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Conserved domains on  [gi|379030631|ref|NP_001243800|]
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ubiquitin carboxyl-terminal hydrolase 17-like protein 3 [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 1.77e-146

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: 422.45  E-value: 1.77e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  79 GAGLQNMGNTCYENASLQCLTYTLPLANYMLSREHSQTCQRPKCCMLCTMQAHITWALHSPGHVIQP------SQALASG 152
Cdd:cd02661    1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPrifssnLKQISKH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 153 FHRGKQEDVHEFLMFTVDAMKKACLPGHKQ---VDHHSKDTTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQA 229
Cdd:cd02661   81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKlkaVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 230 AQSVKQALEQLVKPEELNGENAYHCGLCLQRAPASNTLTLHTSAKVLILVLKRFSDVAGNKLAKNVQYPECLDMQPYMSQ 309
Cdd:cd02661  161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 379030631 310 QNTGPLVYVLYAVLVHAGWSCHDGHYFSYVKAQEGQWYKMDDAEVTVCSITSVLSQQAYVLFYI 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 9.25e-04

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: 38.89  E-value: 9.25e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 379030631  417 APELDEHLVERATQESTLDHWKFLQEQNKTKPEFNVGK 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 1.77e-146

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: 422.45  E-value: 1.77e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  79 GAGLQNMGNTCYENASLQCLTYTLPLANYMLSREHSQTCQRPKCCMLCTMQAHITWALHSPGHVIQP------SQALASG 152
Cdd:cd02661    1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPrifssnLKQISKH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 153 FHRGKQEDVHEFLMFTVDAMKKACLPGHKQ---VDHHSKDTTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQA 229
Cdd:cd02661   81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKlkaVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 230 AQSVKQALEQLVKPEELNGENAYHCGLCLQRAPASNTLTLHTSAKVLILVLKRFSDVAGNKLAKNVQYPECLDMQPYMSQ 309
Cdd:cd02661  161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 379030631 310 QNTGPLVYVLYAVLVHAGWSCHDGHYFSYVKAQEGQWYKMDDAEVTVCSITSVLSQQAYVLFYI 373
Cdd:cd02661  241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
80-372 9.87e-73

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 233.87  E-value: 9.87e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631   80 AGLQNMGNTCYENASLQCLTYTLPLANYMLSREHSQTCQRPKCC--MLCTMQAHIT-WALHSPGHVIQPSQALAS----- 151
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKaLQKNSKSSSVSPKMFKKSlgkln 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  152 -GFHRGKQEDVHEFLMFTVDAMKKACLPghkqvDHHSKDTTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQAA 230
Cdd:pfam00443  81 pDFSGYKQQDAQEFLLFLLDGLHEDLNG-----NHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  231 QSVK------QALEQLVKPEELNGENAYHCGLCLQRAPASNTLTLHTSAKVLILVLKRFS-DVAG-NKLAKNVQYPECLD 302
Cdd:pfam00443 156 SAELktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSyNRSTwEKLNTEVEFPLELD 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 379030631  303 MQPYMSQQNTGPLV----YVLYAVLVHAGwSCHDGHYFSYVKAQE-GQWYKMDDAEVTVCS-ITSVLSQQAYVLFY 372
Cdd:pfam00443 236 LSRYLAEELKPKTNnlqdYRLVAVVVHSG-SLSSGHYIAYIKAYEnNRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
81-410 4.58e-24

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 106.88  E-value: 4.58e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631   81 GLQNMGNTCYENASLQCLTYTLPLAN--YMLSREHsqtcQRPKCCMLCTMQaHITWALHSPGHVIQPSQALAS------- 151
Cdd:COG5077   195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDH----PRGRDSVALALQ-RLFYNLQTGEEPVDTTELTRSfgwdsdd 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  152 GFHrgkQEDVHEFLMFTVDAMKKAclpghkqvdhhSKDTTL---IHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQ 228
Cdd:COG5077   270 SFM---QHDIQEFNRVLQDNLEKS-----------MRGTVVenaLNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVK 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  229 AAQSVKQALEQLVKPEELNGENAYHC-GLCLQRapASNTLTLHTSAKVLILVLKRFS-DV---AGNKLAKNVQYPECLDM 303
Cdd:COG5077   336 GMKNLQESFRRYIQVETLDGDNRYNAeKHGLQD--AKKGVIFESLPPVLHLQLKRFEyDFerdMMVKINDRYEFPLEIDL 413
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  304 QPYMS----QQNTGPLVYVLYAVLVHAGwSCHDGHYFSYVKAQ-EGQWYKMDDAEVTVCSITSVLSQ------------- 365
Cdd:COG5077   414 LPFLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkir 492
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 379030631  366 ---------QAYVLFYIQKSEWERHSESVSRGREPRALgAEDTDRRAKQGELKR 410
Cdd:COG5077   493 dhsgikrfmSAYMLVYLRKSMLDDLLNPVAAVDIPPHV-EEVLSEEIDKTEVRC 545
HABP4_PAI-RBP1 pfam04774
Hyaluronan / mRNA binding family; This family includes the HABP4 family of hyaluronan-binding ...
417-454 9.25e-04

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: 38.89  E-value: 9.25e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 379030631  417 APELDEHLVERATQESTLDHWKFLQEQNKTKPEFNVGK 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 1.77e-146

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: 422.45  E-value: 1.77e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  79 GAGLQNMGNTCYENASLQCLTYTLPLANYMLSREHSQTCQRPKCCMLCTMQAHITWALHSPGHVIQP------SQALASG 152
Cdd:cd02661    1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPrifssnLKQISKH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 153 FHRGKQEDVHEFLMFTVDAMKKACLPGHKQ---VDHHSKDTTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQA 229
Cdd:cd02661   81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKlkaVDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 230 AQSVKQALEQLVKPEELNGENAYHCGLCLQRAPASNTLTLHTSAKVLILVLKRFSDVAGNKLAKNVQYPECLDMQPYMSQ 309
Cdd:cd02661  161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 379030631 310 QNTGPLVYVLYAVLVHAGWSCHDGHYFSYVKAQEGQWYKMDDAEVTVCSITSVLSQQAYVLFYI 373
Cdd:cd02661  241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
80-372 9.87e-73

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 233.87  E-value: 9.87e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631   80 AGLQNMGNTCYENASLQCLTYTLPLANYMLSREHSQTCQRPKCC--MLCTMQAHIT-WALHSPGHVIQPSQALAS----- 151
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKaLQKNSKSSSVSPKMFKKSlgkln 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  152 -GFHRGKQEDVHEFLMFTVDAMKKACLPghkqvDHHSKDTTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQAA 230
Cdd:pfam00443  81 pDFSGYKQQDAQEFLLFLLDGLHEDLNG-----NHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  231 QSVK------QALEQLVKPEELNGENAYHCGLCLQRAPASNTLTLHTSAKVLILVLKRFS-DVAG-NKLAKNVQYPECLD 302
Cdd:pfam00443 156 SAELktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSyNRSTwEKLNTEVEFPLELD 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 379030631  303 MQPYMSQQNTGPLV----YVLYAVLVHAGwSCHDGHYFSYVKAQE-GQWYKMDDAEVTVCS-ITSVLSQQAYVLFY 372
Cdd:pfam00443 236 LSRYLAEELKPKTNnlqdYRLVAVVVHSG-SLSSGHYIAYIKAYEnNRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
81-373 6.97e-62

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: 203.48  E-value: 6.97e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  81 GLQNMGNTCYENASLQCLtytlplanymlsrehsqtcqrpkccmlctmqahitwalhspghviqpsqalasgFHRgkQED 160
Cdd:cd02257    1 GLNNLGNTCYLNSVLQAL------------------------------------------------------FSE--QQD 24
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 161 VHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQ----AAQSVKQA 236
Cdd:cd02257   25 AHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLPvkglPQVSLEDC 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 237 LEQLVKPEELNGENAYHCGLClQRAPASNTLTLHTSAKVLILVLKRFS---DVAGNKLAKNVQYPECLDMQPYMSQQ--- 310
Cdd:cd02257  105 LEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYLSEGekd 183
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 379030631 311 ---NTGPLVYVLYAVLVHAGWSCHDGHYFSYVK-AQEGQWYKMDDAEVTVCSITSVL-----SQQAYVLFYI 373
Cdd:cd02257  184 sdsDNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
81-373 2.59e-61

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: 204.53  E-value: 2.59e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  81 GLQNMGNTCYENASLQCLTYTLPLANYMLSREHSQTC--QRPKCCMLCTMqAHITWALHSPGHVIQ--PSQALASGFHRG 156
Cdd:cd02660    2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTClsCSPNSCLSCAM-DEIFQEFYYSGDRSPygPINLLYLSWKHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 157 K------QEDVHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQ-- 228
Cdd:cd02660   81 RnlagysQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPnk 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 229 -------------AAQSVKQALEQLVKPEELnGENAYHCGLCLQRAPASNTLTLHTSAKVLILVLKRFSDVAGN---KLA 292
Cdd:cd02660  161 stpswalgesgvsGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKID 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 293 KNVQYPECLDMQPYM---------SQQNTGPLVYVLYAVLVHAGwSCHDGHYFSYVKAQEGQWYKMDDAEVTVCSITSVL 363
Cdd:cd02660  240 TYVQFPLELNMTPYTsssigdtqdSNSLDPDYTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVL 318
                        330
                 ....*....|
gi 379030631 364 SQQAYVLFYI 373
Cdd:cd02660  319 KSQAYLLFYH 328
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
81-373 5.58e-48

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 165.92  E-value: 5.58e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  81 GLQNMGNTCYENASLQCLtytlplanymlsrehsqtcqrpkccmlctmqahitwalhspghviqpsqalasgFHRgkQED 160
Cdd:cd02674    1 GLRNLGNTCYMNSILQCL------------------------------------------------------SAD--QQD 24
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 161 VHEFLMFTVDAMkkaclpghkqvdhHSkdttLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDI------QAAQSVK 234
Cdd:cd02674   25 AQEFLLFLLDGL-------------HS----IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdAPKVTLE 87
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 235 QALEQLVKPEELNGENAYHCGLCLQRAPASNTLTLHTSAKVLILVLKRFSDVAG--NKLAKNVQYP-ECLDMQPY-MSQQ 310
Cdd:cd02674   88 DCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGstRKLTTPVTFPlNDLDLTPYvDTRS 167
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 379030631 311 NTGPLVYVLYAVLVHAGwSCHDGHYFSYVK-AQEGQWYKMDDAEVTVCSITSVLSQQAYVLFYI 373
Cdd:cd02674  168 FTGPFKYDLYAVVNHYG-SLNGGHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
81-376 3.26e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 164.74  E-value: 3.26e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  81 GLQNMGNTCYENASLQCLTYTLPLAN--YMLSREHSQTCQRPKccmLCTMQAHITWALHSPGHVIQPSQALASGFHRGK- 157
Cdd:cd02659    4 GLKNQGATCYMNSLLQQLYMTPEFRNavYSIPPTEDDDDNKSV---PLALQRLFLFLQLSESPVKTTELTDKTRSFGWDs 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 158 -----QEDVHEFLMFTVDAMKKaCLPGHKQVDhhskdttLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQAAQS 232
Cdd:cd02659   81 lntfeQHDVQEFFRVLFDKLEE-KLKGTGQEG-------LIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 233 VKQALEQLVKPEELNGENAYHCGLCLQRAPASNTLTLHTSAKVLILVLKRFS-D-VAGNKLAKNVQY--PECLDMQPYMS 308
Cdd:cd02659  153 LEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfDfETMMRIKINDRFefPLELDMEPYTE 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 309 Q-----------QNTGPLVYVLYAVLVHAGwSCHDGHYFSYVKAQE-GQWYKMDDAEVTVCSITSVLSQQ---------- 366
Cdd:cd02659  233 KglakkegdsekKDSESYIYELHGVLVHSG-DAHGGHYYSYIKDRDdGKWYKFNDDVVTPFDPNDAEEECfggeetqkty 311
                        330       340
                 ....*....|....*....|..
gi 379030631 367 ------------AYVLFYIQKS 376
Cdd:cd02659  312 dsgprafkrttnAYMLFYERKS 333
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
81-372 2.81e-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: 147.15  E-value: 2.81e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  81 GLQNMGNTCYENASLQCLTYTLPLANYMLsrehsqtcQRPKCCMLCTMQahitwalhspghviqpsqaLASGFHRGKQED 160
Cdd:cd02667    1 GLSNLGNTCFFNAVMQNLSQTPALRELLS--------ETPKELFSQVCR-------------------KAPQFKGYQQQD 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 161 VHEFLMFTVDAMKkaclpghkqvdhhskdtTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIAL----DIQAAQSVKQA 236
Cdd:cd02667   54 SHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSECSIESC 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 237 LEQLVKPEELNGENAYHCGLCLQrapASNTLTLHTSAKVLILVLKRFSDVAGN---KLAKNVQYPECLDMQPYMSQQNTG 313
Cdd:cd02667  117 LKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQPRSAnlrKVSRHVSFPEILDLAPFCDPKCNS 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 314 P-----LVYVLYAVLVHAGwSCHDGHYFSYVKAQ----------------------EGQWYKMDDAEVTVCSITSVLSQQ 366
Cdd:cd02667  194 SedkssVLYRLYGVVEHSG-TMRSGHYVAYVKVRppqqrlsdltkskpaadeagpgSGQWYYISDSDVREVSLEEVLKSE 272

                 ....*.
gi 379030631 367 AYVLFY 372
Cdd:cd02667  273 AYLLFY 278
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
81-372 2.03e-39

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: 145.15  E-value: 2.03e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  81 GLQNMGNTCYENASLQCL----TYTLpLANYMlsreHSQTCQRPKccmlctmqahitWALHSPGHVIQPSQALASGFHRG 156
Cdd:cd02663    1 GLENFGNTCYCNSVLQALyfenLLTC-LKDLF----ESISEQKKR------------TGVISPKKFITRLKRENELFDNY 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 157 KQEDVHEFLMF-------TVDAMKKACLPGHKQVDHHSKD--TTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDI 227
Cdd:cd02663   64 MHQDAHEFLNFllneiaeILDAERKAEKANRKLNNNNNAEpqPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDV 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 228 QAAQSVKQALEQLVKPEELNGENAYHCGLCLQRAPASNTLTLHTSAKVLILVLKRFS---DVAGN-KLAKNVQYPECLDM 303
Cdd:cd02663  144 EQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKydeQLNRYiKLFYRVVFPLELRL 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 379030631 304 QPYMSQQNTGPLVYVLYAVLVHAGWSCHDGHYFSYVKAQeGQWYKMDDAEVTVCSITSVL--------SQQAYVLFY 372
Cdd:cd02663  224 FNTTDDAENPDRLYELVAVVVHIGGGPNHGHYVSIVKSH-GGWLLFDDETVEKIDENAVEeffgdspnQATAYVLFY 299
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
81-372 9.33e-39

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: 144.17  E-value: 9.33e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  81 GLQNMGNTCYENASLQCLTYTLPLANYMLSRehsqTCQRPKCC-----MLCTMQAHitWALHSPGHVIQPSQALAS---- 151
Cdd:cd02664    1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSL----NLPRLGDSqsvmkKLQLLQAH--LMHTQRRAEAPPDYFLEAsrpp 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 152 GFHRGKQEDVHEFLMFTVDAMKkaclpghkqvdhhskdtTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALdiqAAQ 231
Cdd:cd02664   75 WFTPGSQQDCSEYLRYLLDRLH-----------------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL---SFP 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 232 SVKQALEQLVKPEELNGENAYHCGLCLQRAPASNTLTLHTSAKVLILVLKRFSDVAG----NKLAKNVQYPECLDMQPYM 307
Cdd:cd02664  135 SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKthvrEKIMDNVSINEVLSLPVRV 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 308 SQQNTGP-------------------LVYVLYAVLVHAGWSCHDGHYFSYVKAQ---------------------EGQWY 347
Cdd:cd02664  215 ESKSSESplekkeeesgddgelvtrqVHYRLYAVVVHSGYSSESGHYFTYARDQtdadstgqecpepkdaeendeSKNWY 294
                        330       340       350
                 ....*....|....*....|....*....|..
gi 379030631 348 KMDDAEVTVCS------ITSVLSQQ-AYVLFY 372
Cdd:cd02664  295 LFNDSRVTFSSfesvqnVTSRFPKDtPYILFY 326
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
81-354 2.95e-33

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: 129.08  E-value: 2.95e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  81 GLQNMGNTCYENASLQCLTYTLPLANYMLSrehsqtCQRPKCCMLCTMQAHITwalHSPGHVIQPSQAL----------- 149
Cdd:cd02668    1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE------CNSTEDAELKNMPPDKP---HEPQTIIDQLQLIfaqlqfgnrsv 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 150 --------ASGFHRGKQEDVHEFLMFTVDAMKkACLPGHKqvdhHSKDTTLIHQIFGGCWRSQIKCLHCHGISDTFDPYL 221
Cdd:cd02668   72 vdpsgfvkALGLDTGQQQDAQEFSKLFLSLLE-AKLSKSK----NPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFY 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 222 DIALDIQAAQSVKQALEQLVKPEELNGENAYHCGLCLQRAPASNTLTLHTSAKVLILVLKRFS----DVAGNKLAKNVQY 297
Cdd:cd02668  147 ELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVfdrkTGAKKKLNASISF 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 379030631 298 PECLDMQPYMSQQNTGPLVYVLYAVLVHAGWSCHDGHYFSYVK-AQEGQWYKMDDAEV 354
Cdd:cd02668  227 PEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDV 284
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
81-410 4.58e-24

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 106.88  E-value: 4.58e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631   81 GLQNMGNTCYENASLQCLTYTLPLAN--YMLSREHsqtcQRPKCCMLCTMQaHITWALHSPGHVIQPSQALAS------- 151
Cdd:COG5077   195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDH----PRGRDSVALALQ-RLFYNLQTGEEPVDTTELTRSfgwdsdd 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  152 GFHrgkQEDVHEFLMFTVDAMKKAclpghkqvdhhSKDTTL---IHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQ 228
Cdd:COG5077   270 SFM---QHDIQEFNRVLQDNLEKS-----------MRGTVVenaLNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVK 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  229 AAQSVKQALEQLVKPEELNGENAYHC-GLCLQRapASNTLTLHTSAKVLILVLKRFS-DV---AGNKLAKNVQYPECLDM 303
Cdd:COG5077   336 GMKNLQESFRRYIQVETLDGDNRYNAeKHGLQD--AKKGVIFESLPPVLHLQLKRFEyDFerdMMVKINDRYEFPLEIDL 413
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  304 QPYMS----QQNTGPLVYVLYAVLVHAGwSCHDGHYFSYVKAQ-EGQWYKMDDAEVTVCSITSVLSQ------------- 365
Cdd:COG5077   414 LPFLDrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkir 492
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 379030631  366 ---------QAYVLFYIQKSEWERHSESVSRGREPRALgAEDTDRRAKQGELKR 410
Cdd:COG5077   493 dhsgikrfmSAYMLVYLRKSMLDDLLNPVAAVDIPPHV-EEVLSEEIDKTEVRC 545
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
80-372 5.80e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 99.97  E-value: 5.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  80 AGLQNMGNTCYENASLQCLTYTlP--------LANYMLSREHSQTCqrpkcCMLCTMQAHITWALHSPGHVIQPSQALAS 151
Cdd:cd02671   25 VGLNNLGNTCYLNSVLQVLYFC-PgfkhglkhLVSLISSVEQLQSS-----FLLNPEKYNDELANQAPRRLLNALREVNP 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 152 GFHRGKQEDVHEFLMftvdamkkaCLPGHKQvdhhskdtTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQAAQ 231
Cdd:cd02671   99 MYEGYLQHDAQEVLQ---------CILGNIQ--------ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 232 -------------------SVKQALEQLVKPEELNGENAYHCGLCLQRAPASNTLTLHTSAKVLILVLKRFS------DV 286
Cdd:cd02671  162 lskseesseispdpktemkTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAangsefDC 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 287 AGNKLAKNVQYPECLDMQPY-MSQQNTGPlVYVLYAVLVHAGWSCHDGHYFSYVKaqegqWYKMDDAEVTV--------- 356
Cdd:cd02671  242 YGGLSKVNTPLLTPLKLSLEeWSTKPKND-VYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVteekdflea 315
                        330
                 ....*....|....*.
gi 379030631 357 CSITSVLSQQAYVLFY 372
Cdd:cd02671  316 LSPNTSSTSTPYLLFY 331
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
81-372 6.27e-21

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: 93.54  E-value: 6.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  81 GLQNMGNTCYENASLQCLtYTLP-LANYMLSREHSQTC--QRPKCCMLCTM---------------QAHITWALHSPGHv 142
Cdd:cd02658    1 GLRNLGNSCYLNSVLQVL-FSIPsFQWRYDDLENKFPSdvVDPANDLNCQLikladgllsgryskpASLKSENDPYQVG- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 143 IQPSQ--ALASGFHR----GKQEDVHEFLMFTVDAMKKAClpghkqvdhHSKDTTLIHQIFGGCWRSQIKCLHCHGISDT 216
Cdd:cd02658   79 IKPSMfkALIGKGHPefstMRQQDALEFLLHLIDKLDRES---------FKNLGLNPNDLFKFMIEDRLECLSCKKVKYT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 217 FDPYLDIALDIQAA--------------QSVKQALEQLVKPEELngenAYHCGLCLQRAPASNTLTLHTSAKVLILVLKR 282
Cdd:cd02658  150 SELSEILSLPVPKDeatekeegelvyepVPLEDCLKAYFAPETI----EDFCSTCKEKTTATKTTGFKTFPDYLVINMKR 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 283 FsdvagnKLAKNVQyPECLDMQ---PYMsqqnTGPLVYVLYAVLVHAGWSCHDGHYFSYVK---AQEGQWYKMDDAEVTV 356
Cdd:cd02658  226 F------QLLENWV-PKKLDVPidvPEE----LGPGKYELIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFNDEKVVA 294
                        330
                 ....*....|....*.
gi 379030631 357 CSITSVLSQQAYVLFY 372
Cdd:cd02658  295 SQDPPEMKKLGYIYFY 310
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
81-372 4.23e-19

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


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 88.16  E-value: 4.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  81 GLQNMGNTCYENASLQCLtYTLP-----LANYMLSREHS-QTCQRPKCCMLCTMQAhitwaLHSPGHVIQPSqALASGFH 154
Cdd:cd02657    1 GLTNLGNTCYLNSTLQCL-RSVPelrdaLKNYNPARRGAnQSSDNLTNALRDLFDT-----MDKKQEPVPPI-EFLQLLR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 155 RG-------------KQEDVHEFLMFTVDAMKkACLPGHkqvdhhSKDTTLIHQIFGGCWRSQIKC-------------- 207
Cdd:cd02657   74 MAfpqfaekqnqggyAQQDAEECWSQLLSVLS-QKLPGA------GSKGSFIDQLFGIELETKMKCtespdeeevstese 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 208 --LHCHgISDTFD-PYLDIALDiqaaqsvKQALEQLVKPEELNGENAYHcglclqrapaSNTLTLHTSAKVLILVLKRF- 283
Cdd:cd02657  147 ykLQCH-ISITTEvNYLQDGLK-------KGLEEEIEKHSPTLGRDAIY----------TKTSRISRLPKYLTVQFVRFf 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 284 --SDVAGN-KLAKNVQYPECLDMQPYMSqqNTGplVYVLYAVLVHAGWSCHDGHYFSYVK-AQEGQWYKMDDAEVTVCSI 359
Cdd:cd02657  209 wkRDIQKKaKILRKVKFPFELDLYELCT--PSG--YYELVAVITHQGRSADSGHYVAWVRrKNDGKWIKFDDDKVSEVTE 284
                        330       340
                 ....*....|....*....|
gi 379030631 360 TSVL-------SQQAYVLFY 372
Cdd:cd02657  285 EDILklsgggdWHIAYILLY 304
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
237-376 7.20e-18

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 87.25  E-value: 7.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 237 LEQLVKPEELNGENAYHCGLCLQRAPASNTLTLHTSAKVLILVLKRFSDV--AGNKLAKNVQYP-ECLDMQPYMSQQNTG 313
Cdd:COG5560  681 LNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVrsFRDKIDDLVEYPiDDLDLSGVEYMVDDP 760
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 379030631 314 PLVYVLYAVLVHAGWScHDGHYFSYVK-AQEGQWYKMDDAEVT-VCSITSVLSqQAYVLFYIQKS 376
Cdd:COG5560  761 RLIYDLYAVDNHYGGL-SGGHYTAYARnFANNGWYLFDDSRITeVDPEDSVTS-SAYVLFYRRKS 823
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
81-375 2.08e-17

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 82.54  E-value: 2.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  81 GLQNMGNTCYENASLQCLTYTLP-LANYML-----SREHSQTCQRPKCCM-LCTMQAHITwALHSPGHviqpsQALASGF 153
Cdd:COG5533    1 GLPNLGNTCFMNSVLQILALYLPkLDELLDdlskeLKVLKNVIRKPEPDLnQEEALKLFT-ALWSSKE-----HKVGWIP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 154 HRGKQEDVHEFLMFTVDAMKkacLPGHKQVdhhskdTTLIHQIFGgcwrSQIKclhcHGISDTFDpyLDIALDIQAAQSV 233
Cdd:COG5533   75 PMGSQEDAHELLGKLLDELK---LDLVNSF------TIRIFKTTK----DKKK----TSTGDWFD--IIIELPDQTWVNN 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 234 KQALEQLVK------PEELNGENAYHCGLCLQrAPASNTLTLHTSAKVLILVLKRFSDVAGN-KLAKNVQYPECLDMQPY 306
Cdd:COG5533  136 LKTLQEFIDnmeelvDDETGVKAKENEELEVQ-AKQEYEVSFVKLPKILTIQLKRFANLGGNqKIDTEVDEKFELPVKHD 214
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 379030631 307 MSQQNTGPLVYVLYAVLVHAGwSCHDGHYFSYVKaQEGQWYKMDDAEVTVCSITSVL---SQQAYVLFYIQK 375
Cdd:COG5533  215 QILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPVSEEEAInekAKNAYLYFYERI 284
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
70-227 1.90e-16

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 82.62  E-value: 1.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  70 LSSRRPAAVGaGLQNMGNTCYENASLQCLTYTLPLANYMLSREHSQTCQR--PKCCM--LCTMQAHITWALHSPG-HVIQ 144
Cdd:COG5560  257 RSINKEAGTC-GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEenPLGMHgsVASAYADLIKQLYDGNlHAFT 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 145 PSQ------ALASGFHRGKQEDVHEFLMFTVDAM--------------KKACLPGHKQV----------DHHSKDTTLIH 194
Cdd:COG5560  336 PSGfkktigSFNEEFSGYDQQDSQEFIAFLLDGLhedlnriikkpytsKPDLSPGDDVVvkkkakecwwEHLKRNDSIIT 415
                        170       180       190
                 ....*....|....*....|....*....|...
gi 379030631 195 QIFGGCWRSQIKCLHCHGISDTFDPYLDIALDI 227
Cdd:COG5560  416 DLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
81-372 3.24e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 69.32  E-value: 3.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  81 GLQNMGNTCYENASLQCLTyTLP-----LANYMlsrehsqtcqrpkccmlctmqahitwalhspghviqpsqalasgfhr 155
Cdd:cd02662    1 GLVNLGNTCFMNSVLQALA-SLPslieyLEEFL----------------------------------------------- 32
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 156 gKQEDVHEFLmftvdamkkaclpghkqvdHHSkdTTLIHQIFGGCWR----SQIKCLHCHGIS-DTFDPYLDIALDIQAA 230
Cdd:cd02662   33 -EQQDAHELF-------------------QVL--LETLEQLLKFPFDgllaSRIVCLQCGESSkVRYESFTMLSLPVPNQ 90
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 231 QSV-----KQALEQLVKPEELNGENAYHCGLCLQRAPasntltlhtsaKVLILVLKRFS-DVAGN--KLAKNVQYPECLd 302
Cdd:cd02662   91 SSGsgttlEHCLDDFLSTEIIDDYKCDRCQTVIVRLP-----------QILCIHLSRSVfDGRGTstKNSCKVSFPERL- 158
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 303 mQPYMsqqntgplvYVLYAVLVHAGwSCHDGHYFSYVKAQE---------------------GQWYKMDDAEVTVCSITS 361
Cdd:cd02662  159 -PKVL---------YRLRAVVVHYG-SHSSGHYVCYRRKPLfskdkepgsfvrmregpsstsHPWWRISDTTVKEVSESE 227
                        330
                 ....*....|..
gi 379030631 362 VLSQ-QAYVLFY 372
Cdd:cd02662  228 VLEQkSAYMLFY 239
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
80-351 8.20e-11

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 63.06  E-value: 8.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631   80 AGLQNMGNTCYENASLQCLTYTLPLANYMLSreHSQT-CQRPKCcMLCTM---------------QA------------- 130
Cdd:pfam13423   1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALS--HLATeCLKEHC-LLCELgflfdmlekakgkncQAsnflralssipea 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  131 ---------HITWALHSPGHVIQpsqalasGFHRgkqedvheFLMftvdamKKACLPGHKQVDHHSKDTTLIHQIFGGCW 201
Cdd:pfam13423  78 salglldedRETNSAISLSSLIQ-------SFNR--------FLL------DQLSSEENSTPPNPSPAESPLEQLFGIDA 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  202 RSQIKCLHCHGISDTFDPYLDIALD------IQAAQSVKQALEQLVKpEELNGENAY--HCGLCLQRAPASNTLTLHTSA 273
Cdd:pfam13423 137 ETTIRCSNCGHESVRESSTHVLDLIyprkpsSNNKKPPNQTFSSILK-SSLERETTTkaWCEKCKRYQPLESRRTVRNLP 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  274 KVLILVLKRFSDVAGNKLAKNVQYPECLDMQPYMSQQNTGPL-VYVLYAVLVHAGWSCHDGHYFSYVK--------AQEG 344
Cdd:pfam13423 216 PVLSLNAALTNEEWRQLWKTPGWLPPEIGLTLSDDLQGDNEIvKYELRGVVVHIGDSGTSGHLVSFVKvadseledPTES 295

                  ....*..
gi 379030631  345 QWYKMDD 351
Cdd:pfam13423 296 QWYLFND 302
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
81-372 8.75e-10

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


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 60.80  E-value: 8.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  81 GLQNMGNTCYENASLQCLTYTLPLANYMLSREHSQTCQRpKCCMLCTMQAHITWALHSP----GHViQPSQ-----ALAS 151
Cdd:cd02669  121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKD-RKSELVKRLSELIRKIWNPrnfkGHV-SPHEllqavSKVS 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 152 G--FHRGKQEDVHEFLMFTVDAMkkaclpgHKQVDHHSKD-TTLIHQIFGGCWR--------------SQIKCLHCHGIS 214
Cdd:cd02669  199 KkkFSITEQSDPVEFLSWLLNTL-------HKDLGGSKKPnSSIIHDCFQGKVQietqkikphaeeegSKDKFFKDSRVK 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 215 DTFD-PYLDIALDI---------QAAQSVKQ-ALEQLVKpeELNGENAYHCGlclqraPASNTLTLHTSAKVLILVLKRF 283
Cdd:cd02669  272 KTSVsPFLLLTLDLpppplfkdgNEENIIPQvPLKQLLK--KYDGKTETELK------DSLKRYLISRLPKYLIFHIKRF 343
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 284 SDVAGNKlAKN---VQYP-ECLDMQPYMS--QQNTGPLV-YVLYAVLVHAGWSCHDGHYFSYV-KAQEGQWYKMDDAEVT 355
Cdd:cd02669  344 SKNNFFK-EKNptiVNFPiKNLDLSDYVHfdKPSLNLSTkYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQDLNVK 422
                        330
                 ....*....|....*..
gi 379030631 356 VCSITSVLSQQAYVLFY 372
Cdd:cd02669  423 EVLPQLIFLSESYIQIW 439
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
82-372 2.13e-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: 58.31  E-value: 2.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631  82 LQNMGNTCYENASLQcltytlplanymlsrehsqtcqrpkccmlctmqahitwALHSPGHVIqpsqalaSGFHRGKQEDV 161
Cdd:cd02673    2 LVNTGNSCYFNSTMQ--------------------------------------ALSSIGKIN-------TEFDNDDQQDA 36
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 162 HEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQI--FGGCWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVKQalEQ 239
Cdd:cd02673   37 HEFLLTLLEAIDDIMQVNRTNVPPSNIEIKRLNPLeaFKYTIESSYVCIGCSFEENVSDVGNFLDVSMIDNKLDID--EL 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 240 LVKPEELNGENAYHCGLC-LQRAPASNTLTlhTSAKVLILVLKRF--SDVAGNKLAKNvqypeCLDMQPYMSQQNTgplv 316
Cdd:cd02673  115 LISNFKTWSPIEKDCSSCkCESAISSERIM--TFPECLSINLKRYklRIATSDYLKKN-----EEIMKKYCGTDAK---- 183
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 379030631 317 YVLYAVLVHAGWSCHDGHYFSYVK--AQEGQWYKMDDAEVTVCSITSVL---SQQAYVLFY 372
Cdd:cd02673  184 YSLVAVICHLGESPYDGHYIAYTKelYNGSSWLYCSDDEIRPVSKNDVStnaRSSGYLIFY 244
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
214-372 7.21e-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: 41.36  E-value: 7.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 214 SDTFDPYLDIALDIQAAQ--------SVKQALEQLVKPEELNGENAYhCGLCLQRAPASNTLTLHTSakVLILVLKRFSD 285
Cdd:cd02670   35 DKLLMPLLEPKVDIIHGGkkdqdddkLVNERLLQIPVPDDDDGGGIT-LEQCLEQYFNNSVFAKAPS--CLIICLKRYGK 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 286 VAGN--KLAKNVQYPECLDMQPYMSQQNT----------------------GPLVYVLYAVLVHAGWSCHDGHYFSYVK- 340
Cdd:cd02670  112 TEGKaqKMFKKILIPDEIDIPDFVADDPRacskcqlecrvcyddkdfsptcGKFKLSLCSAVCHRGTSLETGHYVAFVRy 191
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 379030631 341 -----------AQEGQWYK---MDDAEVTVCSI---TSVLSQQAYVLFY 372
Cdd:cd02670  192 gsysltetdneAYNAQWVFfddMADRDGVSNGFnipAARLLEDPYMLFY 240
HABP4_PAI-RBP1 pfam04774
Hyaluronan / mRNA binding family; This family includes the HABP4 family of hyaluronan-binding ...
417-454 9.25e-04

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: 38.89  E-value: 9.25e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 379030631  417 APELDEHLVERATQESTLDHWKFLQEQNKTKPEFNVGK 454
Cdd:pfam04774  68 AAAEEEEKEPNEDKEMTLDEYKKVQEEKRALPAFNIRK 105
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
275-373 1.39e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 40.23  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379030631 275 VLILVLKRFS--DVAGNKLAKNVQYPECLDMQPYMsqqntgplvyvLYAVLVHAGwSCHDGHYFSYVKAQEGQ-WYKMDD 351
Cdd:cd02665  131 VLTFELSRFEfnQGRPEKIHDKLEFPQIIQQVPYE-----------LHAVLVHEG-QANAGHYWAYIYKQSRQeWEKYND 198
                         90       100       110
                 ....*....|....*....|....*....|
gi 379030631 352 AEVTVCSITSVLSQ--------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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