd:cd02661   161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820480215 310 TNSGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQEGQWYKMDDAEVTASSITSVLSQQAYVLFYI 373
Cdd:cd02661   241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
HABP4_PAI-RBP1 super family cl04741
Hyaluronan / mRNA binding family; This family includes the HABP4 family of hyaluronan-binding ...
 417-454 1.90e-05

Hyaluronan / mRNA binding family; This family includes the HABP4 family of hyaluronan-binding proteins, and the PAI-1 mRNA-binding protein, PAI-RBP1. HABP4 has been observed to bind hyaluronan (a glucosaminoglycan), but it is not known whether this is its primary role in vivo. It has also been observed to bind RNA, but with a lower affinity than that for hyaluronan. PAI-1 mRNA-binding protein specifically binds the mRNA of type-1 plasminogen activator inhibitor (PAI-1), and is thought to be involved in regulation of mRNA stability. However, in both cases, the sequence motifs predicted to be important for ligand binding are not conserved throughout the family, so it is not known whether members of this family share a common function.


The actual alignment was detected with superfamily member pfam04774:

Pssm-ID: 461421  Cd Length: 108  Bit Score: 43.90  E-value: 1.90e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1820480215 417 APELDEHLVERATQESTLDHWKFLQEQNKTKPEFNVRK 454
Cdd:pfam04774  68 AAAEEEEKEPNEDKEMTLDEYKKVQEEKRALPAFNIRK 105
 
Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 79-373 1.79e-156

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: 449.03  E-value: 1.79e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  79 GAGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMQAHITRALHNPGHVIQP------SQALAAG 152
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPrifssnLKQISKH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 153 FHRGKQEDAHEFLMFTVDAMKKACLPGHKQ---VDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQA 229
Cdd:cd02661    81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKlkaVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 230 AQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKIDKNVQYPECLDMKLYMSQ 309
Cdd:cd02661   161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820480215 310 TNSGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQEGQWYKMDDAEVTASSITSVLSQQAYVLFYI 373
Cdd:cd02661   241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
80-372 2.64e-78

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 248.90  E-value: 2.64e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  80 AGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGC--MLCTMQAHITRALHNPGH-VIQPSQALAA----- 151
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNSKSsSVSPKMFKKSlgkln 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 152 -GFHRGKQEDAHEFLMFTVDAMKKACLPghkqvDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAA 230
Cdd:pfam00443  81 pDFSGYKQQDAQEFLLFLLDGLHEDLNG-----NHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 231 QSV------QQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS-DV-TGNKIDKNVQYPECLD 302
Cdd:pfam00443 156 SAElktaslQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSyNRsTWEKLNTEVEFPLELD 235

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820480215 303 MKLYMSQTNSGPLV----YVLYAVLVHAGwSCHNGHYFSYVKAQE-GQWYKMDDAEVTASS-ITSVLSQQAYVLFY 372
Cdd:pfam00443 236 LSRYLAEELKPKTNnlqdYRLVAVVVHSG-SLSSGHYIAYIKAYEnNRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 81-376 1.21e-27

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 118.05  E-value: 1.21e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215   81 GLQNMGNTCYVNASLQCLTYTPPLAN--YMLSREHSQTchrhKGCMLCTMQahitRALHNPGHVIQPSQAL--------- 149
Cdd:COG5077    195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPRG----RDSVALALQ----RLFYNLQTGEEPVDTTeltrsfgwd 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  150 -AAGFHrgkQEDAHEFLMFTVDAMKKAclpghkqvdhhSKDTTL---IHQIFGGYWRSQIKCLHCHGISDTFDPYLDIAL 225
Cdd:COG5077    267 sDDSFM---QHDIQEFNRVLQDNLEKS-----------MRGTVVenaLNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  226 DIQAAQSVQQALEQLVKPEELNGENAYHC-GVCLQRapASKTLTLHTSAKVLILVLKRFS-DV-TGN--KIDKNVQYPEC 300
Cdd:COG5077    333 NVKGMKNLQESFRRYIQVETLDGDNRYNAeKHGLQD--AKKGVIFESLPPVLHLQLKRFEyDFeRDMmvKINDRYEFPLE 410

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  301 LDMKLYMS----QTNSGPLVYVLYAVLVHAGwSCHNGHYFSYVKAQ-EGQWYKMDDAEVTASSITSVLSQ---------- 365
Cdd:COG5077    411 IDLLPFLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykd 489

                          330       340
                   ....*....|....*....|...
gi 1820480215  366 ------------QAYVLFYIQKS 376
Cdd:COG5077    490 kirdhsgikrfmSAYMLVYLRKS 512
HABP4_PAI-RBP1 pfam04774
Hyaluronan / mRNA binding family; This family includes the HABP4 family of hyaluronan-binding ...
 417-454 1.90e-05

Hyaluronan / mRNA binding family; This family includes the HABP4 family of hyaluronan-binding proteins, and the PAI-1 mRNA-binding protein, PAI-RBP1. HABP4 has been observed to bind hyaluronan (a glucosaminoglycan), but it is not known whether this is its primary role in vivo. It has also been observed to bind RNA, but with a lower affinity than that for hyaluronan. PAI-1 mRNA-binding protein specifically binds the mRNA of type-1 plasminogen activator inhibitor (PAI-1), and is thought to be involved in regulation of mRNA stability. However, in both cases, the sequence motifs predicted to be important for ligand binding are not conserved throughout the family, so it is not known whether members of this family share a common function.


Pssm-ID: 461421  Cd Length: 108  Bit Score: 43.90  E-value: 1.90e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1820480215 417 APELDEHLVERATQESTLDHWKFLQEQNKTKPEFNVRK 454
Cdd:pfam04774  68 AAAEEEEKEPNEDKEMTLDEYKKVQEEKRALPAFNIRK 105
 
Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 79-373 1.79e-156

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: 449.03  E-value: 1.79e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  79 GAGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMQAHITRALHNPGHVIQP------SQALAAG 152
Cdd:cd02661     1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPrifssnLKQISKH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 153 FHRGKQEDAHEFLMFTVDAMKKACLPGHKQ---VDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQA 229
Cdd:cd02661    81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKlkaVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 230 AQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKIDKNVQYPECLDMKLYMSQ 309
Cdd:cd02661   161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820480215 310 TNSGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQEGQWYKMDDAEVTASSITSVLSQQAYVLFYI 373
Cdd:cd02661   241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
80-372 2.64e-78

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 248.90  E-value: 2.64e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  80 AGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGC--MLCTMQAHITRALHNPGH-VIQPSQALAA----- 151
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNSKSsSVSPKMFKKSlgkln 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 152 -GFHRGKQEDAHEFLMFTVDAMKKACLPghkqvDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAA 230
Cdd:pfam00443  81 pDFSGYKQQDAQEFLLFLLDGLHEDLNG-----NHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 231 QSV------QQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS-DV-TGNKIDKNVQYPECLD 302
Cdd:pfam00443 156 SAElktaslQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSyNRsTWEKLNTEVEFPLELD 235

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820480215 303 MKLYMSQTNSGPLV----YVLYAVLVHAGwSCHNGHYFSYVKAQE-GQWYKMDDAEVTASS-ITSVLSQQAYVLFY 372
Cdd:pfam00443 236 LSRYLAEELKPKTNnlqdYRLVAVVVHSG-SLSSGHYIAYIKAYEnNRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 81-373 3.30e-70

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: 228.41  E-value: 3.30e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  81 GLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRH--KGCMLCTMqAHITRALHNPGHVIQ--PSQALAAGFHRG 156
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCspNSCLSCAM-DEIFQEFYYSGDRSPygPINLLYLSWKHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 157 K------QEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQ-- 228
Cdd:cd02660    81 RnlagysQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPnk 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 229 -------------AAQSVQQALEQLVKPEELnGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRF---SDVTGNKID 292
Cdd:cd02660   161 stpswalgesgvsGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFehsLNKTSRKID 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 293 KNVQYPECLDMKLYM---------SQTNSGPLVYVLYAVLVHAGwSCHNGHYFSYVKAQEGQWYKMDDAEVTASSITSVL 363
Cdd:cd02660   240 TYVQFPLELNMTPYTsssigdtqdSNSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVL 318

                         330
                  ....*....|
gi 1820480215 364 SQQAYVLFYI 373
Cdd:cd02660   319 KSQAYLLFYH 328
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 81-373 1.32e-67

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: 219.28  E-value: 1.32e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  81 GLQNMGNTCYVNASLQCLtytpplanymlsrehsqtchrhkgcmlctmqahitralhnpghviqpsqalaagFHRgkQED 160
Cdd:cd02257     1 GLNNLGNTCYLNSVLQAL------------------------------------------------------FSE--QQD 24

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 161 AHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQ----AAQSVQQA 236
Cdd:cd02257    25 AHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPvkglPQVSLEDC 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 237 LEQLVKPEELNGENAYHCGVClQRAPASKTLTLHTSAKVLILVLKRFS---DVTGNKIDKNVQYPECLDMKLYM------ 307
Cdd:cd02257   105 LEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYLsegekd 183

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820480215 308 SQTNSGPLVYVLYAVLVHAGWSCHNGHYFSYVK-AQEGQWYKMDDAEVTASSITSVL-----SQQAYVLFYI 373
Cdd:cd02257   184 SDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 81-373 5.22e-52

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: 177.09  E-value: 5.22e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  81 GLQNMGNTCYVNASLQCLtytpplanymlsrehsqtCHRhkgcmlctmqahitralhnpghviqpsqalaagfhrgkQED 160
Cdd:cd02674     1 GLRNLGNTCYMNSILQCL------------------SAD--------------------------------------QQD 24

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 161 AHEFLMFTVDAMkkaclpghkqvdhHSkdttLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDI------QAAQSVQ 234
Cdd:cd02674    25 AQEFLLFLLDGL-------------HS----IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdAPKVTLE 87

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 235 QALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS--DVTGNKIDKNVQYP-ECLDMKLY-MSQT 310
Cdd:cd02674    88 DCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSfsRGSTRKLTTPVTFPlNDLDLTPYvDTRS 167

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820480215 311 NSGPLVYVLYAVLVHAGwSCHNGHYFSYVK-AQEGQWYKMDDAEVTASSITSVLSQQAYVLFYI 373
Cdd:cd02674   168 FTGPFKYDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 81-376 6.69e-51

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 177.83  E-value: 6.69e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  81 GLQNMGNTCYVNASLQCLTYTPPLAN--YMLSREHSQTCHRHKGCML----CTMQAHITRAL-HNPGHVIQ--PSQALAA 151
Cdd:cd02659     4 GLKNQGATCYMNSLLQQLYMTPEFRNavYSIPPTEDDDDNKSVPLALqrlfLFLQLSESPVKtTELTDKTRsfGWDSLNT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 152 GfhrgKQEDAHEFLMFTVDAMKKaCLPGHKQVDhhskdttLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQ 231
Cdd:cd02659    84 F----EQHDVQEFFRVLFDKLEE-KLKGTGQEG-------LIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 232 SVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS-D-VTGNKIDKNVQY--PECLDMKLYM 307
Cdd:cd02659   152 NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfDfETMMRIKINDRFefPLELDMEPYT 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 308 SQTN-----------SGPLVYVLYAVLVHAGwSCHNGHYFSYVKAQE-GQWYKMDDAEVTASSITSVLSQQ--------- 366
Cdd:cd02659   232 EKGLakkegdsekkdSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDdGKWYKFNDDVVTPFDPNDAEEECfggeetqkt 310

                         330       340
                  ....*....|....*....|...
gi 1820480215 367 -------------AYVLFYIQKS 376
Cdd:cd02659   311 ydsgprafkrttnAYMLFYERKS 333
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 81-372 2.84e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 163.71  E-value: 2.84e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  81 GLQNMGNTCYVNASLQCLTYTPPLANYMLSREH---SQTCHRHkgcmlctmqahitralhnpghviqpSQalaagFHRGK 157
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKelfSQVCRKA-------------------------PQ-----FKGYQ 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 158 QEDAHEFLMFTVDAMKkaclpghkqvdhhskdtTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIAL----DIQAAQSV 233
Cdd:cd02667    51 QQDSHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSECSI 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 234 QQALEQLVKPEELNGENAYHCGVCLQrapASKTLTLHTSAKVLILVLKRF---SDVTGNKIDKNVQYPECLDMKLYMSQT 310
Cdd:cd02667   114 ESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqqpRSANLRKVSRHVSFPEILDLAPFCDPK 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 311 NSGP-----LVYVLYAVLVHAGwSCHNGHYFSYVKAQ----------------------EGQWYKMDDAEVTASSITSVL 363
Cdd:cd02667   191 CNSSedkssVLYRLYGVVEHSG-TMRSGHYVAYVKVRppqqrlsdltkskpaadeagpgSGQWYYISDSDVREVSLEEVL 269


                  ....*....
gi 1820480215 364 SQQAYVLFY 372
Cdd:cd02667   270 KSEAYLLFY 278
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 81-372 9.88e-43

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: 154.78  E-value: 9.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  81 GLQNMGNTCYVNASLQCL----TYTPpLANYMlsreHSQTCHRHKGcmlctmqahitralhnpgHVIQPS---QAL--AA 151
Cdd:cd02663     1 GLENFGNTCYCNSVLQALyfenLLTC-LKDLF----ESISEQKKRT------------------GVISPKkfiTRLkrEN 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 152 GFHRGK-QEDAHEFLMF-------TVDAMKKACLPGHKQVDHHSKD--TTLIHQIFGGYWRSQIKCLHCHGISDTFDPYL 221
Cdd:cd02663    58 ELFDNYmHQDAHEFLNFllneiaeILDAERKAEKANRKLNNNNNAEpqPTWVHEIFQGILTNETRCLTCETVSSRDETFL 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 222 DIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS---DVTGN-KIDKNVQY 297
Cdd:cd02663   138 DLSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKydeQLNRYiKLFYRVVF 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 298 PECLDMKLYMSQTNSGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQeGQWYKMDDAEVTA---SSITSVL-----SQQAYV 369
Cdd:cd02663   218 PLELRLFNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKSH-GGWLLFDDETVEKideNAVEEFFgdspnQATAYV 296


                  ...
gi 1820480215 370 LFY 372
Cdd:cd02663   297 LFY 299
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 81-372 5.31e-42

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: 153.42  E-value: 5.31e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  81 GLQNMGNTCYVNASLQCLTYTPPLANYMLSRehsqTCHRHKGC-----MLCTMQAHitrALHNPGHVIQP-----SQALA 150
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSL----NLPRLGDSqsvmkKLQLLQAH---LMHTQRRAEAPpdyflEASRP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 151 AGFHRGKQEDAHEFLMFTVDAMKkaclpghkqvdhhskdtTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALdiqAA 230
Cdd:cd02664    74 PWFTPGSQQDCSEYLRYLLDRLH-----------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL---SF 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 231 QSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDV--TGN--KIDKNVQYPECLDMKLY 306
Cdd:cd02664   134 PSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDqkTHVreKIMDNVSINEVLSLPVR 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 307 MSQTNSGP-------------------LVYVLYAVLVHAGWSCHNGHYFSYVKAQ---------------------EGQW 346
Cdd:cd02664   214 VESKSSESplekkeeesgddgelvtrqVHYRLYAVVVHSGYSSESGHYFTYARDQtdadstgqecpepkdaeendeSKNW 293

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1820480215 347 YKMDDAEVTASS------ITSVLSQQ-AYVLFY 372
Cdd:cd02664   294 YLFNDSRVTFSSfesvqnVTSRFPKDtPYILFY 326
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 81-354 1.04e-35

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 136.01  E-value: 1.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  81 GLQNMGNTCYVNASLQCLTYTPPLANYMLS--------REHSQTCHRHKGCMLCTMQAHITRALHNPG-HVIQPSQ-ALA 150
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYEcnstedaeLKNMPPDKPHEPQTIIDQLQLIFAQLQFGNrSVVDPSGfVKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 151 AGFHRGKQEDAHEFLMFTVDAMKkACLPGHKqvdhHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAA 230
Cdd:cd02668    81 LGLDTGQQQDAQEFSKLFLSLLE-AKLSKSK----NPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 231 QSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS--DVTGN--KIDKNVQYPECLDMKLY 306
Cdd:cd02668   156 KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVfdRKTGAkkKLNASISFPEILDMGEY 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1820480215 307 MSQTNSGPLVYVLYAVLVHAGWSCHNGHYFSYVK-AQEGQWYKMDDAEV 354
Cdd:cd02668   236 LAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDV 284
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 81-376 1.21e-27

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 118.05  E-value: 1.21e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215   81 GLQNMGNTCYVNASLQCLTYTPPLAN--YMLSREHSQTchrhKGCMLCTMQahitRALHNPGHVIQPSQAL--------- 149
Cdd:COG5077    195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPRG----RDSVALALQ----RLFYNLQTGEEPVDTTeltrsfgwd 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  150 -AAGFHrgkQEDAHEFLMFTVDAMKKAclpghkqvdhhSKDTTL---IHQIFGGYWRSQIKCLHCHGISDTFDPYLDIAL 225
Cdd:COG5077    267 sDDSFM---QHDIQEFNRVLQDNLEKS-----------MRGTVVenaLNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  226 DIQAAQSVQQALEQLVKPEELNGENAYHC-GVCLQRapASKTLTLHTSAKVLILVLKRFS-DV-TGN--KIDKNVQYPEC 300
Cdd:COG5077    333 NVKGMKNLQESFRRYIQVETLDGDNRYNAeKHGLQD--AKKGVIFESLPPVLHLQLKRFEyDFeRDMmvKINDRYEFPLE 410

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  301 LDMKLYMS----QTNSGPLVYVLYAVLVHAGwSCHNGHYFSYVKAQ-EGQWYKMDDAEVTASSITSVLSQ---------- 365
Cdd:COG5077    411 IDLLPFLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykd 489

                          330       340
                   ....*....|....*....|...
gi 1820480215  366 ------------QAYVLFYIQKS 376
Cdd:COG5077    490 kirdhsgikrfmSAYMLVYLRKS 512
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 80-372 9.01e-27

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: 111.14  E-value: 9.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  80 AGLQNMGNTCYVNASLQCLTYTP-------PLANYMLSREHSQTChrhkgCMLCTMQAHITRALHNPGHVIQPSQALAAG 152
Cdd:cd02671    25 VGLNNLGNTCYLNSVLQVLYFCPgfkhglkHLVSLISSVEQLQSS-----FLLNPEKYNDELANQAPRRLLNALREVNPM 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 153 FHRGKQEDAHEFLMftvdamkkaCLPGHKQvdhhskdtTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQ- 231
Cdd:cd02671   100 YEGYLQHDAQEVLQ---------CILGNIQ--------ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESEl 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 232 ------------------SVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFS------DVT 287
Cdd:cd02671   163 skseesseispdpktemkTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAangsefDCY 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 288 GNKIDKNVQYPECLDMKLYMSQTNSGPLVYVLYAVLVHAGWSCHNGHYFSYVKaqegqWYKMDDAEV---------TASS 358
Cdd:cd02671   243 GGLSKVNTPLLTPLKLSLEEWSTKPKNDVYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVkvteekdflEALS 317

                         330
                  ....*....|....
gi 1820480215 359 ITSVLSQQAYVLFY 372
Cdd:cd02671   318 PNTSSTSTPYLLFY 331
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
81-375 7.64e-25

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 104.50  E-value: 7.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  81 GLQNMGNTCYVNASLQCLT-YTPPLANYM---------LSREHSQtchRHKGCMLCTMQAHITRAlhnpghVIQPSQALA 150
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlYLPKLDELLddlskelkvLKNVIRK---PEPDLNQEEALKLFTAL------WSSKEHKVG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 151 AGFHRGKQEDAHEFLMFTVDAMKkacLPGHKQVdhhskdTTLIHQIFGGYWRsqikclhcHGISDTFDpyLDIALDIQAA 230
Cdd:COG5533    72 WIPPMGSQEDAHELLGKLLDELK---LDLVNSF------TIRIFKTTKDKKK--------TSTGDWFD--IIIELPDQTW 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 231 QSVQQALEQLvkPEELNGENAYHCGVCLQ-------RAPASKTLTLHTSAKVLILVLKRFS-DVTGNKIDKNVQYPecLD 302
Cdd:COG5533   133 VNNLKTLQEF--IDNMEELVDDETGVKAKeneelevQAKQEYEVSFVKLPKILTIQLKRFAnLGGNQKIDTEVDEK--FE 208

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820480215 303 MKLYMSQT--NSGPLVYVLYAVLVHAGwSCHNGHYFSYVKaQEGQWYKMDDAEVTASSITSVL---SQQAYVLFYIQK 375
Cdd:COG5533   209 LPVKHDQIlnIVKETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPVSEEEAInekAKNAYLYFYERI 284
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 81-372 7.27e-23

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 99.32  E-value: 7.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  81 GLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCH--RHKGCMLCTMqAHITRAL--------------HNPGHV-I 143
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDvvDPANDLNCQL-IKLADGLlsgryskpaslkseNDPYQVgI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 144 QPSQ--ALAAGFHR----GKQEDAHEFLMFTVDAMKKAClpghkqvdhHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTF 217
Cdd:cd02658    80 KPSMfkALIGKGHPefstMRQQDALEFLLHLIDKLDRES---------FKNLGLNPNDLFKFMIEDRLECLSCKKVKYTS 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 218 DPYLDIALDIQAA--------------QSVQQALEQLVKPEELngenAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRF 283
Cdd:cd02658   151 ELSEILSLPVPKDeatekeegelvyepVPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFKTFPDYLVINMKRF 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 284 ---SDVTGNKIDKNVQYPECLdmklymsqtnsGPLVYVLYAVLVHAGWSCHNGHYFSYVK---AQEGQWYKMDDAEVTAS 357
Cdd:cd02658   227 qllENWVPKKLDVPIDVPEEL-----------GPGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVVAS 295

                         330
                  ....*....|....*
gi 1820480215 358 SITSVLSQQAYVLFY 372
Cdd:cd02658   296 QDPPEMKKLGYIYFY 310
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 81-372 2.99e-22

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 97.40  E-value: 2.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  81 GLQNMGNTCYVNASLQCLTYTPP----LANYMLSREHS-QTCHRhkgcmlctmqahITRALHN-------------PGHV 142
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPElrdaLKNYNPARRGAnQSSDN------------LTNALRDlfdtmdkkqepvpPIEF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 143 IQ------PSQALAAGFHRGKQEDAHEFLMFTVDAMkKACLPGhkqvdhHSKDTTLIHQIFGGYWRSQIKC--------- 207
Cdd:cd02657    69 LQllrmafPQFAEKQNQGGYAQQDAEECWSQLLSVL-SQKLPG------AGSKGSFIDQLFGIELETKMKCtespdeeev 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 208 -------LHCHgISDTFD-PYLDIALDiqaaqsvQQALEQLVKPEELNGENAYHcgvclqrapaSKTLTLHTSAKVLILV 279
Cdd:cd02657   142 steseykLQCH-ISITTEvNYLQDGLK-------KGLEEEIEKHSPTLGRDAIY----------TKTSRISRLPKYLTVQ 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 280 LKRF----SDVTGNKIDKNVQYPECLDmkLYMSQTNSGplVYVLYAVLVHAGWSCHNGHYFSYVK-AQEGQWYKMDDAEV 354
Cdd:cd02657   204 FVRFfwkrDIQKKAKILRKVKFPFELD--LYELCTPSG--YYELVAVITHQGRSADSGHYVAWVRrKNDGKWIKFDDDKV 279

                         330       340
                  ....*....|....*....|....*
gi 1820480215 355 TASSITSVL-------SQQAYVLFY 372
Cdd:cd02657   280 SEVTEEDILklsgggdWHIAYILLY 304
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
232-376 4.24e-22

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 100.73  E-value: 4.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 232 SVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTG--NKIDKNVQYP-ECLDMKLYMS 308
Cdd:COG5560   676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSfrDKIDDLVEYPiDDLDLSGVEY 755

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820480215 309 QTNSGPLVYVLYAVLVHAGWScHNGHYFSYVK-AQEGQWYKMDDAEVTASSITSVLSQQAYVLFYIQKS 376
Cdd:COG5560   756 MVDDPRLIYDLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
70-227 1.20e-17

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 86.48  E-value: 1.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  70 LSSRRPAAVGaGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHR--HKGCM--LCTMQAHITRALHNPG-HVIQ 144
Cdd:COG5560   257 RSINKEAGTC-GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEenPLGMHgsVASAYADLIKQLYDGNlHAFT 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 145 PSQ------ALAAGFHRGKQEDAHEFLMFTVDAM--------------KKACLPGHKQV----------DHHSKDTTLIH 194
Cdd:COG5560   336 PSGfkktigSFNEEFSGYDQQDSQEFIAFLLDGLhedlnriikkpytsKPDLSPGDDVVvkkkakecwwEHLKRNDSIIT 415

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1820480215 195 QIFGGYWRSQIKCLHCHGISDTFDPYLDIALDI 227
Cdd:COG5560   416 DLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 81-355 6.85e-15

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 76.97  E-value: 6.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  81 GLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMqAHITRALHNP----GHV-----IQPSQALAA 151
Cdd:cd02669   121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSELVKRL-SELIRKIWNPrnfkGHVsphelLQAVSKVSK 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 152 G-FHRGKQEDAHEFLMFTVDAMkkaclpgHKQVDHHSKD-TTLIHQIFGG--------------YWRSQIKCLHCHGISD 215
Cdd:cd02669   200 KkFSITEQSDPVEFLSWLLNTL-------HKDLGGSKKPnSSIIHDCFQGkvqietqkikphaeEEGSKDKFFKDSRVKK 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 216 TFD-PYLDIALDI---------QAAQSVQQ-ALEQLVKpeELNGENAYHCGvclqraPASKTLTLHTSAKVLILVLKRFS 284
Cdd:cd02669   273 TSVsPFLLLTLDLpppplfkdgNEENIIPQvPLKQLLK--KYDGKTETELK------DSLKRYLISRLPKYLIFHIKRFS 344

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820480215 285 DVTGNKiDKN---VQYP-ECLDMKLYMSQTNSGPLVYVLY---AVLVHAGWSCHNGHYFSYV-KAQEGQWYKMDDAEVT 355
Cdd:cd02669   345 KNNFFK-EKNptiVNFPiKNLDLSDYVHFDKPSLNLSTKYnlvANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQDLNVK 422
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 81-372 8.11e-15

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


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 74.32  E-value: 8.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  81 GLQNMGNTCYVNASLQCLTYTPPLANYmlsrehsqtchrhkgcmlctmqahITRALhnpghviqpsqalaagfhrgKQED 160
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLIEY------------------------LEEFL--------------------EQQD 36

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 161 AHEFLmftvdamkkaclpghkqvdHHSkdTTLIHQIFGGYWR----SQIKCLHCHGIS-DTFDPYLDIALDIQAAQSVQ- 234
Cdd:cd02662    37 AHELF-------------------QVL--LETLEQLLKFPFDgllaSRIVCLQCGESSkVRYESFTMLSLPVPNQSSGSg 95

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 235 QALEQLV----KPEELNGENAYHCGVCLQRAPasKTLTLHTSAkvliLVLKRFSDVTGNKIdkNVQYPECLDMKLYMsqt 310
Cdd:cd02662    96 TTLEHCLddflSTEIIDDYKCDRCQTVIVRLP--QILCIHLSR----SVFDGRGTSTKNSC--KVSFPERLPKVLYR--- 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 311 nsgplvyvLYAVLVHAGwSCHNGHYFSYVKAQE---------------------GQWYKMDDAEVTASSITSVLSQ-QAY 368
Cdd:cd02662   165 --------LRAVVVHYG-SHSSGHYVCYRRKPLfskdkepgsfvrmregpsstsHPWWRISDTTVKEVSESEVLEQkSAY 235


                  ....
gi 1820480215 369 VLFY 372
Cdd:cd02662   236 MLFY 239
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
80-351 8.20e-15

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 75.38  E-value: 8.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  80 AGLQNMGNTCYVNASLQCLTYTPPLANYMLSreHSQTCHRHKGCMLCTM---------------QA-------------- 130
Cdd:pfam13423   1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATECLKEHCLLCELgflfdmlekakgkncQAsnflralssipeas 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 131 --------HITRALHNPGHVIQpsqalaaGFHRgkqedaheFLMftvdamKKACLPGHKQVDHHSKDTTLIHQIFGGYWR 202
Cdd:pfam13423  79 alglldedRETNSAISLSSLIQ-------SFNR--------FLL------DQLSSEENSTPPNPSPAESPLEQLFGIDAE 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 203 SQIKCLHCHGISDTFDPYLDIALDI----------QAAQSVQQALEQLVKPEELNgeNAyHCGVCLQRAPASKTLTLHTS 272
Cdd:pfam13423 138 TTIRCSNCGHESVRESSTHVLDLIYprkpssnnkkPPNQTFSSILKSSLERETTT--KA-WCEKCKRYQPLESRRTVRNL 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 273 AKVLILVLKRFSDVTGNKIDKNVQYPECLDMKLYM-SQTNSGPLVYVLYAVLVHAGWSCHNGHYFSYVK--------AQE 343
Cdd:pfam13423 215 PPVLSLNAALTNEEWRQLWKTPGWLPPEIGLTLSDdLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseledPTE 294


                  ....*...
gi 1820480215 344 GQWYKMDD 351
Cdd:pfam13423 295 SQWYLFND 302
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 82-372 1.47e-09

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


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 58.69  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  82 LQNMGNTCYVNASLQcltytpplanymlsrehsqtchrhkgcmlctmqahitrALHNPGHVIQpsqalaaGFHRGKQEDA 161
Cdd:cd02673     2 LVNTGNSCYFNSTMQ--------------------------------------ALSSIGKINT-------EFDNDDQQDA 36

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 162 HEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQI--FGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVQQalEQ 239
Cdd:cd02673    37 HEFLLTLLEAIDDIMQVNRTNVPPSNIEIKRLNPLeaFKYTIESSYVCIGCSFEENVSDVGNFLDVSMIDNKLDID--EL 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 240 LVKPEELNGENAYHCGVC-LQRAPASKTLTlhTSAKVLILVLKRF--SDVTGNKIDKNvqypeCLDMKLYMSQTNSgplv 316
Cdd:cd02673   115 LISNFKTWSPIEKDCSSCkCESAISSERIM--TFPECLSINLKRYklRIATSDYLKKN-----EEIMKKYCGTDAK---- 183

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820480215 317 YVLYAVLVHAGWSCHNGHYFSYVK--AQEGQWYKMDDAEVTASSITSVL---SQQAYVLFY 372
Cdd:cd02673   184 YSLVAVICHLGESPYDGHYIAYTKelYNGSSWLYCSDDEIRPVSKNDVStnaRSSGYLIFY 244
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 80-355 1.49e-06

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 50.57  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215  80 AGLQNMGNTCYVNASLQCLTYTPPLANYMLS-----REHSQTCHRHK--GCMLCTMQ--------AHITRAL-----HNP 139
Cdd:cd02666     2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNfdeskAELASDYPTERriGGREVSRSelqrsnqfVYELRSLfndliHSN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 140 GHVIQPSQALA-AGFhrgKQEDAHEFL---MFTVDAMKKAclPGHKQVDHHSKD----TTLIHQIF-GGYWRSQIKCLHC 210
Cdd:cd02666    82 TRSVTPSKELAyLAL---RQQDVTECIdnvLFQLEVALEP--ISNAFAGPDTEDdkeqSDLIKRLFsGKTKQQLVPESMG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 211 HGISDTFDPYLDIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKrfSDVTGNK 290
Cdd:cd02666   157 NQPSVRTKTERFLSLLVDVGKKGREIVVLLEPKDLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRELIS--MDRYELP 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 291 IDKNV-----------QYPECLDMKLYMSQTNS---------GPLVYVLYAVLVHAGWSCHnGHYFSYVK-AQEGQWYKM 349
Cdd:cd02666   235 SSIDDidelireaiqsESSLVRQAQNELAELKHeiekqfddlKSYGYRLHAVFIHRGEASS-GHYWVYIKdFEENVWRKY 313


                  ....*.
gi 1820480215 350 DDAEVT 355
Cdd:cd02666   314 NDETVT 319
HABP4_PAI-RBP1 pfam04774
Hyaluronan / mRNA binding family; This family includes the HABP4 family of hyaluronan-binding ...
 417-454 1.90e-05

Hyaluronan / mRNA binding family; This family includes the HABP4 family of hyaluronan-binding proteins, and the PAI-1 mRNA-binding protein, PAI-RBP1. HABP4 has been observed to bind hyaluronan (a glucosaminoglycan), but it is not known whether this is its primary role in vivo. It has also been observed to bind RNA, but with a lower affinity than that for hyaluronan. PAI-1 mRNA-binding protein specifically binds the mRNA of type-1 plasminogen activator inhibitor (PAI-1), and is thought to be involved in regulation of mRNA stability. However, in both cases, the sequence motifs predicted to be important for ligand binding are not conserved throughout the family, so it is not known whether members of this family share a common function.


Pssm-ID: 461421  Cd Length: 108  Bit Score: 43.90  E-value: 1.90e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1820480215 417 APELDEHLVERATQESTLDHWKFLQEQNKTKPEFNVRK 454
Cdd:pfam04774  68 AAAEEEEKEPNEDKEMTLDEYKKVQEEKRALPAFNIRK 105
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 214-372 4.12e-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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 42.13  E-value: 4.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 214 SDTFDPYLDIALDIQAAQ--------SVQQALEQLVKPEELNGENAYhCGVCLQRAPASKTLTLHTSakVLILVLKRFSD 285
Cdd:cd02670    35 DKLLMPLLEPKVDIIHGGkkdqdddkLVNERLLQIPVPDDDDGGGIT-LEQCLEQYFNNSVFAKAPS--CLIICLKRYGK 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 286 VTGN--KIDKNVQYPECLDMKLYMSQTN----------------------SGPLVYVLYAVLVHAGWSCHNGHYFSYVK- 340
Cdd:cd02670   112 TEGKaqKMFKKILIPDEIDIPDFVADDPracskcqlecrvcyddkdfsptCGKFKLSLCSAVCHRGTSLETGHYVAFVRy 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1820480215 341 -----------AQEGQWYKMDD-----AEVTASSITSVLSQQ-AYVLFY 372
Cdd:cd02670   192 gsysltetdneAYNAQWVFFDDmadrdGVSNGFNIPAARLLEdPYMLFY 240
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 275-373 9.08e-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: 41.00  E-value: 9.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480215 275 VLILVLKRFS--DVTGNKIDKNVQYPECLdmklymSQTNsgplvYVLYAVLVHAGwSCHNGHYFSYVKAQEGQ-WYKMDD 351
Cdd:cd02665   131 VLTFELSRFEfnQGRPEKIHDKLEFPQII------QQVP-----YELHAVLVHEG-QANAGHYWAYIYKQSRQeWEKYND 198

                          90       100       110
                  ....*....|....*....|....*....|
gi 1820480215 352 AEVTASSITSVLSQ--------QAYVLFYI 373
Cdd:cd02665   199 ISVTESSWEEVERDsfgggrnpSAYCLMYI 228
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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