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Conserved domains on  [gi|1722208472|ref|NP_001359025|]
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ubiquitin carboxyl-terminal hydrolase 47 isoform h [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 186-566 7.77e-154

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: 466.35  E-value: 7.77e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  186 GYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWeFEESEEDPVTSIPYQLQRLFVLLQTSKKRAIET--TDVTRSFGWD 263
Cdd:cd02659      1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-PPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTelTDKTRSFGWD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  264 SSEAWQQHDVQELCRVMFDALEQKWKQTEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSsqafasV 343
Cdd:cd02659     80 SLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKN------L 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  344 EEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSTFIDV 423
Cdd:cd02659    154 EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEK 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  424 EDEKSPQTESCTDSGaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknSLIYELFSVMVHSGSAAGGH 503
Cdd:cd02659    234 GLAKKEGDSEKKDSE---------------------------------------------SYIYELHGVLVHSGDAHGGH 268

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1722208472  504 YYACIKSFSDEQWYSFNDQHVSRITQEDIKKTH---GGSSGSRGYYSSAFASSTNAYMLIYRLKDP 566
Cdd:cd02659    269 YYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECfggEETQKTYDSGPRAFKRTTNAYMLFYERKSP 334
USP47_C super family cl45120
Ubiquitin carboxyl-terminal hydrolase 47 C-terminal; This is the C-terminal domain of ...
 1124-1312 1.40e-76

Ubiquitin carboxyl-terminal hydrolase 47 C-terminal; This is the C-terminal domain of Ubiquitin carboxyl-terminal hydrolase 47 (USP47), a ubiquitin-specific protease involved in deubiquitinating of monoubiquitinated DNA polymerase beta (Polbeta), being required for its stability and, therefore, plays a role in DNA base excision repair (BER). The C-terminal domains in USPs mediate protein- protein interactions.


The actual alignment was detected with superfamily member pfam19718:

Pssm-ID: 466158  Cd Length: 240  Bit Score: 253.52  E-value: 1.40e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472 1124 RVKVYQLLVNEQEPCKFLLDAVFAKGMTVRQSKEELIPQLREQ-CGLELSIDRFRLRKKTWKNPGTVFLDYHIYEeDINI 1202
Cdd:pfam19718    1 RVKLYQLQVNNTEFCKYMMESIVAKGTPVREFKKQIIEEAKVQgIDCVLELDKMRLRKKTWVYPGTVYLDHQVID-DIQI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472 1203 SSNWEVFLEVLDGVEKMKSMSQLAVLSRRWKPSEMKLDPFQEVVLESSSVDELREKLSEISGIPLDDIEFAKGRGTFPCD 1282
Cdd:pfam19718   80 YPNWEMYVEPLKGPEKKKHTTQLQVYVRRWHPSQCSVDPFEEIILDNRTPKELKEKLSELSGVPVEYIYIAKGKGSFPCE 159

                          170       180       190
                   ....*....|....*....|....*....|
gi 1722208472 1283 ISVLDIHQDLDWNPKVSTLNVWPLYICDDG 1312
Cdd:pfam19718  160 ISVLDIENELEWNSITSSLSSYPLYLYEDG 189
MSCRAMM_ClfA super family cl41352
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 834-1025 2.87e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


The actual alignment was detected with superfamily member NF033609:

Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 42.20  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  834 VSYSKRTAYQKAGGDSGNVDDDC--ERVKGPvgslKSVEAILEESTEKLKSLSLQQQQDGDNGDSSKSTETSDF--ENIE 909
Cdd:NF033609   521 MSWDNEVAFNNGSGSGDGIDKPVvpEQPDEP----GEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSgsDSAS 596

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  910 SPLNERDSSASVDNRELEQHIQTSDPENFQ-SEERSDSDVNNDRSTSSVDSDILSSSHSSDTLCNADNAQiplanglDSH 988
Cdd:NF033609   597 DSDSASDSDSASDSDSASDSDSASDSDSASdSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDS-------DSD 669

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1722208472  989 SITSSRRTKANEGKKETWDTAEEDSGTDSEYDESGKS 1025
Cdd:NF033609   670 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 706
 
Name Accession Description Interval E-value
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 186-566 7.77e-154

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: 466.35  E-value: 7.77e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  186 GYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWeFEESEEDPVTSIPYQLQRLFVLLQTSKKRAIET--TDVTRSFGWD 263
Cdd:cd02659      1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-PPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTelTDKTRSFGWD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  264 SSEAWQQHDVQELCRVMFDALEQKWKQTEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSsqafasV 343
Cdd:cd02659     80 SLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKN------L 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  344 EEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSTFIDV 423
Cdd:cd02659    154 EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEK 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  424 EDEKSPQTESCTDSGaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknSLIYELFSVMVHSGSAAGGH 503
Cdd:cd02659    234 GLAKKEGDSEKKDSE---------------------------------------------SYIYELHGVLVHSGDAHGGH 268

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1722208472  504 YYACIKSFSDEQWYSFNDQHVSRITQEDIKKTH---GGSSGSRGYYSSAFASSTNAYMLIYRLKDP 566
Cdd:cd02659    269 YYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECfggEETQKTYDSGPRAFKRTTNAYMLFYERKSP 334
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 182-612 3.28e-77

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 278.29  E-value: 3.28e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  182 KSETGYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEEseEDPVTSIPYQLQRLFVLLQTSKKrAIETTDVTRSFG 261
Cdd:COG5077    188 KKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDH--PRGRDSVALALQRLFYNLQTGEE-PVDTTELTRSFG 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  262 WDSSEAWQQHDVQELCRVMFDALEQKWKQTEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLvirpygSSQAFA 341
Cdd:COG5077    265 WDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL------NVKGMK 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  342 SVEEALHAFIQPEILDGPNQYFCERCKKKcDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSTFI 421
Cdd:COG5077    339 NLQESFRRYIQVETLDGDNRYNAEKHGLQ-DAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFL 417

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  422 DVEDEKSpqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglEKNSLIYELFSVMVHSGSAAG 501
Cdd:COG5077    418 DRDADKS----------------------------------------------------ENSDAVYVLYGVLVHSGDLHE 445

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  502 GHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKTH---GGSSGSRGYYSSAFASSTNAYMLIYRLKDPARN-AKFLEVDE 577
Cdd:COG5077    446 GHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENfggDHPYKDKIRDHSGIKRFMSAYMLVYLRKSMLDDlLNPVAAVD 525

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1722208472  578 YPEHIKNLVQKERELEEQEKRQREIERNTCKIKLF 612
Cdd:COG5077    526 IPPHVEEVLSEEIDKTEVRCKEIDEIHLYRGVRLY 560
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
188-561 3.76e-77

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 257.76  E-value: 3.76e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  188 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWE--FEESEEDPVTSIPYQLQRLF-VLLQTSKKRAIETTDVTRSFGWDS 264
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISplSEDSRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSLGKLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  265 SE--AWQQHDVQELCRVMFDALEQKWKQ---TEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQA 339
Cdd:pfam00443   81 PDfsGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  340 FASVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTmhRIKLNDRMTFPEELDMST 419
Cdd:pfam00443  161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLELDLSR 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  420 FIDVEDEKspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksgLEKNSLIYELFSVMVHSGSA 499
Cdd:pfam00443  239 YLAEELKP----------------------------------------------------KTNNLQDYRLVAVVVHSGSL 266

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1722208472  500 AGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKTHggssgsrgyyssafasstNAYMLIY 561
Cdd:pfam00443  267 SSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLSS------------------SAYILFY 310
USP47_C pfam19718
Ubiquitin carboxyl-terminal hydrolase 47 C-terminal; This is the C-terminal domain of ...
 1124-1312 1.40e-76

Ubiquitin carboxyl-terminal hydrolase 47 C-terminal; This is the C-terminal domain of Ubiquitin carboxyl-terminal hydrolase 47 (USP47), a ubiquitin-specific protease involved in deubiquitinating of monoubiquitinated DNA polymerase beta (Polbeta), being required for its stability and, therefore, plays a role in DNA base excision repair (BER). The C-terminal domains in USPs mediate protein- protein interactions.


Pssm-ID: 466158  Cd Length: 240  Bit Score: 253.52  E-value: 1.40e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472 1124 RVKVYQLLVNEQEPCKFLLDAVFAKGMTVRQSKEELIPQLREQ-CGLELSIDRFRLRKKTWKNPGTVFLDYHIYEeDINI 1202
Cdd:pfam19718    1 RVKLYQLQVNNTEFCKYMMESIVAKGTPVREFKKQIIEEAKVQgIDCVLELDKMRLRKKTWVYPGTVYLDHQVID-DIQI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472 1203 SSNWEVFLEVLDGVEKMKSMSQLAVLSRRWKPSEMKLDPFQEVVLESSSVDELREKLSEISGIPLDDIEFAKGRGTFPCD 1282
Cdd:pfam19718   80 YPNWEMYVEPLKGPEKKKHTTQLQVYVRRWHPSQCSVDPFEEIILDNRTPKELKEKLSELSGVPVEYIYIAKGKGSFPCE 159

                          170       180       190
                   ....*....|....*....|....*....|
gi 1722208472 1283 ISVLDIHQDLDWNPKVSTLNVWPLYICDDG 1312
Cdd:pfam19718  160 ISVLDIENELEWNSITSSLSSYPLYLYEDG 189
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 834-1025 2.87e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 42.20  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  834 VSYSKRTAYQKAGGDSGNVDDDC--ERVKGPvgslKSVEAILEESTEKLKSLSLQQQQDGDNGDSSKSTETSDF--ENIE 909
Cdd:NF033609   521 MSWDNEVAFNNGSGSGDGIDKPVvpEQPDEP----GEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSgsDSAS 596

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  910 SPLNERDSSASVDNRELEQHIQTSDPENFQ-SEERSDSDVNNDRSTSSVDSDILSSSHSSDTLCNADNAQiplanglDSH 988
Cdd:NF033609   597 DSDSASDSDSASDSDSASDSDSASDSDSASdSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDS-------DSD 669

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1722208472  989 SITSSRRTKANEGKKETWDTAEEDSGTDSEYDESGKS 1025
Cdd:NF033609   670 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 706
 
Name Accession Description Interval E-value
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 186-566 7.77e-154

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: 466.35  E-value: 7.77e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  186 GYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWeFEESEEDPVTSIPYQLQRLFVLLQTSKKRAIET--TDVTRSFGWD 263
Cdd:cd02659      1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-PPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTelTDKTRSFGWD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  264 SSEAWQQHDVQELCRVMFDALEQKWKQTEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSsqafasV 343
Cdd:cd02659     80 SLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKN------L 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  344 EEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSTFIDV 423
Cdd:cd02659    154 EESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEK 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  424 EDEKSPQTESCTDSGaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknSLIYELFSVMVHSGSAAGGH 503
Cdd:cd02659    234 GLAKKEGDSEKKDSE---------------------------------------------SYIYELHGVLVHSGDAHGGH 268

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1722208472  504 YYACIKSFSDEQWYSFNDQHVSRITQEDIKKTH---GGSSGSRGYYSSAFASSTNAYMLIYRLKDP 566
Cdd:cd02659    269 YYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECfggEETQKTYDSGPRAFKRTTNAYMLFYERKSP 334
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 182-612 3.28e-77

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 278.29  E-value: 3.28e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  182 KSETGYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEEseEDPVTSIPYQLQRLFVLLQTSKKrAIETTDVTRSFG 261
Cdd:COG5077    188 KKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDH--PRGRDSVALALQRLFYNLQTGEE-PVDTTELTRSFG 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  262 WDSSEAWQQHDVQELCRVMFDALEQKWKQTEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLvirpygSSQAFA 341
Cdd:COG5077    265 WDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQL------NVKGMK 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  342 SVEEALHAFIQPEILDGPNQYFCERCKKKcDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSTFI 421
Cdd:COG5077    339 NLQESFRRYIQVETLDGDNRYNAEKHGLQ-DAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFL 417

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  422 DVEDEKSpqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglEKNSLIYELFSVMVHSGSAAG 501
Cdd:COG5077    418 DRDADKS----------------------------------------------------ENSDAVYVLYGVLVHSGDLHE 445

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  502 GHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKTH---GGSSGSRGYYSSAFASSTNAYMLIYRLKDPARN-AKFLEVDE 577
Cdd:COG5077    446 GHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENfggDHPYKDKIRDHSGIKRFMSAYMLVYLRKSMLDDlLNPVAAVD 525

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1722208472  578 YPEHIKNLVQKERELEEQEKRQREIERNTCKIKLF 612
Cdd:COG5077    526 IPPHVEEVLSEEIDKTEVRCKEIDEIHLYRGVRLY 560
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
188-561 3.76e-77

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 257.76  E-value: 3.76e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  188 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWE--FEESEEDPVTSIPYQLQRLF-VLLQTSKKRAIETTDVTRSFGWDS 264
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISplSEDSRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSLGKLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  265 SE--AWQQHDVQELCRVMFDALEQKWKQ---TEQADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQA 339
Cdd:pfam00443   81 PDfsGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  340 FASVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTmhRIKLNDRMTFPEELDMST 419
Cdd:pfam00443  161 TASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLELDLSR 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  420 FIDVEDEKspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksgLEKNSLIYELFSVMVHSGSA 499
Cdd:pfam00443  239 YLAEELKP----------------------------------------------------KTNNLQDYRLVAVVVHSGSL 266

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1722208472  500 AGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKTHggssgsrgyyssafasstNAYMLIY 561
Cdd:pfam00443  267 SSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLSS------------------SAYILFY 310
USP47_C pfam19718
Ubiquitin carboxyl-terminal hydrolase 47 C-terminal; This is the C-terminal domain of ...
 1124-1312 1.40e-76

Ubiquitin carboxyl-terminal hydrolase 47 C-terminal; This is the C-terminal domain of Ubiquitin carboxyl-terminal hydrolase 47 (USP47), a ubiquitin-specific protease involved in deubiquitinating of monoubiquitinated DNA polymerase beta (Polbeta), being required for its stability and, therefore, plays a role in DNA base excision repair (BER). The C-terminal domains in USPs mediate protein- protein interactions.


Pssm-ID: 466158  Cd Length: 240  Bit Score: 253.52  E-value: 1.40e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472 1124 RVKVYQLLVNEQEPCKFLLDAVFAKGMTVRQSKEELIPQLREQ-CGLELSIDRFRLRKKTWKNPGTVFLDYHIYEeDINI 1202
Cdd:pfam19718    1 RVKLYQLQVNNTEFCKYMMESIVAKGTPVREFKKQIIEEAKVQgIDCVLELDKMRLRKKTWVYPGTVYLDHQVID-DIQI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472 1203 SSNWEVFLEVLDGVEKMKSMSQLAVLSRRWKPSEMKLDPFQEVVLESSSVDELREKLSEISGIPLDDIEFAKGRGTFPCD 1282
Cdd:pfam19718   80 YPNWEMYVEPLKGPEKKKHTTQLQVYVRRWHPSQCSVDPFEEIILDNRTPKELKEKLSELSGVPVEYIYIAKGKGSFPCE 159

                          170       180       190
                   ....*....|....*....|....*....|
gi 1722208472 1283 ISVLDIHQDLDWNPKVSTLNVWPLYICDDG 1312
Cdd:pfam19718  160 ISVLDIENELEWNSITSSLSSYPLYLYEDG 189
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 189-562 1.62e-59

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: 207.66  E-value: 1.62e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  189 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDPV---------TSIPYQLQRLFVLLQTSKKRAIETTDVTRS 259
Cdd:cd02668      1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNmppdkphepQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  260 FGWDSSeawQQHDVQELCRVMFDALEQKWKQTEQADLIN---ELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIrpygs 336
Cdd:cd02668     81 LGLDTG---QQQDAQEFSKLFLSLLEAKLSKSKNPDLKNivqDLFRGEYSYVTQCSKCGRESSLPSKFYELELQL----- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  337 sQAFASVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELD 416
Cdd:cd02668    153 -KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILD 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  417 MSTFIDVEDEkspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglekNSLIYELFSVMVHS 496
Cdd:cd02668    232 MGEYLAESDE--------------------------------------------------------GSYVYELSGVLIHQ 255

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1722208472  497 G-SAAGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIK--KTHGGSSGSRGYYSSAFASSTNAYMLIYR 562
Cdd:cd02668    256 GvSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKlgNSEDPAKPRKSEIKKGTHSSRTAYMLVYK 324
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 189-562 1.81e-58

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: 202.33  E-value: 1.81e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  189 GLVNQAMTCYLNSLLQTLFMtpefrnalykwefeeseedpvtsipyqlqrlfvllqtskkraiettdvtrsfgwdsseaw 268
Cdd:cd02257      1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  269 QQHDVQELCRVMFDALEQKWKQ--------TEQADLINELYQGKLKDYVRCLECGYEG--WRIDTYLDIPLVIRPYGSSq 338
Cdd:cd02257     21 EQQDAHEFLLFLLDKLHEELKKsskrtsdsSSLKSLIHDLFGGKLESTIVCLECGHESvsTEPELFLSLPLPVKGLPQV- 99

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  339 afaSVEEALHAFIQPEILDGPNQYFCErCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYtTMHRIKLNDRMTFPEELDMS 418
Cdd:cd02257    100 ---SLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNE-DGTKEKLNTKVSFPLELDLS 174

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  419 TFIDVEDEKSPQtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglEKNSLIYELFSVMVHSGS 498
Cdd:cd02257    175 PYLSEGEKDSDS--------------------------------------------------DNGSYKYELVAVVVHSGT 204

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1722208472  499 AA-GGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKthggssgsrgyyssAFASSTNAYMLIYR 562
Cdd:cd02257    205 SAdSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLE--------------FGSLSSSAYILFYE 255
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 189-561 3.16e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 174.39  E-value: 3.16e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  189 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDP----VTSIPYQLQRlfVLLQTSKKRAI-----ETTDVTRS 259
Cdd:cd02661      3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEgfcmMCALEAHVER--ALASSGPGSAPrifssNLKQISKH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  260 FGWDSseawqQHDVQELCRVMFDALEQ----KWKQTEQAD-------LINELYQGKLKDYVRCLECGYEGWRIDTYLDIP 328
Cdd:cd02661     81 FRIGR-----QEDAHEFLRYLLDAMQKacldRFKKLKAVDpssqettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLS 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  329 LVIRpyGSSqafaSVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYttMHriKLNDR 408
Cdd:cd02661    156 LDIK--GAD----SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GG--KINKQ 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  409 MTFPEELDMSTFidvedekspqtesctdsgaenegschsdqMSNdfSNDdgvdegicletnsgtekisksglekNSLIYE 488
Cdd:cd02661    226 ISFPETLDLSPY-----------------------------MSQ--PND-------------------------GPLKYK 249

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1722208472  489 LFSVMVHSG-SAAGGHYYACIKSfSDEQWYSFNDQHVSRITQEDIkkthggssgsrgyyssafaSSTNAYMLIY 561
Cdd:cd02661    250 LYAVLVHSGfSPHSGHYYCYVKS-SNGKWYNMDDSKVSPVSIETV-------------------LSQKAYILFY 303
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 189-562 9.16e-47

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 171.14  E-value: 9.16e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  189 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKweFEESEEDPVTSIPYQLQRLFVLLQTSKKRAIETTDvtrSFGWDSSEAW 268
Cdd:cd02664      1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS--LNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPD---YFLEASRPPW 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  269 ----QQHDVQELCRVMFDALEQkwkqteqadLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLvirpygssqAFASVE 344
Cdd:cd02664     76 ftpgSQQDCSEYLRYLLDRLHT---------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL---------SFPSVQ 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  345 EALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMStfidVE 424
Cdd:cd02664    138 DLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLP----VR 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  425 DEkspqTESCTDSGAENEGschsdqmsndfsnDDGVDEGICLETnsgtekisksgleknsLIYELFSVMVHSG-SAAGGH 503
Cdd:cd02664    214 VE----SKSSESPLEKKEE-------------ESGDDGELVTRQ----------------VHYRLYAVVVHSGySSESGH 260

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1722208472  504 YY--------------ACIKSFSDEQ------WYSFNDQHVSRITQEDIKKThggssgsrgyysSAFASSTNAYMLIYR 562
Cdd:cd02664    261 YFtyardqtdadstgqECPEPKDAEEndesknWYLFNDSRVTFSSFESVQNV------------TSRFPKDTPYILFYE 327
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 269-562 1.52e-34

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


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 132.41  E-value: 1.52e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  269 QQHDVQELCRVMFDALEQkwkqteqadLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQAFASVEEALH 348
Cdd:cd02674     21 DQQDAQEFLLFLLDGLHS---------IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDAPKVTLEDCLR 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  349 AFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMhrIKLNDRMTFP-EELDMSTFIDVEDEK 427
Cdd:cd02674     92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGST--RKLTTPVTFPlNDLDLTPYVDTRSFT 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  428 SPQTesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknsliYELFSVMVHSGSAAGGHYYAC 507
Cdd:cd02674    170 GPFK-------------------------------------------------------YDLYAVVNHYGSLNGGHYTAY 194

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1722208472  508 IKSFSDEQWYSFNDQHVSRITQEDIKkthggssgsrgyyssafasSTNAYMLIYR 562
Cdd:cd02674    195 CKNNETNDWYKFDDSRVTKVSESSVV-------------------SSSAYILFYE 230
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 189-561 1.83e-29

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 120.56  E-value: 1.83e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  189 GLVNQAMTCYLNSLLQTLFMTPEFRNALY--KWEFEESEEDPVTSIPYQLQRLFVLLQTSKKRaiettdvtRSFG----- 261
Cdd:cd02660      2 GLINLGATCFMNVILQALLHNPLLRNYFLsdRHSCTCLSCSPNSCLSCAMDEIFQEFYYSGDR--------SPYGpinll 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  262 ---WDSS---EAWQQHDVQELCRVMFDALEQKWK--QTEQAD------LINELYQGKLKDYVRCLECGYEGWRIDTYLDI 327
Cdd:cd02660     74 ylsWKHSrnlAGYSQQDAHEFFQFLLDQLHTHYGgdKNEANDeshcncIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  328 PLVIRPYGSS---------QAFASVEEALHAFIQPEILdGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYT 398
Cdd:cd02660    154 SLDIPNKSTPswalgesgvSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLN 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  399 TMHRiKLNDRMTFPEELDMSTFIDVedekspqtesctdsgaenegSCHSDQMSNDFSNDdgvdegicletnsgtekisks 478
Cdd:cd02660    233 KTSR-KIDTYVQFPLELNMTPYTSS--------------------SIGDTQDSNSLDPD--------------------- 270

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  479 gleknsLIYELFSVMVHSGSAAGGHYYACIKsFSDEQWYSFNDQHVSRITQEDIKKthggssgsrgyyssafassTNAYM 558
Cdd:cd02660    271 ------YTYDLFAVVVHKGTLDTGHYTAYCR-QGDGQWFKFDDAMITRVSEEEVLK-------------------SQAYL 324


                   ...
gi 1722208472  559 LIY 561
Cdd:cd02660    325 LFY 327
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 189-562 2.55e-26

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


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 110.17  E-value: 2.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  189 GLVNQAMTCYLNSLLQTLFMTPEFRNALykwefeesEEDPVTsipyqlqrlfvLLQTSKKRAIETTDvtrsfgwdsseaW 268
Cdd:cd02667      1 GLSNLGNTCFFNAVMQNLSQTPALRELL--------SETPKE-----------LFSQVCRKAPQFKG------------Y 49

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  269 QQHDVQELCRVMFDALEQkwkqteqadLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQAfaSVEEALH 348
Cdd:cd02667     50 QQQDSHELLRYLLDGLRT---------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIKSEC--SIESCLK 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  349 AFIQPEILDGPNQYFCERCKKkcdARKGLRFLHFPYLLTLQLKRFDFDYTTMHRiKLNDRMTFPEELDMSTFIDVedeks 428
Cdd:cd02667    119 QFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQPRSANLR-KVSRHVSFPEILDLAPFCDP----- 189

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  429 pqtesctdsgaenegSCHSDQmsndfsnddgvdegicletnsgtekisksglEKNSLIYELFSVMVHSGSAAGGHYYACI 508
Cdd:cd02667    190 ---------------KCNSSE-------------------------------DKSSVLYRLYGVVEHSGTMRSGHYVAYV 223

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1722208472  509 KS---------------FSDE------QWYSFNDQHVSRITQEDIkkthggssgsrgyyssafaSSTNAYMLIYR 562
Cdd:cd02667    224 KVrppqqrlsdltkskpAADEagpgsgQWYYISDSDVREVSLEEV-------------------LKSEAYLLFYE 279
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 189-561 1.83e-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 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: 99.31  E-value: 1.83e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  189 GLVNQAMTCYLNSLLQTLFmtpeFRNALYkwefeeSEEDPVTSIPYQLQRLFVLlqtSKKRAIETTDVTRSFgWDSSeaw 268
Cdd:cd02663      1 GLENFGNTCYCNSVLQALY----FENLLT------CLKDLFESISEQKKRTGVI---SPKKFITRLKRENEL-FDNY--- 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  269 QQHDVQE----LCRVMFDALEQKWKQTE-------------QADLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVI 331
Cdd:cd02663     64 MHQDAHEflnfLLNEIAEILDAERKAEKanrklnnnnnaepQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDV 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  332 RPYgssqafASVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTF 411
Cdd:cd02663    144 EQN------TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVF 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  412 PEELDMStfidvedekspqteSCTDsgaenegschsdqmsnDFSNDDgvdegicletnsgtekisksgleknsLIYELFS 491
Cdd:cd02663    218 PLELRLF--------------NTTD----------------DAENPD--------------------------RLYELVA 241

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1722208472  492 VMVHSGSAAG-GHYYACIKsfSDEQWYSFNDQHVSRITQEDIKKTHGGSsgsrgyyssafASSTNAYMLIY 561
Cdd:cd02663    242 VVVHIGGGPNhGHYVSIVK--SHGGWLLFDDETVEKIDENAVEEFFGDS-----------PNQATAYVLFY 299
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 187-531 3.18e-20

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: 93.42  E-value: 3.18e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  187 YVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDPVTSIPYQLQRLF--VLLQTSKKRAIETT-DVTRSFgwd 263
Cdd:cd02671     24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQSSFLLNPEKYndELANQAPRRLLNALrEVNPMY--- 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  264 ssEAWQQHDVQELCRVMFDALEqkwkqteqaDLINELYQGKLKDYVRCLECGYEGWRIDTYLDIPLVIRPYGSSQAFASV 343
Cdd:cd02671    101 --EGYLQHDAQEVLQCILGNIQ---------ELVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESELSKSEESS 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  344 E-------------EALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRI----KLN 406
Cdd:cd02671    170 EispdpktemktlkWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCYgglsKVN 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  407 DRMTFPEELdmstfidvedekspqtesctdsgaenegSCH--SDQMSNDfsnddgvdegicletnsgtekisksglekns 484
Cdd:cd02671    250 TPLLTPLKL----------------------------SLEewSTKPKND------------------------------- 270

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1722208472  485 lIYELFSVMVHSG-SAAGGHYYACIKsfsdeqWYSFNDQHVSRITQED 531
Cdd:cd02671    271 -VYRLFAVVMHSGaTISSGHYTAYVR------WLLFDDSEVKVTEEKD 311
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 189-536 1.65e-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 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: 90.85  E-value: 1.65e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  189 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKWE--FEESEEDPVTSIPYQLQRL---FVLLQTSKKRAIETTDVT------ 257
Cdd:cd02658      1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLEnkFPSDVVDPANDLNCQLIKLadgLLSGRYSKPASLKSENDPyqvgik 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  258 -RSF----GWDSSE--AWQQHDVQELCRVMFDALEQKWKQTEQADlINELYQGKLKDYVRCLECGYEGW--RIDTYLDIP 328
Cdd:cd02658     81 pSMFkaliGKGHPEfsTMRQQDALEFLLHLIDKLDRESFKNLGLN-PNDLFKFMIEDRLECLSCKKVKYtsELSEILSLP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  329 LVIRPYGSSQAFASV------EEALHAFIQPEildgPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDF--DYTtm 400
Cdd:cd02658    160 VPKDEATEKEEGELVyepvplEDCLKAYFAPE----TIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLleNWV-- 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  401 hriklndrmtfPEELDMStfIDVEDEKSPQTesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksgl 480
Cdd:cd02658    234 -----------PKKLDVP--IDVPEELGPGK------------------------------------------------- 251

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1722208472  481 eknsliYELFSVMVHSG-SAAGGHYYACIKSFSDE--QWYSFNDQHVSRITQEDIKKTH 536
Cdd:cd02658    252 ------YELIAFISHKGtSVHSGHYVAHIKKEIDGegKWVLFNDEKVVASQDPPEMKKL 304
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 189-535 1.23e-16

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: 82.38  E-value: 1.23e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  189 GLVNQAMTCYLNSLLQTLFMTPEFRNAL--YKWEFEESEE--DPVTSipyQLQRLFVLLQTSKKRA--IETTDVTR---- 258
Cdd:cd02657      1 GLTNLGNTCYLNSTLQCLRSVPELRDALknYNPARRGANQssDNLTN---ALRDLFDTMDKKQEPVppIEFLQLLRmafp 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  259 SFGWDSSEA-WQQHDVQELCRVMFDALEQKWK-QTEQADLINELYQGKLKDYVRCLEcgyegwridtyldIPLVIRPYGS 336
Cdd:cd02657     78 QFAEKQNQGgYAQQDAEECWSQLLSVLSQKLPgAGSKGSFIDQLFGIELETKMKCTE-------------SPDEEEVSTE 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  337 SQAFASveeaLHAFIQPEI---LDGPNQYFCERCKKKCDAR-------KGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLN 406
Cdd:cd02657    145 SEYKLQ----CHISITTEVnylQDGLKKGLEEEIEKHSPTLgrdaiytKTSRISRLPKYLTVQFVRFFWKRDIQKKAKIL 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  407 DRMTFPEELDMSTFidvedekspqtesCTDSGaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknslI 486
Cdd:cd02657    221 RKVKFPFELDLYEL-------------CTPSG-----------------------------------------------Y 240

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1722208472  487 YELFSVMVHSG-SAAGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKT 535
Cdd:cd02657    241 YELVAVITHQGrSADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKL 290
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 189-561 7.28e-16

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: 78.56  E-value: 7.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  189 GLVNQAMTCYLNSLLQTLFMTPEFRnalykwEFeeseedpvtsipyqLQRLFvllqtskkraiettdvtrsfgwdsseaw 268
Cdd:cd02662      1 GLVNLGNTCFMNSVLQALASLPSLI------EY--------------LEEFL---------------------------- 32

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  269 QQHDVQELCRVMFDALEQKWKQteqadlineLYQGKLKDYVRCLECGY-EGWRIDTYLDIPLVIrPYGSSQAFASVEEAL 347
Cdd:cd02662     33 EQQDAHELFQVLLETLEQLLKF---------PFDGLLASRIVCLQCGEsSKVRYESFTMLSLPV-PNQSSGSGTTLEHCL 102

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  348 HAFIQPEILDGpnqYFCERCKKKcdarkglrFLHFPYLLTLQLKRFDFDYTTMHRiKLNDRMTFPEELdmstfidvedek 427
Cdd:cd02662    103 DDFLSTEIIDD---YKCDRCQTV--------IVRLPQILCIHLSRSVFDGRGTST-KNSCKVSFPERL------------ 158

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  428 spqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglekNSLIYELFSVMVHSGSAAGGHY--- 504
Cdd:cd02662    159 -------------------------------------------------------PKVLYRLRAVVVHYGSHSSGHYvcy 183

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1722208472  505 --------YACIKSFS---------DEQWYSFNDQHVSRITQEDIkkthggssgsrgyyssafASSTNAYMLIY 561
Cdd:cd02662    184 rrkplfskDKEPGSFVrmregpsstSHPWWRISDTTVKEVSESEV------------------LEQKSAYMLFY 239
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 188-532 4.90e-14

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: 75.22  E-value: 4.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  188 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYkwEFEESEEDPVTSIP----------------------YQLQRLFVLLQT 245
Cdd:cd02666      2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVL--NFDESKAELASDYPterriggrevsrselqrsnqfvYELRSLFNDLIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  246 SKKRAIETTDVTrsfgwdSSEAWQQHDVQELCRVMFDALE-------------QKWKQTEQADLINELYQGKLK-DYVRC 311
Cdd:cd02666     80 SNTRSVTPSKEL------AYLALRQQDVTECIDNVLFQLEvalepisnafagpDTEDDKEQSDLIKRLFSGKTKqQLVPE 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  312 LECGYEGWRIDTYLDIPLVIrPYGSSQAFASVEEalHAfiqPEILDGPNQYFCERCKKKcdarkglrflhFPYLLTLQLK 391
Cdd:cd02666    154 SMGNQPSVRTKTERFLSLLV-DVGKKGREIVVLL--EP---KDLYDALDRYFDYDSLTK-----------LPQRSQVQAQ 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  392 rfdfdyttmhriklNDRMTFPEELDMSTFidvEDEKSPQTESCTDSGAENEGSCHSDQMSNdfsnddgvdegiclETNSG 471
Cdd:cd02666    217 --------------LAQPLQRELISMDRY---ELPSSIDDIDELIREAIQSESSLVRQAQN--------------ELAEL 265

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1722208472  472 TEKISKSGLEKNSLIYELFSVMVHSGSAAGGHYYACIKSFSDEQWYSFNDQHVSRITQEDI 532
Cdd:cd02666    266 KHEIEKQFDDLKSYGYRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEV 326
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
342-564 3.23e-13

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 74.53  E-value: 3.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  342 SVEEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTmhRIKLNDRMTFP-EELDMSTF 420
Cdd:COG5560    676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPiDDLDLSGV 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  421 IdvedekspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekiskSGLEKNSLIYELFSVMVHSGSAA 500
Cdd:COG5560    754 E--------------------------------------------------------YMVDDPRLIYDLYAVDNHYGGLS 777

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1722208472  501 GGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKTHggssgsrgyyssafasstnAYMLIYRLK 564
Cdd:COG5560    778 GGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSS-------------------AYVLFYRRK 822
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
189-532 2.34e-10

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 62.90  E-value: 2.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  189 GLVNQAMTCYLNSLLQTL-FMTPEFRNALYKWEFE--------ESEEDPVTsipyQLQRLFVLlqtskkRAIETTDVTRs 259
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKElkvlknviRKPEPDLN----QEEALKLF------TALWSSKEHK- 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  260 FGWDSSEAwQQHDVQELCRVMFDALEqkwkqTEQADLINELYQGKLKDYVRclecgyegwriDTYLDIPLVI--RPYGSS 337
Cdd:COG5533     70 VGWIPPMG-SQEDAHELLGKLLDELK-----LDLVNSFTIRIFKTTKDKKK-----------TSTGDWFDIIieLPDQTW 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  338 -QAFASVEEALHAFiQPEILDGPNQYFCERCKKKCDARKG--LRFLHFPYLLTLQLKRFDFDyttmhriklndrmtfpee 414
Cdd:COG5533    133 vNNLKTLQEFIDNM-EELVDDETGVKAKENEELEVQAKQEyeVSFVKLPKILTIQLKRFANL------------------ 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  415 ldmSTFIDVEDEkspqtesctdsgaenegschsdqmsndfsnddgVDEGICLetnsgTEKISKSGLEKNSLIYELFSVMV 494
Cdd:COG5533    194 ---GGNQKIDTE---------------------------------VDEKFEL-----PVKHDQILNIVKETYYDLVGFVL 232

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1722208472  495 HSGSAAGGHYYACIKsfSDEQWYSFNDQHVSRITQEDI 532
Cdd:COG5533    233 HQGSLEGGHYIAYVK--KGGKWEKANDSDVTPVSEEEA 268
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
188-521 2.37e-08

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 57.28  E-value: 2.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  188 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDpvTSIPYQLQRLFVLLQTSKKRAIETTDVTRSFG------ 261
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATECLKE--HCLLCELGFLFDMLEKAKGKNCQASNFLRALSsipeas 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  262 ----WDSSEAWQQHD-----VQELCRVMFDALEQKWKQTEQ-----ADLINELYQGKLKDYVRCLECGYEGWR----IDT 323
Cdd:pfam13423   79 alglLDEDRETNSAIslsslIQSFNRFLLDQLSSEENSTPPnpspaESPLEQLFGIDAETTIRCSNCGHESVResstHVL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  324 YLDIPLVIRPYGSSQAFASVEEALHAFIQPEILdgpNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYttmhri 403
Cdd:pfam13423  159 DLIYPRKPSSNNKKPPNQTFSSILKSSLERETT---TKAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEW------ 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  404 kLNDRMT---FPEELDMSTFIDvedekspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekiskSGL 480
Cdd:pfam13423  230 -RQLWKTpgwLPPEIGLTLSDD-------------------------------------------------------LQG 253

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1722208472  481 EKNSLIYELFSVMVH-SGSAAGGHYYACIKSFSDE-------QWYSFND 521
Cdd:pfam13423  254 DNEIVKYELRGVVVHiGDSGTSGHLVSFVKVADSEledptesQWYLFND 302
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 487-561 1.78e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 50.63  E-value: 1.78e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1722208472  487 YELFSVMVHSGSAAGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKthggssgsrgyysSAFASSTN--AYMLIY 561
Cdd:cd02665    164 YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVER-------------DSFGGGRNpsAYCLMY 227
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
184-331 2.83e-06

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 51.81  E-value: 2.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  184 ETGYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEES--EEDP------VTSIPYQL-QRLFvllqTSKKRAIETT 254
Cdd:COG5560    262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESinEENPlgmhgsVASAYADLiKQLY----DGNLHAFTPS 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  255 DVTRSFGWDSSE--AWQQHDVQELCRVMFDALE------QKWKQTEQADL--------------------------INEL 300
Cdd:COG5560    338 GFKKTIGSFNEEfsGYDQQDSQEFIAFLLDGLHedlnriIKKPYTSKPDLspgddvvvkkkakecwwehlkrndsiITDL 417

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1722208472  301 YQGKLKDYVRCLECGYEGWRIDTYLDIPLVI 331
Cdd:COG5560    418 FQGMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 834-1025 2.87e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 42.20  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  834 VSYSKRTAYQKAGGDSGNVDDDC--ERVKGPvgslKSVEAILEESTEKLKSLSLQQQQDGDNGDSSKSTETSDF--ENIE 909
Cdd:NF033609   521 MSWDNEVAFNNGSGSGDGIDKPVvpEQPDEP----GEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSgsDSAS 596

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722208472  910 SPLNERDSSASVDNRELEQHIQTSDPENFQ-SEERSDSDVNNDRSTSSVDSDILSSSHSSDTLCNADNAQiplanglDSH 988
Cdd:NF033609   597 DSDSASDSDSASDSDSASDSDSASDSDSASdSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDS-------DSD 669

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1722208472  989 SITSSRRTKANEGKKETWDTAEEDSGTDSEYDESGKS 1025
Cdd:NF033609   670 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 706
 
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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