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Conserved domains on  [gi|1722213020|ref|NP_001359027|]
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ubiquitin carboxyl-terminal hydrolase 47 isoform j [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 ...
 166-496 2.28e-126

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: 393.16  E-value: 2.28e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  166 GYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWeFEESEEDPVTSIPYQLQRLFVLLQTSKKRAIET--TDVTRSFGWD 243
Cdd:cd02659      1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-PPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTelTDKTRSFGWD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  244 SSEAWQQHDVQELCRVMFDALEQKWKQTEQ--------------------------------------------EEALHA 279
Cdd:cd02659     80 SLNTFEQHDVQEFFRVLFDKLEEKLKGTGQegliknlfggklvnyiickecphesereeyfldlqvavkgkknlEESLDA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  280 FIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSTFIDVEDEKSP 359
Cdd:cd02659    160 YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  360 QTESCTDSGaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknSLIYELFSVMVHSGSAAGGHYYACIK 439
Cdd:cd02659    240 GDSEKKDSE---------------------------------------------SYIYELHGVLVHSGDAHGGHYYSYIK 274

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  440 SFSDEQWYSFNDQHVSRITQEDIKKTH---GGSSGSRGYYSSAFASSTNAYMLIYRLKDP 496
Cdd:cd02659    275 DRDDGKWYKFNDDVVTPFDPNDAEEECfggEETQKTYDSGPRAFKRTTNAYMLFYERKSP 334
USP47_C super family cl45120
Ubiquitin carboxyl-terminal hydrolase 47 C-terminal; This is the C-terminal domain of ...
 1054-1293 2.50e-101

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: 322.09  E-value: 2.50e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020 1054 RVKVYQLLVNEQEPCKFLLDAVFAKGMTVRQSKEELIPQLREQ-CGLELSIDRFRLRKKTWKNPGTVFLDYHIYEeDINI 1132
Cdd:pfam19718    1 RVKLYQLQVNNTEFCKYMMESIVAKGTPVREFKKQIIEEAKVQgIDCVLELDKMRLRKKTWVYPGTVYLDHQVID-DIQI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020 1133 SSNWEVFLEVLDGVEKMKSMSQLAVLSRRWKPSEMKLDPFQEVVLESSSVDELREKLSEISGIPLDDIEFAKGRGTFPCD 1212
Cdd:pfam19718   80 YPNWEMYVEPLKGPEKKKHTTQLQVYVRRWHPSQCSVDPFEEIILDNRTPKELKEKLSELSGVPVEYIYIAKGKGSFPCE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020 1213 ISVLDIHQDLDWNPKVSTLNVWPLYICDDGAVIFYRDKTEELMELTDEQRNELMKKESSRLQKTGHRVTYSPRKEKALKI 1292
Cdd:pfam19718  160 ISVLDIENELEWNSITSSLSSYPLYLYEDGHVIYYKDNRETMKELTDEERSEIQQKENARLTKISERSSYSPRKERALKI 239


                   .
gi 1722213020 1293 Y 1293
Cdd:pfam19718  240 Y 240
MSCRAMM_ClfA super family cl41352
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 764-955 4.52e-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: 41.43  E-value: 4.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  764 VSYSKRTAYQKAGGDSGNVDDDC--ERVKGPvgslKSVEAILEESTEKLKSLSLQQQQDGDNGDSSKSTETSDF--ENIE 839
Cdd:NF033609   521 MSWDNEVAFNNGSGSGDGIDKPVvpEQPDEP----GEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSgsDSAS 596

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  840 SPLNERDSSASVDNRELEQHIQTSDPENFQ-SEERSDSDVNNDRSTSSVDSDILSSSHSSDTLCNADNAQiplanglDSH 918
Cdd:NF033609   597 DSDSASDSDSASDSDSASDSDSASDSDSASdSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDS-------DSD 669

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1722213020  919 SITSSRRTKANEGKKETWDTAEEDSGTDSEYDESGKS 955
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 ...
 166-496 2.28e-126

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: 393.16  E-value: 2.28e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  166 GYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWeFEESEEDPVTSIPYQLQRLFVLLQTSKKRAIET--TDVTRSFGWD 243
Cdd:cd02659      1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-PPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTelTDKTRSFGWD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  244 SSEAWQQHDVQELCRVMFDALEQKWKQTEQ--------------------------------------------EEALHA 279
Cdd:cd02659     80 SLNTFEQHDVQEFFRVLFDKLEEKLKGTGQegliknlfggklvnyiickecphesereeyfldlqvavkgkknlEESLDA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  280 FIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSTFIDVEDEKSP 359
Cdd:cd02659    160 YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  360 QTESCTDSGaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknSLIYELFSVMVHSGSAAGGHYYACIK 439
Cdd:cd02659    240 GDSEKKDSE---------------------------------------------SYIYELHGVLVHSGDAHGGHYYSYIK 274

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  440 SFSDEQWYSFNDQHVSRITQEDIKKTH---GGSSGSRGYYSSAFASSTNAYMLIYRLKDP 496
Cdd:cd02659    275 DRDDGKWYKFNDDVVTPFDPNDAEEECfggEETQKTYDSGPRAFKRTTNAYMLFYERKSP 334
USP47_C pfam19718
Ubiquitin carboxyl-terminal hydrolase 47 C-terminal; This is the C-terminal domain of ...
 1054-1293 2.50e-101

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: 322.09  E-value: 2.50e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020 1054 RVKVYQLLVNEQEPCKFLLDAVFAKGMTVRQSKEELIPQLREQ-CGLELSIDRFRLRKKTWKNPGTVFLDYHIYEeDINI 1132
Cdd:pfam19718    1 RVKLYQLQVNNTEFCKYMMESIVAKGTPVREFKKQIIEEAKVQgIDCVLELDKMRLRKKTWVYPGTVYLDHQVID-DIQI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020 1133 SSNWEVFLEVLDGVEKMKSMSQLAVLSRRWKPSEMKLDPFQEVVLESSSVDELREKLSEISGIPLDDIEFAKGRGTFPCD 1212
Cdd:pfam19718   80 YPNWEMYVEPLKGPEKKKHTTQLQVYVRRWHPSQCSVDPFEEIILDNRTPKELKEKLSELSGVPVEYIYIAKGKGSFPCE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020 1213 ISVLDIHQDLDWNPKVSTLNVWPLYICDDGAVIFYRDKTEELMELTDEQRNELMKKESSRLQKTGHRVTYSPRKEKALKI 1292
Cdd:pfam19718  160 ISVLDIENELEWNSITSSLSSYPLYLYEDGHVIYYKDNRETMKELTDEERSEIQQKENARLTKISERSSYSPRKERALKI 239


                   .
gi 1722213020 1293 Y 1293
Cdd:pfam19718  240 Y 240
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 162-542 9.71e-63

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 233.99  E-value: 9.71e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  162 KSETGYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEEseEDPVTSIPYQLQRLFVLLQTSKKrAIETTDVTRSFG 241
Cdd:COG5077    188 KKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDH--PRGRDSVALALQRLFYNLQTGEE-PVDTTELTRSFG 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  242 WDSSEAWQQHDVQELCRVMFDALEQKWKQTEQEEALH------------------------------------------- 278
Cdd:COG5077    265 WDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNgifvgkmksyikcvnvnyesarvedfwdiqlnvkgmknlqesf 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  279 -AFIQPEILDGPNQYFCERCKKKcDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSTFIDVEDEK 357
Cdd:COG5077    345 rRYIQVETLDGDNRYNAEKHGLQ-DAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDRDADK 423

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  358 SpqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglEKNSLIYELFSVMVHSGSAAGGHYYAC 437
Cdd:COG5077    424 S----------------------------------------------------ENSDAVYVLYGVLVHSGDLHEGHYYAL 451

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  438 IKSFSDEQWYSFNDQHVSRITQEDIKKTH---GGSSGSRGYYSSAFASSTNAYMLIYRLKDPARN-AKFLEVDEYPEHIK 513
Cdd:COG5077    452 LKPEKDGRWYKFDDTRVTRATEKEVLEENfggDHPYKDKIRDHSGIKRFMSAYMLVYLRKSMLDDlLNPVAAVDIPPHVE 531

                          410       420
                   ....*....|....*....|....*....
gi 1722213020  514 NLVQKERELEEQEKRQREIERNTCKIKLF 542
Cdd:COG5077    532 EVLSEEIDKTEVRCKEIDEIHLYRGVRLY 560
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
168-491 1.16e-57

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 201.90  E-value: 1.16e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  168 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWE--FEESEEDPVTSIPYQLQRLF-VLLQTSKKRAIETTDVTRSFGWDS 244
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISplSEDSRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSLGKLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  245 SE--AWQQHDVQELCRVMFDALEQK--------------------WKQTEQ----------------------------- 273
Cdd:pfam00443   81 PDfsGYKQQDAQEFLLFLLDGLHEDlngnhsteneslitdlfrgqLKSRLKclscgevsetfepfsdlslpipgdsaelk 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  274 ----EEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTmhRIKLNDRMTFPEELDMST 349
Cdd:pfam00443  161 taslQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLELDLSR 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  350 FIDVEDEKspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksgLEKNSLIYELFSVMVHSGSA 429
Cdd:pfam00443  239 YLAEELKP----------------------------------------------------KTNNLQDYRLVAVVVHSGSL 266

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1722213020  430 AGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKTHggssgsrgyyssafasstNAYMLIY 491
Cdd:pfam00443  267 SSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLSS------------------SAYILFY 310
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 764-955 4.52e-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: 41.43  E-value: 4.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  764 VSYSKRTAYQKAGGDSGNVDDDC--ERVKGPvgslKSVEAILEESTEKLKSLSLQQQQDGDNGDSSKSTETSDF--ENIE 839
Cdd:NF033609   521 MSWDNEVAFNNGSGSGDGIDKPVvpEQPDEP----GEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSgsDSAS 596

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  840 SPLNERDSSASVDNRELEQHIQTSDPENFQ-SEERSDSDVNNDRSTSSVDSDILSSSHSSDTLCNADNAQiplanglDSH 918
Cdd:NF033609   597 DSDSASDSDSASDSDSASDSDSASDSDSASdSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDS-------DSD 669

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1722213020  919 SITSSRRTKANEGKKETWDTAEEDSGTDSEYDESGKS 955
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 ...
 166-496 2.28e-126

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: 393.16  E-value: 2.28e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  166 GYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWeFEESEEDPVTSIPYQLQRLFVLLQTSKKRAIET--TDVTRSFGWD 243
Cdd:cd02659      1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-PPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTelTDKTRSFGWD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  244 SSEAWQQHDVQELCRVMFDALEQKWKQTEQ--------------------------------------------EEALHA 279
Cdd:cd02659     80 SLNTFEQHDVQEFFRVLFDKLEEKLKGTGQegliknlfggklvnyiickecphesereeyfldlqvavkgkknlEESLDA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  280 FIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSTFIDVEDEKSP 359
Cdd:cd02659    160 YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  360 QTESCTDSGaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknSLIYELFSVMVHSGSAAGGHYYACIK 439
Cdd:cd02659    240 GDSEKKDSE---------------------------------------------SYIYELHGVLVHSGDAHGGHYYSYIK 274

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  440 SFSDEQWYSFNDQHVSRITQEDIKKTH---GGSSGSRGYYSSAFASSTNAYMLIYRLKDP 496
Cdd:cd02659    275 DRDDGKWYKFNDDVVTPFDPNDAEEECfggEETQKTYDSGPRAFKRTTNAYMLFYERKSP 334
USP47_C pfam19718
Ubiquitin carboxyl-terminal hydrolase 47 C-terminal; This is the C-terminal domain of ...
 1054-1293 2.50e-101

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: 322.09  E-value: 2.50e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020 1054 RVKVYQLLVNEQEPCKFLLDAVFAKGMTVRQSKEELIPQLREQ-CGLELSIDRFRLRKKTWKNPGTVFLDYHIYEeDINI 1132
Cdd:pfam19718    1 RVKLYQLQVNNTEFCKYMMESIVAKGTPVREFKKQIIEEAKVQgIDCVLELDKMRLRKKTWVYPGTVYLDHQVID-DIQI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020 1133 SSNWEVFLEVLDGVEKMKSMSQLAVLSRRWKPSEMKLDPFQEVVLESSSVDELREKLSEISGIPLDDIEFAKGRGTFPCD 1212
Cdd:pfam19718   80 YPNWEMYVEPLKGPEKKKHTTQLQVYVRRWHPSQCSVDPFEEIILDNRTPKELKEKLSELSGVPVEYIYIAKGKGSFPCE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020 1213 ISVLDIHQDLDWNPKVSTLNVWPLYICDDGAVIFYRDKTEELMELTDEQRNELMKKESSRLQKTGHRVTYSPRKEKALKI 1292
Cdd:pfam19718  160 ISVLDIENELEWNSITSSLSSYPLYLYEDGHVIYYKDNRETMKELTDEERSEIQQKENARLTKISERSSYSPRKERALKI 239


                   .
gi 1722213020 1293 Y 1293
Cdd:pfam19718  240 Y 240
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 162-542 9.71e-63

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 233.99  E-value: 9.71e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  162 KSETGYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEEseEDPVTSIPYQLQRLFVLLQTSKKrAIETTDVTRSFG 241
Cdd:COG5077    188 KKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDH--PRGRDSVALALQRLFYNLQTGEE-PVDTTELTRSFG 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  242 WDSSEAWQQHDVQELCRVMFDALEQKWKQTEQEEALH------------------------------------------- 278
Cdd:COG5077    265 WDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNgifvgkmksyikcvnvnyesarvedfwdiqlnvkgmknlqesf 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  279 -AFIQPEILDGPNQYFCERCKKKcDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSTFIDVEDEK 357
Cdd:COG5077    345 rRYIQVETLDGDNRYNAEKHGLQ-DAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPFLDRDADK 423

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  358 SpqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglEKNSLIYELFSVMVHSGSAAGGHYYAC 437
Cdd:COG5077    424 S----------------------------------------------------ENSDAVYVLYGVLVHSGDLHEGHYYAL 451

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  438 IKSFSDEQWYSFNDQHVSRITQEDIKKTH---GGSSGSRGYYSSAFASSTNAYMLIYRLKDPARN-AKFLEVDEYPEHIK 513
Cdd:COG5077    452 LKPEKDGRWYKFDDTRVTRATEKEVLEENfggDHPYKDKIRDHSGIKRFMSAYMLVYLRKSMLDDlLNPVAAVDIPPHVE 531

                          410       420
                   ....*....|....*....|....*....
gi 1722213020  514 NLVQKERELEEQEKRQREIERNTCKIKLF 542
Cdd:COG5077    532 EVLSEEIDKTEVRCKEIDEIHLYRGVRLY 560
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
168-491 1.16e-57

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 201.90  E-value: 1.16e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  168 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWE--FEESEEDPVTSIPYQLQRLF-VLLQTSKKRAIETTDVTRSFGWDS 244
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISplSEDSRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKKSLGKLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  245 SE--AWQQHDVQELCRVMFDALEQK--------------------WKQTEQ----------------------------- 273
Cdd:pfam00443   81 PDfsGYKQQDAQEFLLFLLDGLHEDlngnhsteneslitdlfrgqLKSRLKclscgevsetfepfsdlslpipgdsaelk 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  274 ----EEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTmhRIKLNDRMTFPEELDMST 349
Cdd:pfam00443  161 taslQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRST--WEKLNTEVEFPLELDLSR 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  350 FIDVEDEKspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksgLEKNSLIYELFSVMVHSGSA 429
Cdd:pfam00443  239 YLAEELKP----------------------------------------------------KTNNLQDYRLVAVVVHSGSL 266

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1722213020  430 AGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKTHggssgsrgyyssafasstNAYMLIY 491
Cdd:pfam00443  267 SSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLSS------------------SAYILFY 310
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 169-492 6.63e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 174.15  E-value: 6.63e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  169 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDPV---------TSIPYQLQRLFVLLQTSKKRAIETTDVTRS 239
Cdd:cd02668      1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNmppdkphepQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  240 FGWDSSeawQQHDVQELCRVMFDALEQKWKQTEQ---------------------------------------------- 273
Cdd:cd02668     81 LGLDTG---QQQDAQEFSKLFLSLLEAKLSKSKNpdlknivqdlfrgeysyvtqcskcgresslpskfyelelqlkghkt 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  274 -EEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSTFID 352
Cdd:cd02668    158 lEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYLA 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  353 VEDEkspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksglekNSLIYELFSVMVHSG-SAAG 431
Cdd:cd02668    238 ESDE--------------------------------------------------------GSYVYELSGVLIHQGvSAYS 261

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1722213020  432 GHYYACIKSFSDEQWYSFNDQHVSRITQEDIK--KTHGGSSGSRGYYSSAFASSTNAYMLIYR 492
Cdd:cd02668    262 GHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKlgNSEDPAKPRKSEIKKGTHSSRTAYMLVYK 324
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 169-492 6.27e-46

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: 166.12  E-value: 6.27e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  169 GLVNQAMTCYLNSLLQTLFMTPE-----FRNALYKWEFEESEEDPVTSIPYQ----LQRLFVLLQTSKKRAIETTDVTRS 239
Cdd:cd02257      1 GLNNLGNTCYLNSVLQALFSEQQdahefLLFLLDKLHEELKKSSKRTSDSSSlkslIHDLFGGKLESTIVCLECGHESVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  240 FgwdSSEAWQQHDVQelcrvmfdalEQKWKQTEQEEALHAFIQPEILDGPNQYFCErCKKKCDARKGLRFLHFPYLLTLQ 319
Cdd:cd02257     81 T---EPELFLSLPLP----------VKGLPQVSLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIH 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  320 LKRFDFDYtTMHRIKLNDRMTFPEELDMSTFIDVEDEKSPQtesctdsgaenegschsdqmsndfsnddgvdegicletn 399
Cdd:cd02257    147 LKRFSFNE-DGTKEKLNTKVSFPLELDLSPYLSEGEKDSDS--------------------------------------- 186

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  400 sgtekisksglEKNSLIYELFSVMVHSGSAA-GGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKthggssgsrgyyss 478
Cdd:cd02257    187 -----------DNGSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLE-------------- 241

                          330
                   ....*....|....
gi 1722213020  479 AFASSTNAYMLIYR 492
Cdd:cd02257    242 FGSLSSSAYILFYE 255
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 169-492 2.02e-36

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: 141.09  E-value: 2.02e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  169 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKweFEESEEDPVTSIPYQLQRLFVLLQTSKKRAIETTDvtrSFGWDSSEAW 248
Cdd:cd02664      1 GLINLGNTCYMNSVLQALFMAKDFRRQVLS--LNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPD---YFLEASRPPW 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  249 ----QQHDVQELCRVMFDALE---QKW---------------KQTEQEEA--------------LHAFIQPEILDGPNQY 292
Cdd:cd02664     76 ftpgSQQDCSEYLRYLLDRLHtliEKMfggklsttirclncnSTSARTERfrdldlsfpsvqdlLNYFLSPEKLTGDNQY 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  293 FCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMStfidVEDEkspqTESCTDSGAENE 372
Cdd:cd02664    156 YCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLP----VRVE----SKSSESPLEKKE 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  373 GschsdqmsndfsnDDGVDEGICLETnsgtekisksgleknsLIYELFSVMVHSG-SAAGGHYY--------------AC 437
Cdd:cd02664    228 E-------------ESGDDGELVTRQ----------------VHYRLYAVVVHSGySSESGHYFtyardqtdadstgqEC 278

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1722213020  438 IKSFSDEQ------WYSFNDQHVSRITQEDIKKThggssgsrgyysSAFASSTNAYMLIYR 492
Cdd:cd02664    279 PEPKDAEEndesknWYLFNDSRVTFSSFESVQNV------------TSRFPKDTPYILFYE 327
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 169-491 2.56e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 131.24  E-value: 2.56e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  169 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDP----VTSIPYQLQRlfVLLQTSKKRAI-----ETTDVTRS 239
Cdd:cd02661      3 GLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEgfcmMCALEAHVER--ALASSGPGSAPrifssNLKQISKH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  240 FGWDSseawqQHDVQELCRVMFDALEQ----KWKQTEQ------------------------------------------ 273
Cdd:cd02661     81 FRIGR-----QEDAHEFLRYLLDAMQKacldRFKKLKAvdpssqettlvqqifggylrsqvkclnckhvsntydpfldls 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  274 ---------EEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYttMHriKLNDRMTFPEE 344
Cdd:cd02661    156 ldikgadslEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR--GG--KINKQISFPET 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  345 LDMSTFidvedekspqtesctdsgaenegschsdqMSNdfSNDdgvdegicletnsgtekisksglekNSLIYELFSVMV 424
Cdd:cd02661    232 LDLSPY-----------------------------MSQ--PND-------------------------GPLKYKLYAVLV 255

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1722213020  425 HSG-SAAGGHYYACIKSfSDEQWYSFNDQHVSRITQEDIkkthggssgsrgyyssafaSSTNAYMLIY 491
Cdd:cd02661    256 HSGfSPHSGHYYCYVKS-SNGKWYNMDDSKVSPVSIETV-------------------LSQKAYILFY 303
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 274-492 2.71e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 96.97  E-value: 2.71e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  274 EEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMhrIKLNDRMTFP-EELDMSTFID 352
Cdd:cd02674     87 EDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSRGST--RKLTTPVTFPlNDLDLTPYVD 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  353 VEDEKSPQTesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknsliYELFSVMVHSGSAAGG 432
Cdd:cd02674    165 TRSFTGPFK-------------------------------------------------------YDLYAVVNHYGSLNGG 189

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  433 HYYACIKSFSDEQWYSFNDQHVSRITQEDIKkthggssgsrgyyssafasSTNAYMLIYR 492
Cdd:cd02674    190 HYTAYCKNNETNDWYKFDDSRVTKVSESSVV-------------------SSSAYILFYE 230
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 274-491 1.73e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 91.28  E-value: 1.73e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  274 EEALHAFIQPEILdGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRiKLNDRMTFPEELDMSTFIDV 353
Cdd:cd02660    179 SDCLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSR-KIDTYVQFPLELNMTPYTSS 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  354 edekspqtesctdsgaenegSCHSDQMSNDFSNDdgvdegicletnsgtekisksgleknsLIYELFSVMVHSGSAAGGH 433
Cdd:cd02660    257 --------------------SIGDTQDSNSLDPD---------------------------YTYDLFAVVVHKGTLDTGH 289

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1722213020  434 YYACIKsFSDEQWYSFNDQHVSRITQEDIKKthggssgsrgyyssafassTNAYMLIY 491
Cdd:cd02660    290 YTAYCR-QGDGQWFKFDDAMITRVSEEEVLK-------------------SQAYLLFY 327
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 169-492 4.78e-17

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: 82.82  E-value: 4.78e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  169 GLVNQAMTCYLNSLLQTLFMTPEFRNALykwefeesEEDPVTsipyqlqrlfvLLQTSKKRAIETTDvtrsfgwdsseaW 248
Cdd:cd02667      1 GLSNLGNTCFFNAVMQNLSQTPALRELL--------SETPKE-----------LFSQVCRKAPQFKG------------Y 49

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  249 QQHDVQELCRVMFDALE-----------------QKWKQTEQ----------------------EEALHAFIQPEILDGP 289
Cdd:cd02667     50 QQQDSHELLRYLLDGLRtfidsifggeltstimcESCGTVSLvyepfldlslprsdeiksecsiESCLKQFTEVEILEGN 129

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  290 NQYFCERCKKkcdARKGLRFLHFPYLLTLQLKRFDFDYTTMHRiKLNDRMTFPEELDMSTFIDVedekspqtesctdsga 369
Cdd:cd02667    130 NKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQPRSANLR-KVSRHVSFPEILDLAPFCDP---------------- 189

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  370 enegSCHSDQmsndfsnddgvdegicletnsgtekisksglEKNSLIYELFSVMVHSGSAAGGHYYACIKS--------- 440
Cdd:cd02667    190 ----KCNSSE-------------------------------DKSSVLYRLYGVVEHSGTMRSGHYVAYVKVrppqqrlsd 234

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1722213020  441 ------FSDE------QWYSFNDQHVSRITQEDIkkthggssgsrgyyssafaSSTNAYMLIYR 492
Cdd:cd02667    235 ltkskpAADEagpgsgQWYYISDSDVREVSLEEV-------------------LKSEAYLLFYE 279
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 169-465 7.04e-17

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: 83.15  E-value: 7.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  169 GLVNQAMTCYLNSLLQTLFMTPEFRNAL--YKWEFEESEE--DPVTSipyQLQRLF-------------VLLQTSKKRAI 231
Cdd:cd02657      1 GLTNLGNTCYLNSTLQCLRSVPELRDALknYNPARRGANQssDNLTN---ALRDLFdtmdkkqepvppiEFLQLLRMAFP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  232 ETTDVTRSFGW---DSSEAWQQ--------HDVQELCRVMFDAL-----EQKWKQTEQEEA------------LHAFIQP 283
Cdd:cd02657     78 QFAEKQNQGGYaqqDAEECWSQllsvlsqkLPGAGSKGSFIDQLfgielETKMKCTESPDEeevsteseyklqCHISITT 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  284 EI---LDGPNQYFCERCKKKCDAR-------KGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMSTFidv 353
Cdd:cd02657    158 EVnylQDGLKKGLEEEIEKHSPTLgrdaiytKTSRISRLPKYLTVQFVRFFWKRDIQKKAKILRKVKFPFELDLYEL--- 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  354 edekspqtesCTDSGaenegschsdqmsndfsnddgvdegicletnsgtekisksgleknslIYELFSVMVHSG-SAAGG 432
Cdd:cd02657    235 ----------CTPSG-----------------------------------------------YYELVAVITHQGrSADSG 257

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1722213020  433 HYYACIKSFSDEQWYSFNDQHVSRITQEDIKKT 465
Cdd:cd02657    258 HYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKL 290
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 168-462 2.30e-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: 75.99  E-value: 2.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  168 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYkwEFEESEEDPVTSIP----------------------YQLQRLFVLLQT 225
Cdd:cd02666      2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVL--NFDESKAELASDYPterriggrevsrselqrsnqfvYELRSLFNDLIH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  226 SKKRAIETTDVTrsfgwdSSEAWQQHDVQELCRVMFDALEqkwKQTEQEEALHAFIQPEilDGPNQ-------YFCERCK 298
Cdd:cd02666     80 SNTRSVTPSKEL------AYLALRQQDVTECIDNVLFQLE---VALEPISNAFAGPDTE--DDKEQsdlikrlFSGKTKQ 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  299 KKCDARKGL---------RFLHFPY-----------------LLTLQLKRFDFDYTTMHRIKL-----NDRMTFPEELDM 347
Cdd:cd02666    149 QLVPESMGNqpsvrtkteRFLSLLVdvgkkgreivvllepkdLYDALDRYFDYDSLTKLPQRSqvqaqLAQPLQRELISM 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  348 STFidvEDEKSPQTESCTDSGAENEGSCHSDQMSNdfsnddgvdegiclETNSGTEKISKSGLEKNSLIYELFSVMVHSG 427
Cdd:cd02666    229 DRY---ELPSSIDDIDELIREAIQSESSLVRQAQN--------------ELAELKHEIEKQFDDLKSYGYRLHAVFIHRG 291

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1722213020  428 SAAGGHYYACIKSFSDEQWYSFNDQHVSRITQEDI 462
Cdd:cd02666    292 EASSGHYWVYIKDFEENVWRKYNDETVTVVPASEV 326
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 277-491 3.21e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 75.04  E-value: 3.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  277 LHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRIKLNDRMTFPEELDMStfidvede 356
Cdd:cd02663    153 LRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLELRLF-------- 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  357 kspqteSCTDsgaenegschsdqmsnDFSNDDgvdegicletnsgtekisksgleknsLIYELFSVMVHSGSAAG-GHYY 435
Cdd:cd02663    225 ------NTTD----------------DAENPD--------------------------RLYELVAVVVHIGGGPNhGHYV 256

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1722213020  436 ACIKsfSDEQWYSFNDQHVSRITQEDIKKTHGGSsgsrgyyssafASSTNAYMLIY 491
Cdd:cd02663    257 SIVK--SHGGWLLFDDETVEKIDENAVEEFFGDS-----------PNQATAYVLFY 299
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
274-494 4.49e-13

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 74.15  E-value: 4.49e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  274 EEALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTmhRIKLNDRMTFP-EELDMSTFId 352
Cdd:COG5560    678 QDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSF--RDKIDDLVEYPiDDLDLSGVE- 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  353 vedekspqtesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekiskSGLEKNSLIYELFSVMVHSGSAAGG 432
Cdd:COG5560    755 -------------------------------------------------------YMVDDPRLIYDLYAVDNHYGGLSGG 779

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1722213020  433 HYYACIKSFSDEQWYSFNDQHVSRITQEDIKKTHggssgsrgyyssafasstnAYMLIYRLK 494
Cdd:COG5560    780 HYTAYARNFANNGWYLFDDSRITEVDPEDSVTSS-------------------AYVLFYRRK 822
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 167-461 2.55e-11

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 66.46  E-value: 2.55e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  167 YVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDPVTSIPYQLQRLF--VLLQTSKKRAIETT-DVTRSFgwd 243
Cdd:cd02671     24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQLQSSFLLNPEKYndELANQAPRRLLNALrEVNPMY--- 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  244 ssEAWQQHDVQELCRVMFDALEQKWKQ------------------TEQEE------------------------------ 275
Cdd:cd02671    101 --EGYLQHDAQEVLQCILGNIQELVEKdfqgqlvlrtrclecetfTERREdfqdisvpvqeselskseesseispdpkte 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  276 ------ALHAFIQPEILDGPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDFDYTTMHRI----KLNDRMTFPEEL 345
Cdd:cd02671    179 mktlkwAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCYgglsKVNTPLLTPLKL 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  346 dmstfidvedekspqtesctdsgaenegSCH--SDQMSNDfsnddgvdegicletnsgtekisksgleknslIYELFSVM 423
Cdd:cd02671    259 ----------------------------SLEewSTKPKND--------------------------------VYRLFAVV 278

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1722213020  424 VHSG-SAAGGHYYACIKsfsdeqWYSFNDQHVSRITQED 461
Cdd:cd02671    279 MHSGaTISSGHYTAYVR------WLLFDDSEVKVTEEKD 311
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 169-466 2.23e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 63.50  E-value: 2.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  169 GLVNQAMTCYLNSLLQTLFMTPEFRNALYKWE--FEESEEDPVTSIPYQLQRL---FVLLQTSKKRAIETTDVT------ 237
Cdd:cd02658      1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLEnkFPSDVVDPANDLNCQLIKLadgLLSGRYSKPASLKSENDPyqvgik 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  238 -RSF----GWDSSE--AWQQHDVQELCRVMFDALEQKWKQTEQ------------------------------------- 273
Cdd:cd02658     81 pSMFkaliGKGHPEfsTMRQQDALEFLLHLIDKLDRESFKNLGlnpndlfkfmiedrleclsckkvkytselseilslpv 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  274 --------------------EEALHAFIQPEildgPNQYFCERCKKKCDARKGLRFLHFPYLLTLQLKRFDF--DYTtmh 331
Cdd:cd02658    161 pkdeatekeegelvyepvplEDCLKAYFAPE----TIEDFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLleNWV--- 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  332 riklndrmtfPEELDMStfIDVEDEKSPQTesctdsgaenegschsdqmsndfsnddgvdegicletnsgtekisksgle 411
Cdd:cd02658    234 ----------PKKLDVP--IDVPEELGPGK-------------------------------------------------- 251

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1722213020  412 knsliYELFSVMVHSG-SAAGGHYYACIKSFSDE--QWYSFNDQHVSRITQEDIKKTH 466
Cdd:cd02658    252 -----YELIAFISHKGtSVHSGHYVAHIKKEIDGegKWVLFNDEKVVASQDPPEMKKL 304
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
169-462 3.31e-09

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 59.43  E-value: 3.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  169 GLVNQAMTCYLNSLLQTL-FMTPEFRNALYKWEFE--------ESEEDPVTsipyQLQRLFVLlqtskkRAIETTDVTRs 239
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKElkvlknviRKPEPDLN----QEEALKLF------TALWSSKEHK- 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  240 FGWDSSEAwQQHDVQELCRVMFDALE-QKWKQTEQ------EEALHAFIQP---------------------EILDGPNQ 291
Cdd:COG5533     70 VGWIPPMG-SQEDAHELLGKLLDELKlDLVNSFTIrifkttKDKKKTSTGDwfdiiielpdqtwvnnlktlqEFIDNMEE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  292 YFCERCKKKCDARKGLR----------FLHFPYLLTLQLKRFDFDyttmhriklndrmtfpeeldmSTFIDVEDEkspqt 361
Cdd:COG5533    149 LVDDETGVKAKENEELEvqakqeyevsFVKLPKILTIQLKRFANL---------------------GGNQKIDTE----- 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  362 esctdsgaenegschsdqmsndfsnddgVDEGICLetnsgTEKISKSGLEKNSLIYELFSVMVHSGSAAGGHYYACIKsf 441
Cdd:COG5533    203 ----------------------------VDEKFEL-----PVKHDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVK-- 247

                          330       340
                   ....*....|....*....|.
gi 1722213020  442 SDEQWYSFNDQHVSRITQEDI 462
Cdd:COG5533    248 KGGKWEKANDSDVTPVSEEEA 268
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 417-491 1.81e-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: 1.81e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1722213020  417 YELFSVMVHSGSAAGGHYYACIKSFSDEQWYSFNDQHVSRITQEDIKKthggssgsrgyysSAFASSTN--AYMLIY 491
Cdd:cd02665    164 YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVER-------------DSFGGGRNpsAYCLMY 227
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
164-292 1.14e-03

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 43.33  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  164 ETGYVGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEES--EEDP------VTSIPYQL-QRLFvllqTSKKRAIETT 234
Cdd:COG5560    262 EAGTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESinEENPlgmhgsVASAYADLiKQLY----DGNLHAFTPS 337

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  235 DVTRSFGWDSSE--AWQQHDVQELCRVMFDALeqkwkqteqEEALHAFIQPEILDGPNQY 292
Cdd:COG5560    338 GFKKTIGSFNEEfsGYDQQDSQEFIAFLLDGL---------HEDLNRIIKKPYTSKPDLS 388
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
168-451 1.56e-03

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 42.26  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  168 VGLVNQAMTCYLNSLLQTLFMTPEFRNALYKWEFEESEEDpvTSIPYQLQRLFVLLQTSKKRAIETTDVTRSFG------ 241
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHLATECLKE--HCLLCELGFLFDMLEKAKGKNCQASNFLRALSsipeas 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  242 ----WDSSEAWQQHD-----VQELCRVMFDALEQKWKQTEQEEALH-AFIQpEIL--DGPNQYFCERCKKKcDARKGLRF 309
Cdd:pfam13423   79 alglLDEDRETNSAIslsslIQSFNRFLLDQLSSEENSTPPNPSPAeSPLE-QLFgiDAETTIRCSNCGHE-SVRESSTH 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  310 LHfpylltlqlkrfDFDY--TTMHRIKLNDRMTFPEELDMStfidVEDEKSPQT--ESC-----TDSG----------AE 370
Cdd:pfam13423  157 VL------------DLIYprKPSSNNKKPPNQTFSSILKSS----LERETTTKAwcEKCkryqpLESRrtvrnlppvlSL 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  371 NEGsCHSDQMSNDFSNDDGVDEGIcletnsGTEKISKSGLEKNSLIYELFSVMVH-SGSAAGGHYYACIKSFSDE----- 444
Cdd:pfam13423  221 NAA-LTNEEWRQLWKTPGWLPPEI------GLTLSDDLQGDNEIVKYELRGVVVHiGDSGTSGHLVSFVKVADSEledpt 293


                   ....*....
gi 1722213020  445 --QWYSFND 451
Cdd:pfam13423  294 esQWYLFND 302
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 764-955 4.52e-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: 41.43  E-value: 4.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  764 VSYSKRTAYQKAGGDSGNVDDDC--ERVKGPvgslKSVEAILEESTEKLKSLSLQQQQDGDNGDSSKSTETSDF--ENIE 839
Cdd:NF033609   521 MSWDNEVAFNNGSGSGDGIDKPVvpEQPDEP----GEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSgsDSAS 596

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722213020  840 SPLNERDSSASVDNRELEQHIQTSDPENFQ-SEERSDSDVNNDRSTSSVDSDILSSSHSSDTLCNADNAQiplanglDSH 918
Cdd:NF033609   597 DSDSASDSDSASDSDSASDSDSASDSDSASdSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDS-------DSD 669

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1722213020  919 SITSSRRTKANEGKKETWDTAEEDSGTDSEYDESGKS 955
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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