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Conserved domains on  [gi|160703803|gb|EAT79673|]
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hypothetical protein SNOG_12873 [Parastagonospora nodorum SN15]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1439-1785 1.18e-112

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


The actual alignment was detected with superfamily member cd02659:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 334  Bit Score: 361.96  E-value: 1.18e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1439 GYVGLYNPRAICYMNSLLTQLFMNLNFRQFVLNLKVNEGF-GSQKLLFETQRLFAQMQNSFRKWTDPRDFaGCVKSLDKT 1517
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDdDNKSVPLALQRLFLFLQLSESPVKTTELT-DKTRSFGWD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1518 PIDIAVQMDADEFYNLLFDQWEAQMFKQEHKSKFRAFYGGQTMNQIKSKECEHVSERVEPFFAVQCDIAGKANLQESLQA 1597
Cdd:cd02659    80 SLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1598 YVEGDVMEGDNKYKCESCdGKFVDAVKryvraevrycsianadRTCLKDAPDNLIFHLKRFEFDLNDFSRRKIYDHFAFP 1677
Cdd:cd02659   160 YVQGETLEGDNKYFCEKC-GKKVDAEK----------------GVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFP 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1678 ETLDISPYKFDHLADPE-----KPREEDVFDLVGVLVHTGTCENGHYYSYIRQRPcssesaTPTWVEFNDSEVTPFDPAE 1752
Cdd:cd02659   223 LELDMEPYTEKGLAKKEgdsekKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD------DGKWYKFNDDVVTPFDPND 296
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 160703803 1753 IAERTFGGFTEGEGYNRQIKQF----SAYMLFYQRRS 1785
Cdd:cd02659   297 AEEECFGGEETQKTYDSGPRAFkrttNAYMLFYERKS 333
DUF3517 super family cl13466
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ...
1913-2294 7.59e-16

Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 340 amino acids in length. This domain is found associated with pfam00443.


The actual alignment was detected with superfamily member pfam12030:

Pssm-ID: 463438  Cd Length: 407  Bit Score: 82.35  E-value: 7.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  1913 SAMTNILIKCTHPTLRSQMRALLVDSLKSLREQ-EPSAYESDSSDSDMEVDSSTP--VEGVLVALTRrLRitaDESYEST 1989
Cdd:pfam12030    2 EALRELLLRNPDAEVRSAFGKLIVFALHKLKELyGLPDGPCDPDDLEEEWRSLSDsvLEAVVALLDH-LW---KEFHTHL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  1990 RGWEDFYLLLTQIAEMGLLETAVLLNHSFLQFCLKLFCMHTH--KPSREDCPELARVMDKRRSI-FNRLICFVWKLLSQM 2066
Cdd:pfam12030   78 RSWDEYFGLLLSYANLGPREVAQLLDLGFLLKCLEIIAADEGdgPPLKYQYARMLRLVEKRRPPsYEKLIQLLSVLLRCC 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  2067 DLNLDVLNDNDT-HDRLSTFDRERMkfPLSIRETAAVMYWSDDIKaiaiidkilEVFDDSKTDHFYPGD----IIKWILE 2141
Cdd:pfam12030  158 DLSLPPQSINEGaEPLPNSLPDGPF--PLTSEEADLLRPLGRTNG---------SIFVKKLLEIDQNPEatrkILRFLLW 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  2142 SrSAKLQSDMGRTIIEGIQMEP--PFCDAYIQAALPLCEASAisekittTINTVVKMVassKRAAEDRLpsgdavlglff 2219
Cdd:pfam12030  227 E-NPELSDSILKTLLWGIRGAPahLLRDPFLRAAIVFCEDSW-------QAHRIHNLI---DHVAKQAD----------- 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  2220 GLLTAENQAFF-YHK------------HPHAFYHCLMQRSSVYGIALLCHDEDRVRKSTNIFFQKLYGTKEaMALETIAI 2286
Cdd:pfam12030  285 SLNNTEGRAFLhFFKrayqcincrlgfDKEWFASQVLENIPDWAPPLLSYPDSNVRSETEDFLQEELFSHE-MGPDPQFR 363

                   ....*...
gi 160703803  2287 KYKSAREL 2294
Cdd:pfam12030  364 LREAARRL 371
 
Name Accession Description Interval E-value
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1439-1785 1.18e-112

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: 361.96  E-value: 1.18e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1439 GYVGLYNPRAICYMNSLLTQLFMNLNFRQFVLNLKVNEGF-GSQKLLFETQRLFAQMQNSFRKWTDPRDFaGCVKSLDKT 1517
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDdDNKSVPLALQRLFLFLQLSESPVKTTELT-DKTRSFGWD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1518 PIDIAVQMDADEFYNLLFDQWEAQMFKQEHKSKFRAFYGGQTMNQIKSKECEHVSERVEPFFAVQCDIAGKANLQESLQA 1597
Cdd:cd02659    80 SLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1598 YVEGDVMEGDNKYKCESCdGKFVDAVKryvraevrycsianadRTCLKDAPDNLIFHLKRFEFDLNDFSRRKIYDHFAFP 1677
Cdd:cd02659   160 YVQGETLEGDNKYFCEKC-GKKVDAEK----------------GVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFP 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1678 ETLDISPYKFDHLADPE-----KPREEDVFDLVGVLVHTGTCENGHYYSYIRQRPcssesaTPTWVEFNDSEVTPFDPAE 1752
Cdd:cd02659   223 LELDMEPYTEKGLAKKEgdsekKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD------DGKWYKFNDDVVTPFDPND 296
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 160703803 1753 IAERTFGGFTEGEGYNRQIKQF----SAYMLFYQRRS 1785
Cdd:cd02659   297 AEEECFGGEETQKTYDSGPRAFkrttNAYMLFYERKS 333
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1441-1781 2.10e-53

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 190.73  E-value: 2.10e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  1441 VGLYNPRAICYMNSLLTQLFMNLNFRQFVLN----LKVNEGFGSQKLLFETQRLFAQMQ-NSFRKWTDPRDFagcVKSLD 1515
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRisplSEDSRYNKDINLLCALRDLFKALQkNSKSSSVSPKMF---KKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  1516 KTPIDIAV--QMDADEFYNLLFDQWEAQMFKQEHKSK----FRAFyGGQTMNQIKSKECEHVSERVEPFFAVQCDIAGKA 1589
Cdd:pfam00443   78 KLNPDFSGykQQDAQEFLLFLLDGLHEDLNGNHSTENesliTDLF-RGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  1590 N------LQESLQAYVEGDVMEGDNKYKCESCdGKFVDAVKRyvraevrycsianadrTCLKDAPDNLIFHLKRFEFDLn 1663
Cdd:pfam00443  157 AelktasLQICFLQFSKLEELDDEEKYYCDKC-GCKQDAIKQ----------------LKISRLPPVLIIHLKRFSYNR- 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  1664 dFSRRKIYDHFAFPETLDISPYkfdhLADPEKPREEDV--FDLVGVLVHTGTCENGHYYSYIRQRPCSSesatptWVEFN 1741
Cdd:pfam00443  219 -STWEKLNTEVEFPLELDLSRY----LAEELKPKTNNLqdYRLVAVVVHSGSLSSGHYIAYIKAYENNR------WYKFD 287
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 160703803  1742 DSEVTPFDPAeiaertfggftegegynRQIKQFSAYMLFY 1781
Cdd:pfam00443  288 DEKVTEVDEE-----------------TAVLSSSAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
1438-1789 3.48e-45

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 180.07  E-value: 3.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1438 TGYVGLYNPRAICYMNSLLTQLFMNLNFRQFVLNLKVNEGFGSQKLLFETQRLFAQMQNSfrkwTDPRDFAGCVKSLDKT 1517
Cdd:COG5077   191 TGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTG----EEPVDTTELTRSFGWD 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1518 PIDIAVQMDADEFYNLLFDQWEAQMFKQEHKSKFRAFYGGQTMNQIKSKECEHVSERVEPFFAVQCDIAGKANLQESLQA 1597
Cdd:COG5077   267 SDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRR 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1598 YVEGDVMEGDNKYKCEscDGKFVDAVKryvraEVRYCSIanadrtclkdaPDNLIFHLKRFEFDLNDFSRRKIYDHFAFP 1677
Cdd:COG5077   347 YIQVETLDGDNRYNAE--KHGLQDAKK-----GVIFESL-----------PPVLHLQLKRFEYDFERDMMVKINDRYEFP 408
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1678 ETLDISPYkfdhlADPEKPREED---VFDLVGVLVHTGTCENGHYYSYIRQRPCSSesatptWVEFNDSEVTPFDPAEIA 1754
Cdd:COG5077   409 LEIDLLPF-----LDRDADKSENsdaVYVLYGVLVHSGDLHEGHYYALLKPEKDGR------WYKFDDTRVTRATEKEVL 477
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 160703803 1755 ERTFGG----FTEGEGYNRQIKQFSAYMLFYQRRSAVEE 1789
Cdd:COG5077   478 EENFGGdhpyKDKIRDHSGIKRFMSAYMLVYLRKSMLDD 516
DUF3517 pfam12030
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ...
1913-2294 7.59e-16

Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 340 amino acids in length. This domain is found associated with pfam00443.


Pssm-ID: 463438  Cd Length: 407  Bit Score: 82.35  E-value: 7.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  1913 SAMTNILIKCTHPTLRSQMRALLVDSLKSLREQ-EPSAYESDSSDSDMEVDSSTP--VEGVLVALTRrLRitaDESYEST 1989
Cdd:pfam12030    2 EALRELLLRNPDAEVRSAFGKLIVFALHKLKELyGLPDGPCDPDDLEEEWRSLSDsvLEAVVALLDH-LW---KEFHTHL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  1990 RGWEDFYLLLTQIAEMGLLETAVLLNHSFLQFCLKLFCMHTH--KPSREDCPELARVMDKRRSI-FNRLICFVWKLLSQM 2066
Cdd:pfam12030   78 RSWDEYFGLLLSYANLGPREVAQLLDLGFLLKCLEIIAADEGdgPPLKYQYARMLRLVEKRRPPsYEKLIQLLSVLLRCC 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  2067 DLNLDVLNDNDT-HDRLSTFDRERMkfPLSIRETAAVMYWSDDIKaiaiidkilEVFDDSKTDHFYPGD----IIKWILE 2141
Cdd:pfam12030  158 DLSLPPQSINEGaEPLPNSLPDGPF--PLTSEEADLLRPLGRTNG---------SIFVKKLLEIDQNPEatrkILRFLLW 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  2142 SrSAKLQSDMGRTIIEGIQMEP--PFCDAYIQAALPLCEASAisekittTINTVVKMVassKRAAEDRLpsgdavlglff 2219
Cdd:pfam12030  227 E-NPELSDSILKTLLWGIRGAPahLLRDPFLRAAIVFCEDSW-------QAHRIHNLI---DHVAKQAD----------- 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  2220 GLLTAENQAFF-YHK------------HPHAFYHCLMQRSSVYGIALLCHDEDRVRKSTNIFFQKLYGTKEaMALETIAI 2286
Cdd:pfam12030  285 SLNNTEGRAFLhFFKrayqcincrlgfDKEWFASQVLENIPDWAPPLLSYPDSNVRSETEDFLQEELFSHE-MGPDPQFR 363

                   ....*...
gi 160703803  2287 KYKSAREL 2294
Cdd:pfam12030  364 LREAARRL 371
 
Name Accession Description Interval E-value
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1439-1785 1.18e-112

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: 361.96  E-value: 1.18e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1439 GYVGLYNPRAICYMNSLLTQLFMNLNFRQFVLNLKVNEGF-GSQKLLFETQRLFAQMQNSFRKWTDPRDFaGCVKSLDKT 1517
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDdDNKSVPLALQRLFLFLQLSESPVKTTELT-DKTRSFGWD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1518 PIDIAVQMDADEFYNLLFDQWEAQMFKQEHKSKFRAFYGGQTMNQIKSKECEHVSERVEPFFAVQCDIAGKANLQESLQA 1597
Cdd:cd02659    80 SLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1598 YVEGDVMEGDNKYKCESCdGKFVDAVKryvraevrycsianadRTCLKDAPDNLIFHLKRFEFDLNDFSRRKIYDHFAFP 1677
Cdd:cd02659   160 YVQGETLEGDNKYFCEKC-GKKVDAEK----------------GVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFP 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1678 ETLDISPYKFDHLADPE-----KPREEDVFDLVGVLVHTGTCENGHYYSYIRQRPcssesaTPTWVEFNDSEVTPFDPAE 1752
Cdd:cd02659   223 LELDMEPYTEKGLAKKEgdsekKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRD------DGKWYKFNDDVVTPFDPND 296
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 160703803 1753 IAERTFGGFTEGEGYNRQIKQF----SAYMLFYQRRS 1785
Cdd:cd02659   297 AEEECFGGEETQKTYDSGPRAFkrttNAYMLFYERKS 333
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1441-1781 2.10e-53

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 190.73  E-value: 2.10e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  1441 VGLYNPRAICYMNSLLTQLFMNLNFRQFVLN----LKVNEGFGSQKLLFETQRLFAQMQ-NSFRKWTDPRDFagcVKSLD 1515
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRisplSEDSRYNKDINLLCALRDLFKALQkNSKSSSVSPKMF---KKSLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  1516 KTPIDIAV--QMDADEFYNLLFDQWEAQMFKQEHKSK----FRAFyGGQTMNQIKSKECEHVSERVEPFFAVQCDIAGKA 1589
Cdd:pfam00443   78 KLNPDFSGykQQDAQEFLLFLLDGLHEDLNGNHSTENesliTDLF-RGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  1590 N------LQESLQAYVEGDVMEGDNKYKCESCdGKFVDAVKRyvraevrycsianadrTCLKDAPDNLIFHLKRFEFDLn 1663
Cdd:pfam00443  157 AelktasLQICFLQFSKLEELDDEEKYYCDKC-GCKQDAIKQ----------------LKISRLPPVLIIHLKRFSYNR- 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  1664 dFSRRKIYDHFAFPETLDISPYkfdhLADPEKPREEDV--FDLVGVLVHTGTCENGHYYSYIRQRPCSSesatptWVEFN 1741
Cdd:pfam00443  219 -STWEKLNTEVEFPLELDLSRY----LAEELKPKTNNLqdYRLVAVVVHSGSLSSGHYIAYIKAYENNR------WYKFD 287
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 160703803  1742 DSEVTPFDPAeiaertfggftegegynRQIKQFSAYMLFY 1781
Cdd:pfam00443  288 DEKVTEVDEE-----------------TAVLSSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
1442-1782 3.45e-53

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: 188.08  E-value: 3.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1442 GLYNPRAICYMNSLLtqlfmnlnfrqfvlnlkvnegfgsqkllfetQRLFAQMQnsfrkwtdprdfagcvksldktpidi 1521
Cdd:cd02257     1 GLNNLGNTCYLNSVL-------------------------------QALFSEQQ-------------------------- 23
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1522 avqmDADEFYNLLFDQWEAQMFKQEHKSKFRAF--------YGGQTMNQIKSKECEHVSERVEPFFAVQCDIAGKA---- 1589
Cdd:cd02257    24 ----DAHEFLLFLLDKLHEELKKSSKRTSDSSSlkslihdlFGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGlpqv 99
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1590 NLQESLQAYVEGDVMEGDNKYKCESCdgKFVDAVKRyvraevrycsianadrTCLKDAPDNLIFHLKRFEFDlNDFSRRK 1669
Cdd:cd02257   100 SLEDCLEKFFKEEILEGDNCYKCEKK--KKQEATKR----------------LKIKKLPPVLIIHLKRFSFN-EDGTKEK 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1670 IYDHFAFPETLDISPYKFDHLADPEKPREEDVFDLVGVLVHTGTCEN-GHYYSYIRQRPCSSesatptWVEFNDSEVTPF 1748
Cdd:cd02257   161 LNTKVSFPLELDLSPYLSEGEKDSDSDNGSYKYELVAVVVHSGTSADsGHYVAYVKDPSDGK------WYKFNDDKVTEV 234
                         330       340       350
                  ....*....|....*....|....*....|....
gi 160703803 1749 DPAEIAERTFggftegegynrqiKQFSAYMLFYQ 1782
Cdd:cd02257   235 SEEEVLEFGS-------------LSSSAYILFYE 255
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
1438-1789 3.48e-45

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 180.07  E-value: 3.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1438 TGYVGLYNPRAICYMNSLLTQLFMNLNFRQFVLNLKVNEGFGSQKLLFETQRLFAQMQNSfrkwTDPRDFAGCVKSLDKT 1517
Cdd:COG5077   191 TGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIPTDHPRGRDSVALALQRLFYNLQTG----EEPVDTTELTRSFGWD 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1518 PIDIAVQMDADEFYNLLFDQWEAQMFKQEHKSKFRAFYGGQTMNQIKSKECEHVSERVEPFFAVQCDIAGKANLQESLQA 1597
Cdd:COG5077   267 SDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRR 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1598 YVEGDVMEGDNKYKCEscDGKFVDAVKryvraEVRYCSIanadrtclkdaPDNLIFHLKRFEFDLNDFSRRKIYDHFAFP 1677
Cdd:COG5077   347 YIQVETLDGDNRYNAE--KHGLQDAKK-----GVIFESL-----------PPVLHLQLKRFEYDFERDMMVKINDRYEFP 408
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1678 ETLDISPYkfdhlADPEKPREED---VFDLVGVLVHTGTCENGHYYSYIRQRPCSSesatptWVEFNDSEVTPFDPAEIA 1754
Cdd:COG5077   409 LEIDLLPF-----LDRDADKSENsdaVYVLYGVLVHSGDLHEGHYYALLKPEKDGR------WYKFDDTRVTRATEKEVL 477
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 160703803 1755 ERTFGG----FTEGEGYNRQIKQFSAYMLFYQRRSAVEE 1789
Cdd:COG5077   478 EENFGGdhpyKDKIRDHSGIKRFMSAYMLVYLRKSMLDD 516
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1442-1781 3.65e-44

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: 164.52  E-value: 3.65e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1442 GLYNPRAICYMNSLLTQLFMNLNFRQFVL-----------NLKVNEGFGSQKLLFETQRLFAQMQNSFRKWTDPRDFagc 1510
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYecnstedaelkNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGF--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1511 VKSLDktpIDIAVQMDADEFYNLLFDQWEAQMFKQEH---KSKFRAFYGGQTMNQIKSKECEHVSERVEPFFAVQCDIAG 1587
Cdd:cd02668    78 VKALG---LDTGQQQDAQEFSKLFLSLLEAKLSKSKNpdlKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1588 KANLQESLQAYVEGDVMEGDNKYKCESCDGKfVDAVKryvraevrycsianadRTCLKDAPDNLIFHLKRFEFDLNDFSR 1667
Cdd:cd02668   155 HKTLEECIDEFLKEEQLTGDNQYFCESCNSK-TDATR----------------RIRLTTLPPTLNFQLLRFVFDRKTGAK 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1668 RKIYDHFAFPETLDISPYKfdhladPEKPREEDVFDLVGVLVHTGTCEN-GHYYSYIRqrpcssESATPTWVEFNDSEVT 1746
Cdd:cd02668   218 KKLNASISFPEILDMGEYL------AESDEGSYVYELSGVLIHQGVSAYsGHYIAHIK------DEQTGEWYKFNDEDVE 285
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 160703803 1747 PFDP---AEIAERTFGGFTEGEGYNRQIKQFSAYMLFY 1781
Cdd:cd02668   286 EMPGkplKLGNSEDPAKPRKSEIKKGTHSSRTAYMLVY 323
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1442-1781 5.21e-39

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


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 148.58  E-value: 5.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1442 GLYNPRAICYMNSLL-----TQLFMNLNFRQFVLNLKVNEGFgsqKLLFETQRLFAQMQNSFRKWTDPRDFAGCVKSLDK 1516
Cdd:cd02661     3 GLQNLGNTCFLNSVLqclthTPPLANYLLSREHSKDCCNEGF---CMMCALEAHVERALASSGPGSAPRIFSSNLKQISK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1517 TpIDIAVQMDADEFYNLLFDQWEA---QMFKQEHKSKFRAF--------YGGQTMNQIKSKECEHVSERVEPFFAVQCDI 1585
Cdd:cd02661    80 H-FRIGRQEDAHEFLRYLLDAMQKaclDRFKKLKAVDPSSQettlvqqiFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1586 AGKANLQESLQAYVEGDVMEGDNKYKCESCdgkfvdavKRYVRAEVRYcSIanaDRtclkdAPDNLIFHLKRFEFdlndF 1665
Cdd:cd02661   159 KGADSLEDALEQFTKPEQLDGENKYKCERC--------KKKVKASKQL-TI---HR-----APNVLTIHLKRFSN----F 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1666 SRRKIYDHFAFPETLDISPYkfdhLADPekPREEDVFDLVGVLVHTGT-CENGHYYSYIRqrpcsseSATPTWVEFNDSE 1744
Cdd:cd02661   218 RGGKINKQISFPETLDLSPY----MSQP--NDGPLKYKLYAVLVHSGFsPHSGHYYCYVK-------SSNGKWYNMDDSK 284
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 160703803 1745 VTPFDPAEIaertfggftegegYNRQikqfsAYMLFY 1781
Cdd:cd02661   285 VSPVSIETV-------------LSQK-----AYILFY 303
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1442-1782 1.84e-31

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: 127.61  E-value: 1.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1442 GLYNPRAICYMNSLLTQLFMNLNFRQFVLNLKVNEGFGSQKLLFETQRLFAQMQNSFRKWTDPRDfagcvKSLDKT---P 1518
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLMHTQRRAEAPPD-----YFLEASrppW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1519 IDIAVQMDADEFYNLLFDQWEA---QMFkqehkskfrafyGGQTMNQIKSKECEHVSERVEPFFAVQCDIagkANLQESL 1595
Cdd:cd02664    76 FTPGSQQDCSEYLRYLLDRLHTlieKMF------------GGKLSTTIRCLNCNSTSARTERFRDLDLSF---PSVQDLL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1596 QAYVEGDVMEGDNKYKCESCdgkfvdavkryvraevryCSIANADRTC-LKDAPDNLIFHLKRFEFDLNDFSRRKIYDHF 1674
Cdd:cd02664   141 NYFLSPEKLTGDNQYYCEKC------------------ASLQDAEKEMkVTGAPEYLILTLLRFSYDQKTHVREKIMDNV 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1675 AFPETL-----DISPYKFDHLADPEKPREED--------VFDLVGVLVHTGTC-ENGHYYSYIRQ----RPCSSESATP- 1735
Cdd:cd02664   203 SINEVLslpvrVESKSSESPLEKKEEESGDDgelvtrqvHYRLYAVVVHSGYSsESGHYFTYARDqtdaDSTGQECPEPk 282
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 160703803 1736 ---------TWVEFNDSEVTPFDPAEIAERTFGGFTEgegynrqikqfSAYMLFYQ 1782
Cdd:cd02664   283 daeendeskNWYLFNDSRVTFSSFESVQNVTSRFPKD-----------TPYILFYE 327
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1442-1781 3.30e-30

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: 123.64  E-value: 3.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1442 GLYNPRAICYMNSLLTQLFMNLNFRQFVLNLKVNEGFGSQK----LLFETQRLFAQMQNSFRK------------WTDPR 1505
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSpnscLSCAMDEIFQEFYYSGDRspygpinllylsWKHSR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1506 DFAGcvksldktpidiAVQMDADEFYNLLFDQweaqmFKQEHKSKF--------------RAFYGgQTMNQIKSKECEHV 1571
Cdd:cd02660    82 NLAG------------YSQQDAHEFFQFLLDQ-----LHTHYGGDKneandeshcnciihQTFSG-SLQSSVTCQRCGGV 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1572 SERVEPFFAVQCDI---------------AGKANLQESLQAYVEGDVMeGDNKYKCESCDGKfVDAVKRYVraevrycsi 1636
Cdd:cd02660   144 STTVDPFLDLSLDIpnkstpswalgesgvSGTPTLSDCLDRFTRPEKL-GDFAYKCSGCGST-QEATKQLS--------- 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1637 anadrtcLKDAPDNLIFHLKRFEFDLNDfSRRKIYDHFAFPETLDISPYKF--DHLADPEKPREEDV-FDLVGVLVHTGT 1713
Cdd:cd02660   213 -------IKKLPPVLCFQLKRFEHSLNK-TSRKIDTYVQFPLELNMTPYTSssIGDTQDSNSLDPDYtYDLFAVVVHKGT 284
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160703803 1714 CENGHYYSYIRQRpcssesaTPTWVEFNDSEVTPFDPAEI-AERtfggftegegynrqikqfsAYMLFY 1781
Cdd:cd02660   285 LDTGHYTAYCRQG-------DGQWFKFDDAMITRVSEEEVlKSQ-------------------AYLLFY 327
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1442-1782 2.92e-29

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


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 120.11  E-value: 2.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1442 GLYNPRAICYMNSLLTQLFMNlnfrqfvlnlkvnegfgsqKLLFETQRLFAQMQNSFRKW--TDPRDFagcVKSLDK-TP 1518
Cdd:cd02663     1 GLENFGNTCYCNSVLQALYFE-------------------NLLTCLKDLFESISEQKKRTgvISPKKF---ITRLKReNE 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1519 I-DIAVQMDADEFYNLLF-----------------DQWEAQMFKQEHKSKFRAFYGGQTMNQIKSKECEHVSERVEPFFA 1580
Cdd:cd02663    59 LfDNYMHQDAHEFLNFLLneiaeildaerkaekanRKLNNNNNAEPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLD 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1581 VQCDIAGKANLQESLQAYVEGDVMEGDNKYKCESCDGKfVDAVKRyVRaevrycsianadrtcLKDAPDNLIFHLKRFEF 1660
Cdd:cd02663   139 LSIDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSL-QEAEKR-MK---------------IKKLPKILALHLKRFKY 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1661 DLNDFSRRKIYDHFAFPETLDIspykFDHLADPEKPreEDVFDLVGVLVHTGTCEN-GHYYSYIRqrpcssesATPTWVE 1739
Cdd:cd02663   202 DEQLNRYIKLFYRVVFPLELRL----FNTTDDAENP--DRLYELVAVVVHIGGGPNhGHYVSIVK--------SHGGWLL 267
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 160703803 1740 FNDSEVTPFDPAEIAErtFGGFTEGegynrqikQFSAYMLFYQ 1782
Cdd:cd02663   268 FDDETVEKIDENAVEE--FFGDSPN--------QATAYVLFYQ 300
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1524-1782 1.07e-28

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: 116.62  E-value: 1.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1524 QMDADEFYNLLFDqweaqmfkqEHKSKFRAFYGGQTMNQIKSKECEHVSERVEPFFAVQCDI------AGKANLQESLQA 1597
Cdd:cd02674    22 QQDAQEFLLFLLD---------GLHSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdAPKVTLEDCLRL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1598 YVEGDVMEGDNKYKCESCdgkfvdavKRYVRAEvRYCSIAnadrtclkDAPDNLIFHLKRFEFDLNdfSRRKIYDHFAFP 1677
Cdd:cd02674    93 FTKEETLDGDNAWKCPKC--------KKKRKAT-KKLTIS--------RLPKVLIIHLKRFSFSRG--STRKLTTPVTFP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1678 -ETLDISPYkfdhlADPEKPREEDVFDLVGVLVHTGTCENGHYYSYIRqrpcssESATPTWVEFNDSEVTPFDPAEIAER 1756
Cdd:cd02674   154 lNDLDLTPY-----VDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCK------NNETNDWYKFDDSRVTKVSESSVVSS 222
                         250       260
                  ....*....|....*....|....*.
gi 160703803 1757 tfggftegegynrqikqfSAYMLFYQ 1782
Cdd:cd02674   223 ------------------SAYILFYE 230
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1503-1747 9.16e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 97.84  E-value: 9.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1503 DPRDFAGCVKSLDKTPIDiAVQMDADEFYNLLFDqweaqmfkqehksKFRAF----YGGQTMNQIKSKECEHVSERVEPF 1578
Cdd:cd02667    31 TPKELFSQVCRKAPQFKG-YQQQDSHELLRYLLD-------------GLRTFidsiFGGELTSTIMCESCGTVSLVYEPF 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1579 FAVQC----DIAGKANLQESLQAYVEGDVMEGDNKYKCESCDgkfvDAVKRYVraevrycsianadrtcLKDAPDNLIFH 1654
Cdd:cd02667    97 LDLSLprsdEIKSECSIESCLKQFTEVEILEGNNKFACENCT----KAKKQYL----------------ISKLPPVLVIH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1655 LKRFeFDLNDFSRRKIYDHFAFPETLDISPY---KFDHLADPEKPReedvFDLVGVLVHTGTCENGHYYSYIRQRPCSSE 1731
Cdd:cd02667   157 LKRF-QQPRSANLRKVSRHVSFPEILDLAPFcdpKCNSSEDKSSVL----YRLYGVVEHSGTMRSGHYVAYVKVRPPQQR 231
                         250
                  ....*....|....*.
gi 160703803 1732 SATPTWVEFNDSEVTP 1747
Cdd:cd02667   232 LSDLTKSKPAADEAGP 247
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1442-1783 6.34e-18

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 86.39  E-value: 6.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1442 GLYNPRAICYMNSLLTQLFMNLNfrqfvlnlKVNEGFGsqKLLFETQRLFAQMQNSFRKWTDPR--DFAGCVKSLDKTPI 1519
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILALYLP--------KLDELLD--DLSKELKVLKNVIRKPEPDLNQEEalKLFTALWSSKEHKV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1520 ----DIAVQMDADEFYNLLFDQWEAQMFKQEHKSKFRAF--YGGQTMNQIKSKECEHVSERvepffavqcdiagKANLQE 1593
Cdd:COG5533    71 gwipPMGSQEDAHELLGKLLDELKLDLVNSFTIRIFKTTkdKKKTSTGDWFDIIIELPDQT-------------WVNNLK 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1594 SLQAYVEGDVMEGDNKykcesCDGKFVDAVKRYVRAEVRYCSIAnadrtclKDAPDNLIFHLKRFEfdlNDFSRRKIYDh 1673
Cdd:COG5533   138 TLQEFIDNMEELVDDE-----TGVKAKENEELEVQAKQEYEVSF-------VKLPKILTIQLKRFA---NLGGNQKIDT- 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1674 fAFPETLDIsPYKFDhlaDPEKPREEDVFDLVGVLVHTGTCENGHYYSYIRQRpcssesatPTWVEFNDSEVTPfdpaei 1753
Cdd:COG5533   202 -EVDEKFEL-PVKHD---QILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKKG--------GKWEKANDSDVTP------ 262
                         330       340       350
                  ....*....|....*....|....*....|
gi 160703803 1754 aertfggFTEGEGYNRQIKQfsAYMLFYQR 1783
Cdd:COG5533   263 -------VSEEEAINEKAKN--AYLYFYER 283
DUF3517 pfam12030
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ...
1913-2294 7.59e-16

Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 340 amino acids in length. This domain is found associated with pfam00443.


Pssm-ID: 463438  Cd Length: 407  Bit Score: 82.35  E-value: 7.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  1913 SAMTNILIKCTHPTLRSQMRALLVDSLKSLREQ-EPSAYESDSSDSDMEVDSSTP--VEGVLVALTRrLRitaDESYEST 1989
Cdd:pfam12030    2 EALRELLLRNPDAEVRSAFGKLIVFALHKLKELyGLPDGPCDPDDLEEEWRSLSDsvLEAVVALLDH-LW---KEFHTHL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  1990 RGWEDFYLLLTQIAEMGLLETAVLLNHSFLQFCLKLFCMHTH--KPSREDCPELARVMDKRRSI-FNRLICFVWKLLSQM 2066
Cdd:pfam12030   78 RSWDEYFGLLLSYANLGPREVAQLLDLGFLLKCLEIIAADEGdgPPLKYQYARMLRLVEKRRPPsYEKLIQLLSVLLRCC 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  2067 DLNLDVLNDNDT-HDRLSTFDRERMkfPLSIRETAAVMYWSDDIKaiaiidkilEVFDDSKTDHFYPGD----IIKWILE 2141
Cdd:pfam12030  158 DLSLPPQSINEGaEPLPNSLPDGPF--PLTSEEADLLRPLGRTNG---------SIFVKKLLEIDQNPEatrkILRFLLW 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  2142 SrSAKLQSDMGRTIIEGIQMEP--PFCDAYIQAALPLCEASAisekittTINTVVKMVassKRAAEDRLpsgdavlglff 2219
Cdd:pfam12030  227 E-NPELSDSILKTLLWGIRGAPahLLRDPFLRAAIVFCEDSW-------QAHRIHNLI---DHVAKQAD----------- 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803  2220 GLLTAENQAFF-YHK------------HPHAFYHCLMQRSSVYGIALLCHDEDRVRKSTNIFFQKLYGTKEaMALETIAI 2286
Cdd:pfam12030  285 SLNNTEGRAFLhFFKrayqcincrlgfDKEWFASQVLENIPDWAPPLLSYPDSNVRSETEDFLQEELFSHE-MGPDPQFR 363

                   ....*...
gi 160703803  2287 KYKSAREL 2294
Cdd:pfam12030  364 LREAARRL 371
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1442-1782 1.01e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 76.25  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1442 GLYNPRAICYMNSLLtqlfmnlnfrQFVLNLKvnegfgsqkllfetqrlfaqmqnSFRKWtdprdfagcvksLDKtpidI 1521
Cdd:cd02662     1 GLVNLGNTCFMNSVL----------QALASLP-----------------------SLIEY------------LEE----F 31
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1522 AVQMDADEFYNLLFDQWEAQMfkqehKSKFRafygGQTMNQIKSKECEHVSE-RVEPFF-----AVQCDIAGKANLQESL 1595
Cdd:cd02662    32 LEQQDAHELFQVLLETLEQLL-----KFPFD----GLLASRIVCLQCGESSKvRYESFTmlslpVPNQSSGSGTTLEHCL 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1596 QAYVEGDVMEGdnkYKCESCdgkfvdavkryvraevrycsianadRTCLKDAPDNLIFHLKRFEFDLNDFSRRKiYDHFA 1675
Cdd:cd02662   103 DDFLSTEIIDD---YKCDRC-------------------------QTVIVRLPQILCIHLSRSVFDGRGTSTKN-SCKVS 153
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1676 FPETLDISPYKfdhladpekpreedvfdLVGVLVHTGTCENGHYYSYIRQRPCSSESATP--------------TWVEFN 1741
Cdd:cd02662   154 FPERLPKVLYR-----------------LRAVVVHYGSHSSGHYVCYRRKPLFSKDKEPGsfvrmregpsstshPWWRIS 216
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 160703803 1742 DSEVTPFDPAEIAErtfggftegegynrqikQFSAYMLFYQ 1782
Cdd:cd02662   217 DTTVKEVSESEVLE-----------------QKSAYMLFYE 240
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1524-1781 1.26e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 75.67  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1524 QMDADEFYNLLFDQWEAQMFKQEH------KSK---FRAFYGGQTMNQIK-SKECEHVservEPFFAVQCDIAGKANLQE 1593
Cdd:cd02665    22 QQDVSEFTHLLLDWLEDAFQAAAEaispgeKSKnpmVQLFYGTFLTEGVLeGKPFCNC----ETFGQYPLQVNGYGNLHE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1594 SLQ-AYVEGDVmegdnkykcescDGKFVDAVKRYVRaevrycsianadRTCLKDAPDNLIFHLKRFEFdlNDFSRRKIYD 1672
Cdd:cd02665    98 CLEaAMFEGEV------------ELLPSDHSVKSGQ------------ERWFTELPPVLTFELSRFEF--NQGRPEKIHD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1673 HFAFPETLDISPYKfdhladpekpreedvfdLVGVLVHTGTCENGHYYSYIRQRPCSSesatptWVEFNDSEVTPFDPAE 1752
Cdd:cd02665   152 KLEFPQIIQQVPYE-----------------LHAVLVHEGQANAGHYWAYIYKQSRQE------WEKYNDISVTESSWEE 208
                         250       260
                  ....*....|....*....|....*....
gi 160703803 1753 IAERTFGGFtegegynrqiKQFSAYMLFY 1781
Cdd:cd02665   209 VERDSFGGG----------RNPSAYCLMY 227
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1442-1781 2.68e-13

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 73.13  E-value: 2.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1442 GLYNPRAICYMNSLLTQLFMNLNFRQFVLNLKVNEGFGSQ---KLLFETQRLFAQMQNS------FRKWTDPRD----FA 1508
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQssdNLTNALRDLFDTMDKKqepvppIEFLQLLRMafpqFA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1509 gcvkslDKTPIDIAVQMDADEFYNLLFdqweaQMFKQE------HKSKFRAFYGGQTMNQIKSKECEHVSE-RVEPFFAV 1581
Cdd:cd02657    81 ------EKQNQGGYAQQDAEECWSQLL-----SVLSQKlpgagsKGSFIDQLFGIELETKMKCTESPDEEEvSTESEYKL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1582 QCDIAGKAN---LQESLQAYVEGDVMegdnkykcescdgKFVDAVKRyvraEVRYCSIANADRTclkdaPDNLIFHLKRF 1658
Cdd:cd02657   150 QCHISITTEvnyLQDGLKKGLEEEIE-------------KHSPTLGR----DAIYTKTSRISRL-----PKYLTVQFVRF 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1659 EFDLNDFSRRKIYDHFAFPETLDIspykFDHLAdpekprEEDVFDLVGVLVHTG-TCENGHYYSYIRQrpcsseSATPTW 1737
Cdd:cd02657   208 FWKRDIQKKAKILRKVKFPFELDL----YELCT------PSGYYELVAVITHQGrSADSGHYVAWVRR------KNDGKW 271
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 160703803 1738 VEFNDSEVTPFDPAEIaERTFGGfteGEgynrqikQFSAYMLFY 1781
Cdd:cd02657   272 IKFDDDKVSEVTEEDI-LKLSGG---GD-------WHIAYILLY 304
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
1568-1785 9.63e-13

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 74.15  E-value: 9.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1568 CEHVSERVEPFFAVQCDI--------AGKANLQESLQAYVEGDVMEGDNKYKCESCDGkFVDAVKRYVraevrycsiana 1639
Cdd:COG5560   646 CEWEEKRYLSLFSYDPLWtireigaaERTITLQDCLNEFSKPEQLGLSDSWYCPGCKE-FRQASKQME------------ 712
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1640 drtcLKDAPDNLIFHLKRFEFDLNdfSRRKIYDHFAFPET-LDISPYkfdhLADPEKPREedVFDLVGVLVHTGTCENGH 1718
Cdd:COG5560   713 ----LWRLPMILIIHLKRFSSVRS--FRDKIDDLVEYPIDdLDLSGV----EYMVDDPRL--IYDLYAVDNHYGGLSGGH 780
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160703803 1719 YYSYIRqrpcssESATPTWVEFNDSEVTPFDPAEIAERtfggftegegynrqikqfSAYMLFYQRRS 1785
Cdd:COG5560   781 YTAYAR------NFANNGWYLFDDSRITEVDPEDSVTS------------------SAYVLFYRRKS 823
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1440-1781 7.91e-12

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


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 69.15  E-value: 7.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1440 YVGLYNPRAICYMNSLLTQLFMNLNFRQFVLNLkvNEGFGSQKLLFETQRLFAQMQNSFRKWTDPRDFAGCVKSLDKTpI 1519
Cdd:cd02671    24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHL--VSLISSVEQLQSSFLLNPEKYNDELANQAPRRLLNALREVNPM-Y 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1520 DIAVQMDADEFYNLLFDQweAQMFkqehkskFRAFYGGQTMNQIKSKECEHVSERVEPF----FAVQCDIAGK------- 1588
Cdd:cd02671   101 EGYLQHDAQEVLQCILGN--IQEL-------VEKDFQGQLVLRTRCLECETFTERREDFqdisVPVQESELSKseessei 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1589 --------ANLQESLQAYVEGDVMEGDNKYKCESCDGkfvdavkrYVRAEvrycsianadRTCLKDA-PDNLIFHLKRFE 1659
Cdd:cd02671   172 spdpktemKTLKWAISQFASVERIVGEDKYFCENCHH--------YTEAE----------RSLLFDKlPEVITIHLKCFA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1660 FDLNDFSR----RKIydHFAFPETLDISPYKFDhladpEKPReEDVFDLVGVLVHTG-TCENGHYYSYIRqrpcssesat 1734
Cdd:cd02671   234 ANGSEFDCygglSKV--NTPLLTPLKLSLEEWS-----TKPK-NDVYRLFAVVMHSGaTISSGHYTAYVR---------- 295
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 160703803 1735 ptWVEFNDSEVTPFDPAEiaertfggFTEGEGYNRQIKQfSAYMLFY 1781
Cdd:cd02671   296 --WLLFDDSEVKVTEEKD--------FLEALSPNTSSTS-TPYLLFY 331
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1524-1745 1.27e-09

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


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 61.96  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1524 QMDADEFYNLLFDQWEaQMFKQEHKSKFRAFYGGQTMNQIKSKECEHV--SERVEPFFA--VQCDIAGKA---------- 1589
Cdd:cd02658   100 QQDALEFLLHLIDKLD-RESFKNLGLNPNDLFKFMIEDRLECLSCKKVkyTSELSEILSlpVPKDEATEKeegelvyepv 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1590 NLQESLQAYVEGDVMEgdnkYKCESCDGKfVDAVKRyvraevrycsianadrTCLKDAPDNLIFHLKRFEFDLNdFSRRK 1669
Cdd:cd02658   179 PLEDCLKAYFAPETIE----DFCSTCKEK-TTATKT----------------TGFKTFPDYLVINMKRFQLLEN-WVPKK 236
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160703803 1670 IYDHFAFPETLDISPYKfdhladpekpreedvfdLVGVLVHTGTCEN-GHYYSYIRQRpcssESATPTWVEFNDSEV 1745
Cdd:cd02658   237 LDVPIDVPEELGPGKYE-----------------LIAFISHKGTSVHsGHYVAHIKKE----IDGEGKWVLFNDEKV 292
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1439-1746 2.78e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 52.32  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1439 GYVGLYNPRAICYMNSLLtQLFMNLN-FRQFVLNLKVNEGFGSQK--LLFETQRLFAQMQNS--FRKWTDPRDFAGCVKS 1513
Cdd:cd02669   118 GFVGLNNIKNNDYANVII-QALSHVKpIRNFFLLYENYENIKDRKseLVKRLSELIRKIWNPrnFKGHVSPHELLQAVSK 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1514 LDKTPIDIAVQMDADEFYNLLFDQWEAQM--FKQEHKSKF-RAFYG---------GQTMNQIKSKECEHVSERVE----- 1576
Cdd:cd02669   197 VSKKKFSITEQSDPVEFLSWLLNTLHKDLggSKKPNSSIIhDCFQGkvqietqkiKPHAEEEGSKDKFFKDSRVKktsvs 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1577 PFFAVQCDIAGKANLQeslqayvegDVMEGD-----------NKYkcescDGKFVDAVKRYVRaevrycsianadRTCLK 1645
Cdd:cd02669   277 PFLLLTLDLPPPPLFK---------DGNEENiipqvplkqllKKY-----DGKTETELKDSLK------------RYLIS 330
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1646 DAPDNLIFHLKRfeFDLNDFSRRKIYDHFAFPETLDISPYKFDHLADPEKPREEdvFDLVGVLVHTGT-CENGHYYSYIR 1724
Cdd:cd02669   331 RLPKYLIFHIKR--FSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLSTK--YNLVANIVHEGTpQEDGTWRVQLR 406
                         330       340
                  ....*....|....*....|..
gi 160703803 1725 QRpcssesATPTWVEFNDSEVT 1746
Cdd:cd02669   407 HK------STNKWFEIQDLNVK 422
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1522-1782 2.80e-05

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


Pssm-ID: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 47.91  E-value: 2.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1522 AVQMDADEFYNLLFDQweaqMFKQEHKSKFRAFYGGQTmnqiKSKECEHVSERVEPFFAVQCDIAGKANLQESLQAYveg 1601
Cdd:cd02670    21 AEQQDPEEFFNFITDK----LLMPLLEPKVDIIHGGKK----DQDDDKLVNERLLQIPVPDDDDGGGITLEQCLEQY--- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1602 dvmegdnkykcescdgkFVDAVkryvraevrycsianadrtcLKDAPDNLIFHLKRFEFdlNDFSRRKIYDHFAFPETLD 1681
Cdd:cd02670    90 -----------------FNNSV--------------------FAKAPSCLIICLKRYGK--TEGKAQKMFKKILIPDEID 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160703803 1682 ISPYKFD--------------HLADPEKPREEDVFDLV--GVLVHTGT-CENGHYYSYIRQrpcSSESATPTWVEFNDSE 1744
Cdd:cd02670   131 IPDFVADdpracskcqlecrvCYDDKDFSPTCGKFKLSlcSAVCHRGTsLETGHYVAFVRY---GSYSLTETDNEAYNAQ 207
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 160703803 1745 VTPFDPAEIAERTFGGFTEGEGYNrqikQFSAYMLFYQ 1782
Cdd:cd02670   208 WVFFDDMADRDGVSNGFNIPAARL----LEDPYMLFYQ 241
 
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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